Difference: RuthStark (1 vs. 20)

• Name: Ruth Stark
• Email: stark@sci.ccny.cuny.edu
• Company Name: CUNY
• Company URL:

• Country: USA
• Comment:

CUNY Distinguished Professor of Chemistry

The City College of New York

Marshak Science Building MR-1208

Convent Avenue at 138th Street

New York, NY 10031 USA

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2008 (Estimated) Awarded Amount to Date $645,555 Investigator(s) Ruth Stark (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: YESHIVA UNIVERSITY

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163 Investigator(s) Ruth Stark (Principal Investigator) Sponsor CUNY College of Staten Island 2800 Victory Boulevard Staten Island, NY 10314 718/982-2254 NSF Program(s) RESEARCH COORD NETWK IN BIO SC, MOLECULAR BIOPHYSICS Field Application(s) Program Reference Code(s) BIOT,9183,1664,1164 Program Element Code(s) 1664,1164 Abstract

The objective of this RCN project is to establish an interactive community of researchers and students in the area of molecular structure and dynamics of macromolecular assemblies, with a specific focus on the forefront technology of solid-state NMR. This project will foster communication of ideas and allow exposure to off-campus equipment facilities for six research groups at the City University of New York (CUNY), the New York Structural Biology Center, Columbia University, and New York University. The networking will be accomplished through an ongoing seminar series held at participating institutes across New York City; an annual symposium held alternately at the CUNY Graduate Center and at the New York Structural Biology Center; an annual hands-on workshop rotating among different laboratories of the core participants; a communications system for teleconferencing and video conferencing; and an interactive website that will announce the activities described above and allow technical networking among the researchers located at the various sites. These programs will facilitate the ability of both junior and well-established investigators to exchange ideas and results, form collaborations in "real time," and advance the field of solid-state NMR as it applies to biopolymers and macromolecular assemblies. In addition, the seminars and website will reach a broad array of researchers and students who would not otherwise have ready access to state-of-the-art NMR methods and experimental results on the molecular structure of biological solids. These individuals include research counterparts in locations distant from New York City as well as local faculty and students. Importantly, the Research Coordination Network will include a significant population of minority students, who comprise 69% of CUNY's student population.

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• Name: Ruth Stark
• Email: stark@sci.ccny.cuny.edu
• Company Name: CUNY
• Company URL:

• Country: USA
• Comment:

Director, CUNY Institute for Macromolecular Assemblies

CUNY Distinguished Professor of Chemistry

The City College of New York

Marshak Science Building MR-1208

Convent Avenue at 138th Street

New York, NY 10031 USA

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2008 (Estimated) Awarded Amount to Date $645,555 Investigator(s) Ruth Stark (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: YESHIVA UNIVERSITY

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163 Investigator(s) Ruth Stark (Principal Investigator) Sponsor CUNY College of Staten Island 2800 Victory Boulevard Staten Island, NY 10314 718/982-2254 NSF Program(s) RESEARCH COORD NETWK IN BIO SC, MOLECULAR BIOPHYSICS Field Application(s) Program Reference Code(s) BIOT,9183,1664,1164 Program Element Code(s) 1664,1164 Abstract

The objective of this RCN project is to establish an interactive community of researchers and students in the area of molecular structure and dynamics of macromolecular assemblies, with a specific focus on the forefront technology of solid-state NMR. This project will foster communication of ideas and allow exposure to off-campus equipment facilities for six research groups at the City University of New York (CUNY), the New York Structural Biology Center, Columbia University, and New York University. The networking will be accomplished through an ongoing seminar series held at participating institutes across New York City; an annual symposium held alternately at the CUNY Graduate Center and at the New York Structural Biology Center; an annual hands-on workshop rotating among different laboratories of the core participants; a communications system for teleconferencing and video conferencing; and an interactive website that will announce the activities described above and allow technical networking among the researchers located at the various sites. These programs will facilitate the ability of both junior and well-established investigators to exchange ideas and results, form collaborations in "real time," and advance the field of solid-state NMR as it applies to biopolymers and macromolecular assemblies. In addition, the seminars and website will reach a broad array of researchers and students who would not otherwise have ready access to state-of-the-art NMR methods and experimental results on the molecular structure of biological solids. These individuals include research counterparts in locations distant from New York City as well as local faculty and students. Importantly, the Research Coordination Network will include a significant population of minority students, who comprise 69% of CUNY's student population.

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• stark.jpg:
  

• Name: Ruth Stark
• Email: stark@sci.ccny.cuny.edu
• Company Name: CUNY
• Company URL:
• Location: CUNY CCNY Office
• Country: USA
• Comment:

Director, CUNY Institute for Macromolecular Assemblies

CUNY Distinguished Professor of Chemistry

The City College of New York

Marshak Science Building MR-1208

Convent Avenue at 138th Street

New York, NY 10031 USA

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2008 (Estimated) Awarded Amount to Date $645,555 Investigator(s) Ruth Stark (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163 Investigator(s) Ruth Stark (Principal Investigator) Sponsor CUNY College of Staten Island 2800 Victory Boulevard Staten Island, NY 10314 718/982-2254 NSF Program(s) RESEARCH COORD NETWK IN BIO SC, MOLECULAR BIOPHYSICS Field Application(s) Program Reference Code(s) BIOT,9183,1664,1164 Program Element Code(s) 1664,1164 Abstract

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• stark.jpg:
  

• Name: Ruth Stark
• Email: stark@sci.ccny.cuny.edu
• Company Name: CUNY
• Company URL:
• Location: CUNY CCNY Office
• Country: USA
• Comment:

Director, CUNY Institute for Macromolecular Assemblies

CUNY Distinguished Professor of Chemistry

The City College of New York

Marshak Science Building MR-1208

Convent Avenue at 138th Street

New York, NY 10031 USA

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2008 (Estimated) Awarded Amount to Date $645,555 Investigator(s) Ruth Stark (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163 Investigator(s) Ruth Stark (Principal Investigator) Sponsor CUNY College of Staten Island 2800 Victory Boulevard Staten Island, NY 10314 718/982-2254 NSF Program(s) RESEARCH COORD NETWK IN BIO SC, MOLECULAR BIOPHYSICS Field Application(s) Program Reference Code(s) BIOT,9183,1664,1164 Program Element Code(s) 1664,1164 Abstract

• Horizontal size of text edit box:
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• Optionally write protect your home page: (set it to your WikiName)
  • Set ALLOWTOPICCHANGE =

Related topics

• TWikiPreferences has site-level preferences of TWiki.
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• stark.jpg:
  

• Name: Ruth Stark
• Email: stark@sci.ccny.cuny.edu
• Company Name: CUNY
• Company URL:
• Location: CUNY CCNY Office
• Country: USA
• Comment:

Director, CUNY Institute for Macromolecular Assemblies

CUNY Distinguished Professor of Chemistry

The City College of New York

Marshak Science Building MR-1208

Convent Avenue at 138th Street

New York, NY 10031 USA

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2008 (Estimated) Awarded Amount to Date $645,555 Investigator(s) Ruth Stark (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: YESHIVA UNIVERSITY

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163 Investigator(s) Ruth Stark (Principal Investigator) Sponsor CUNY College of Staten Island 2800 Victory Boulevard Staten Island, NY 10314 718/982-2254 NSF Program(s) RESEARCH COORD NETWK IN BIO SC, MOLECULAR BIOPHYSICS Field Application(s) Program Reference Code(s) BIOT,9183,1664,1164 Program Element Code(s) 1664,1164 Abstract

The objective of this RCN project is to establish an interactive community of researchers and students in the area of molecular structure and dynamics of macromolecular assemblies, with a specific focus on the forefront technology of solid-state NMR. This project will foster communication of ideas and allow exposure to off-campus equipment facilities for six research groups at the City University of New York (CUNY), the New York Structural Biology Center, Columbia University, and New York University. The networking will be accomplished through an ongoing seminar series held at participating institutes across New York City; an annual symposium held alternately at the CUNY Graduate Center and at the New York Structural Biology Center; an annual hands-on workshop rotating among different laboratories of the core participants; a communications system for teleconferencing and video conferencing; and an interactive website that will announce the activities described above and allow technical networking among the researchers located at the various sites. These programs will facilitate the ability of both junior and well-established investigators to exchange ideas and results, form collaborations in "real time," and advance the field of solid-state NMR as it applies to biopolymers and macromolecular assemblies. In addition, the seminars and website will reach a broad array of researchers and students who would not otherwise have ready access to state-of-the-art NMR methods and experimental results on the molecular structure of biological solids. These individuals include research counterparts in locations distant from New York City as well as local faculty and students. Importantly, the Research Coordination Network will include a significant population of minority students, who comprise 69% of CUNY's student population.

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• Name: Ruth Stark
• Email: stark@sci.ccny.cuny.edu
• Company Name: CUNY
• Company URL:
• Location: CUNY CCNY Office
• Country: USA
• Comment:

Director, CUNY Institute for Macromolecular Assemblies

CUNY Distinguished Professor of Chemistry

The City College of New York

Marshak Science Building MR-1208

Convent Avenue at 138th Street

New York, NY 10031 USA

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2008 (Estimated) Awarded Amount to Date $645,555 Investigator(s) Ruth Stark (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: YESHIVA UNIVERSITY

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163 Investigator(s) Ruth Stark (Principal Investigator) Sponsor CUNY College of Staten Island 2800 Victory Boulevard Staten Island, NY 10314 718/982-2254 NSF Program(s) RESEARCH COORD NETWK IN BIO SC, MOLECULAR BIOPHYSICS Field Application(s) Program Reference Code(s) BIOT,9183,1664,1164 Program Element Code(s) 1664,1164 Abstract

The objective of this RCN project is to establish an interactive community of researchers and students in the area of molecular structure and dynamics of macromolecular assemblies, with a specific focus on the forefront technology of solid-state NMR. This project will foster communication of ideas and allow exposure to off-campus equipment facilities for six research groups at the City University of New York (CUNY), the New York Structural Biology Center, Columbia University, and New York University. The networking will be accomplished through an ongoing seminar series held at participating institutes across New York City; an annual symposium held alternately at the CUNY Graduate Center and at the New York Structural Biology Center; an annual hands-on workshop rotating among different laboratories of the core participants; a communications system for teleconferencing and video conferencing; and an interactive website that will announce the activities described above and allow technical networking among the researchers located at the various sites. These programs will facilitate the ability of both junior and well-established investigators to exchange ideas and results, form collaborations in "real time," and advance the field of solid-state NMR as it applies to biopolymers and macromolecular assemblies. In addition, the seminars and website will reach a broad array of researchers and students who would not otherwise have ready access to state-of-the-art NMR methods and experimental results on the molecular structure of biological solids. These individuals include research counterparts in locations distant from New York City as well as local faculty and students. Importantly, the Research Coordination Network will include a significant population of minority students, who comprise 69% of CUNY's student population.

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• stark.jpg:
  

• Name: Ruth Stark
• Email: stark@sci.ccny.cuny.edu
• Company Name: CUNY
• Company URL:
• Location: CUNY CCNY Office
• Country: USA
• Comment:

Director, CUNY Institute for Macromolecular Assemblies

CUNY Distinguished Professor of Chemistry

The City College of New York

Marshak Science Building MR-1208

Convent Avenue at 138th Street

New York, NY 10031 USA

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2008 (Estimated) Awarded Amount to Date $645,555

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: YESHIVA UNIVERSITY

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163

The objective of this RCN project is to establish an interactive community of researchers and students in the area of molecular structure and dynamics of macromolecular assemblies, with a specific focus on the forefront technology of solid-state NMR. This project will foster communication of ideas and allow exposure to off-campus equipment facilities for six research groups at the City University of New York (CUNY), the New York Structural Biology Center, Columbia University, and New York University. The networking will be accomplished through an ongoing seminar series held at participating institutes across New York City; an annual symposium held alternately at the CUNY Graduate Center and at the New York Structural Biology Center; an annual hands-on workshop rotating among different laboratories of the core participants; a communications system for teleconferencing and video conferencing; and an interactive website that will announce the activities described above and allow technical networking among the researchers located at the various sites. These programs will facilitate the ability of both junior and well-established investigators to exchange ideas and results, form collaborations in "real time," and advance the field of solid-state NMR as it applies to biopolymers and macromolecular assemblies. In addition, the seminars and website will reach a broad array of researchers and students who would not otherwise have ready access to state-of-the-art NMR methods and experimental results on the molecular structure of biological solids. These individuals include research counterparts in locations distant from New York City as well as local faculty and students. Importantly, the Research Coordination Network will include a significant population of minority students, who comprise 69% of CUNY's student population.

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• stark.jpg:
  

• Name: Ruth Stark

• Company Name: CUNY

• Country: USA
• Comment:

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2008 (Estimated) Awarded Amount to Date $645,555 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: YESHIVA UNIVERSITY

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu (Principal Investigator) Sponsor CUNY College of Staten Island 2800 Victory Boulevard Staten Island, NY 10314 718/982-2254 NSF Program(s) RESEARCH COORD NETWK IN BIO SC, MOLECULAR BIOPHYSICS Field Application(s) Program Reference Code(s) BIOT,9183,1664,1164 Program Element Code(s) 1664,1164 Abstract

The objective of this RCN project is to establish an interactive community of researchers and students in the area of molecular structure and dynamics of macromolecular assemblies, with a specific focus on the forefront technology of solid-state NMR. This project will foster communication of ideas and allow exposure to off-campus equipment facilities for six research groups at the City University of New York (CUNY), the New York Structural Biology Center, Columbia University, and New York University. The networking will be accomplished through an ongoing seminar series held at participating institutes across New York City; an annual symposium held alternately at the CUNY Graduate Center and at the New York Structural Biology Center; an annual hands-on workshop rotating among different laboratories of the core participants; a communications system for teleconferencing and video conferencing; and an interactive website that will announce the activities described above and allow technical networking among the researchers located at the various sites. These programs will facilitate the ability of both junior and well-established investigators to exchange ideas and results, form collaborations in "real time," and advance the field of solid-state NMR as it applies to biopolymers and macromolecular assemblies. In addition, the seminars and website will reach a broad array of researchers and students who would not otherwise have ready access to state-of-the-art NMR methods and experimental results on the molecular structure of biological solids. These individuals include research counterparts in locations distant from New York City as well as local faculty and students. Importantly, the Research Coordination Network will include a significant population of minority students, who comprise 69% of CUNY's student population.

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• stark.jpg:
  

• Name: Ruth Stark
• Email: stark@mail.csi.cuny.edu
• Company Name: CUNY
• Company URL: http://www.chem.csi.cuny.edu/mma; http://www.chem.csi.cuny.edu/resgroup; http://www.chem.csi.cuny.edu/rcn
• Location: CUNYCSIOffice
• Country: USA
• Comment:

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2008 (Estimated) Awarded Amount to Date $645,555 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: YESHIVA UNIVERSITY

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu (Principal Investigator) Sponsor CUNY College of Staten Island 2800 Victory Boulevard Staten Island, NY 10314 718/982-2254 NSF Program(s) RESEARCH COORD NETWK IN BIO SC, MOLECULAR BIOPHYSICS Field Application(s) Program Reference Code(s) BIOT,9183,1664,1164 Program Element Code(s) 1664,1164 Abstract

The objective of this RCN project is to establish an interactive community of researchers and students in the area of molecular structure and dynamics of macromolecular assemblies, with a specific focus on the forefront technology of solid-state NMR. This project will foster communication of ideas and allow exposure to off-campus equipment facilities for six research groups at the City University of New York (CUNY), the New York Structural Biology Center, Columbia University, and New York University. The networking will be accomplished through an ongoing seminar series held at participating institutes across New York City; an annual symposium held alternately at the CUNY Graduate Center and at the New York Structural Biology Center; an annual hands-on workshop rotating among different laboratories of the core participants; a communications system for teleconferencing and video conferencing; and an interactive website that will announce the activities described above and allow technical networking among the researchers located at the various sites. These programs will facilitate the ability of both junior and well-established investigators to exchange ideas and results, form collaborations in "real time," and advance the field of solid-state NMR as it applies to biopolymers and macromolecular assemblies. In addition, the seminars and website will reach a broad array of researchers and students who would not otherwise have ready access to state-of-the-art NMR methods and experimental results on the molecular structure of biological solids. These individuals include research counterparts in locations distant from New York City as well as local faculty and students. Importantly, the Research Coordination Network will include a significant population of minority students, who comprise 69% of CUNY's student population.

Personal Preferences (details in TWikiVariables)

• Horizontal size of text edit box:
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• stark.jpg:
  

• Name: Ruth Stark
• Email: stark@mail.csi.cuny.edu

• Company Name: CUNY
• Company URL: http://www.chem.csi.cuny.edu/mma; http://www.chem.csi.cuny.edu/resgroup; http://www.chem.csi.cuny.edu/rcn
• Location: CUNYCSIOffice
• Country: USA
• Comment:

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2008 (Estimated) Awarded Amount to Date $645,555 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: YESHIVA UNIVERSITY

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu (Principal Investigator) Sponsor CUNY College of Staten Island 2800 Victory Boulevard Staten Island, NY 10314 718/982-2254 NSF Program(s) RESEARCH COORD NETWK IN BIO SC, MOLECULAR BIOPHYSICS Field Application(s) Program Reference Code(s) BIOT,9183,1664,1164 Program Element Code(s) 1664,1164 Abstract

The objective of this RCN project is to establish an interactive community of researchers and students in the area of molecular structure and dynamics of macromolecular assemblies, with a specific focus on the forefront technology of solid-state NMR. This project will foster communication of ideas and allow exposure to off-campus equipment facilities for six research groups at the City University of New York (CUNY), the New York Structural Biology Center, Columbia University, and New York University. The networking will be accomplished through an ongoing seminar series held at participating institutes across New York City; an annual symposium held alternately at the CUNY Graduate Center and at the New York Structural Biology Center; an annual hands-on workshop rotating among different laboratories of the core participants; a communications system for teleconferencing and video conferencing; and an interactive website that will announce the activities described above and allow technical networking among the researchers located at the various sites. These programs will facilitate the ability of both junior and well-established investigators to exchange ideas and results, form collaborations in "real time," and advance the field of solid-state NMR as it applies to biopolymers and macromolecular assemblies. In addition, the seminars and website will reach a broad array of researchers and students who would not otherwise have ready access to state-of-the-art NMR methods and experimental results on the molecular structure of biological solids. These individuals include research counterparts in locations distant from New York City as well as local faculty and students. Importantly, the Research Coordination Network will include a significant population of minority students, who comprise 69% of CUNY's student population.

Personal Preferences (details in TWikiVariables)

• Horizontal size of text edit box:
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• Optionally write protect your home page: (set it to your WikiName)
  • Set ALLOWTOPICCHANGE =

Related topics

• TWikiPreferences has site-level preferences of TWiki.
• WebPreferences has preferences of the TWiki.Main web.
• TWikiUsers has a list of other TWiki users.
• stark.jpg:
  

• Name: Ruth Stark
• Email: stark@mail.csi.cuny.edu

• Company Name: CUNY
• Company URL: http://www.chem.csi.cuny.edu/mma; http://www.chem.csi.cuny.edu/resgroup; http://www.chem.csi.cuny.edu/rcn
• Location: CUNYCSIOffice
• Country: USA
• Comment:

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2008 (Estimated) Awarded Amount to Date $645,555 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: YESHIVA UNIVERSITY

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163

The objective of this RCN project is to establish an interactive community of researchers and students in the area of molecular structure and dynamics of macromolecular assemblies, with a specific focus on the forefront technology of solid-state NMR. This project will foster communication of ideas and allow exposure to off-campus equipment facilities for six research groups at the City University of New York (CUNY), the New York Structural Biology Center, Columbia University, and New York University. The networking will be accomplished through an ongoing seminar series held at participating institutes across New York City; an annual symposium held alternately at the CUNY Graduate Center and at the New York Structural Biology Center; an annual hands-on workshop rotating among different laboratories of the core participants; a communications system for teleconferencing and video conferencing; and an interactive website that will announce the activities described above and allow technical networking among the researchers located at the various sites. These programs will facilitate the ability of both junior and well-established investigators to exchange ideas and results, form collaborations in "real time," and advance the field of solid-state NMR as it applies to biopolymers and macromolecular assemblies. In addition, the seminars and website will reach a broad array of researchers and students who would not otherwise have ready access to state-of-the-art NMR methods and experimental results on the molecular structure of biological solids. These individuals include research counterparts in locations distant from New York City as well as local faculty and students. Importantly, the Research Coordination Network will include a significant population of minority students, who comprise 69% of CUNY's student population.

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• Name: Ruth Stark
• Email: stark@mail.csi.cuny.edu

• Company Name: CUNY
• Company URL: http://www.chem.csi.cuny.edu/mma; http://www.chem.csi.cuny.edu/resgroup; http://www.chem.csi.cuny.edu/rcn
• Location: CUNYCSIOffice
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Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

Grant Number: 5R01DK038389-19 PI Name: STORCH, JUDITH PI Email: storch@aesop.rutgers.edu PI Title: PROFESSOR Project Title: Fatty Acid Transport in the Intestine

Abstract: DESCRIPTION (provided by applicant): Fatty acids (FA) and monoacylglycerol (MG), the hydrolytic products of triacylglycerol (TG), provide a major source of dietary energy. Nevertheless, substantial gaps remain in understanding the basic mechanisms of MG and FA assimilation. These include a molecular level understanding of the individual functions of two highly expressed enterocyte fatty acid-binding proteins (FABP), intestinal FABP and liver FABP. In addition, the mechanisms of differential trafficking of MG and FA added to the apical (AP) vs. basolateral (BL) poles of the enterocyte, where AP lipid is more highly incorporated into TG, and BL lipid into phospholipid, are not understood. In this proposal, we will use an integrated approach to address the cellular and molecular mechanisms that underlie the polarity of intestinal FA and MG transport and metabolism, and the specific roles of the two enterocyte FABPs in FA transport, lipid metabolism, and lipoportein secretion. Further, we will explore the regulation and function of monoacylglycerol lipase (MGL), which we have recently shown to be expressed in rat intestine. The specific aims are 1) To determine the functions of IFABP and LFABP in cellular transport and metabolism of FA and MG: Structure-function studies in model systems, analysis of the apo- and holo-LFABP tertiary structures, and direct protein transfer of wild type and specific FABP mutant forms into cultured Caco-2 enterocytes, will allow us to determine the individual functions of IFABP and LFABP, and the structural basis for these functional properties; 2) To determine the cellular basis for metabolic compartmentation of FA and MG in the enterocyte. Studies in rats, mice null for specific enzymes and transport proteins, and Caco-2 cells, will allow us to examine the role of plasma membrane transporters, intracellular FABPs, and specific intracellular enzymes, in the underlying mechanisms of this metabolic divergence; and 3) To explore the role of intestinal monoacylglycerol lipase, using studies in rodents and cultured cells, MGL is higher in neonatal intestine and declines to lower levels in the adult animal, thus we will examine the mechanisms that underlie changes in MGL expression. The ultimate aim of this research program is to understand how to control the rate and extent of dietray lipid assimilation by modulating specific transport and metabolic processes. Such modulation has important implications for the treatment of obesity, diabetes, and hyperlipidemias.

Thesaurus Terms: fatty acid transport, gastrointestinal absorption /transport, protein structure function cellular polarity, fatty acid binding protein, fatty acid metabolism, glycerol, intracellular transport, lipoprotein lipase, liver metabolism, membrane transport protein, protein isoform, protein transport cell line, laboratory mouse, laboratory rat

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK ASB III NEW BRUNSWICK, NJ 08901 Fiscal Year: 2005 Department: NUTRITIONAL SCIENCES Project Start: 01-MAY-1987 Project End: 30-APR-2008 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: GMA

Grant Number: 5R01AI052733-04 PI Name: CASADEVALL, ARTURO PI Email: casadeva@aecom.yu.edu PI Title: PROFESSOR Project Title: Biology of Fungal Melanin

Abstract: This abstract is not available.

Thesaurus Terms:

There are no thesaurus terms on file for this project.

Institution: YESHIVA UNIVERSITY

1. W 185TH ST NEW YORK, NY 10033

NSF Org MCB Intial Amendment Date February 26, 2003 Latest Amendment Date January 4, 2005 Award Number 0233854 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date March 1, 2003 Expires February 28, 2006 (Estimated) Awarded Amount to Date $299163 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu(Principal Investigator) Sponsor CUNY College of Staten Island 2800 Victory Boulevard Staten Island, NY 10314 718/982-2254 NSF Program(s) RESEARCH COORD NETWK IN BIO SC, MOLECULAR BIOPHYSICS Field Application(s) Program Reference Code(s) BIOT,9183,1664,1164 Program Element Code(s) 1664,1164 Abstract

The objective of this RCN project is to establish an interactive community of researchers and students in the area of molecular structure and dynamics of macromolecular assemblies, with a specific focus on the forefront technology of solid-state NMR. This project will foster communication of ideas and allow exposure to off-campus equipment facilities for six research groups at the City University of New York (CUNY), the New York Structural Biology Center, Columbia University, and New York University. The networking will be accomplished through an ongoing seminar series held at participating institutes across New York City; an annual symposium held alternately at the CUNY Graduate Center and at the New York Structural Biology Center; an annual hands-on workshop rotating among different laboratories of the core participants; a communications system for teleconferencing and video conferencing; and an interactive website that will announce the activities described above and allow technical networking among the researchers located at the various sites. These programs will facilitate the ability of both junior and well-established investigators to exchange ideas and results, form collaborations in "real time," and advance the field of solid-state NMR as it applies to biopolymers and macromolecular assemblies. In addition, the seminars and website will reach a broad array of researchers and students who would not otherwise have ready access to state-of-the-art NMR methods and experimental results on the molecular structure of biological solids. These individuals include research counterparts in locations distant from New York City as well as local faculty and students. Importantly, the Research Coordination Network will include a significant population of minority students, who comprise 69% of CUNY's student population.

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• Name: Ruth Stark
• Email: stark@mail.csi.cuny.edu
• Company Name: CUNY
• Company URL: http://www.chem.csi.cuny.edu/mma; http://www.chem.csi.cuny.edu/resgroup; http://www.chem.csi.cuny.edu/rcn
• Location: CUNYCSIOffice
• Country: USA
• Comment:

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2006 (Estimated) Awarded Amount to Date $508155 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

• Horizontal size of text edit box:
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• Name: Ruth Stark
• Email: stark@mail.csi.cuny.edu
• Company Name: CUNY
• Company URL: http://www.chem.csi.cuny.edu/mma; http://www.chem.csi.cuny.edu/resgroup; http://www.chem.csi.cuny.edu/rcn
• Location: CUNYCSIOffice
• Country: USA
• Comment:

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2006 (Estimated) Awarded Amount to Date $508155 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

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• Name: Ruth Stark
• Email: stark@mail.csi.cuny.edu
• Company Name: CUNY

• Location: CUNYCSIOffice
• Country: USA
• Comment:

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2006 (Estimated) Awarded Amount to Date $508155 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

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• Name: Ruth Stark
• Email: stark@mail.csi.cuny.edu
• Company Name: CUNY
• Company URL: http://www.chem.csi.cuny.edu/mma
• Location: CUNYCSIOffice
• Country: USA
• Comment:

Award Number 0134705 Award Instrument Continuing grant Program Manager Kamal Shukla MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences Start Date February 1, 2002 Expires January 31, 2006 (Estimated) Awarded Amount to Date $508155 Investigator(s) Ruth Stark stark@mail.csi.cuny.edu (Principal Investigator) Sponsor Research Foundation of the City University of New York 230 West 41st Street New York, NY 10036 212/417-8423 NSF Program(s) MOLECULAR BIOPHYSICS, BIOMOLECULAR SYSTEMS Field Application(s) Program Reference Code(s) SMET,BIOT,9251,9232,9183,9178,9109,1164,1145 Program Element Code(s) 1164,1144 Abstract

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

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• Name: Ruth Stark
• Email: stark@mail.csi.cuny.edu
• Company Name: CUNY
• Company URL: http://www.chem.csi.cuny.edu/mma
• Location: CUNYCSIOffice
• Country: USA
• Comment:

The leaf and fruit cuticles of higher plants function principally as barriers, controlling bacterial and fungal attack as well as the diffusion of water and chemicals from the outside environment. Their major chemical constituents are waxes that provide waterproofing and either of two insoluble structural support polymers, cutin (for aerial organs) and suberin (at internal locations and in wound tissue). This project aims to understand how the monomer units of the biopolymers are covalently linked together and to cell-wall polysaccharides, how the mechanical properties of the cuticular surface change in response to stress conditions, and how suberin or related materials are involved in textural hardening of potato tissues. Several biophysical approaches will be taken to these problems. (1) Oligomeric fragments of lime fruit cutin and suberized potato wound periderm will be produced by chemical and enzymatic means, separated chromatographically, and identified by nuclear magnetic resonance (NMR) and mass spectrometry (MS). (2) NMR experiments on solvent-swelled samples will be used to develop and apply methodologies to identify polymer chain structures, cross-links, and cell-wall linkages in lime fruit cutin, potato wound periderm, suberized green cotton, and hardened potato tissues. (3) The impact of abrasion, chilling injury, and foliar delivery of pesticides on cuticular mechanical properties and molecular flexibility will be assessed using rheometry, atomic force microscopy (AFM), and solid-state NMR. (4) The biosynthesis of hard polymeric substances deposited in potato tubers that have 'hard-to-cook syndrome' will be studied using texture analysis and NMR spectroscopy. The overall objectives of this project include understanding how the monomer units of the protective cutin and suberin biopolymers are linked together and to supporting cell-wall matrices, how environmental stresses such as wind abrasion and temperature shock alter the mechanical properties of the cuticular membrane, how fruit cuticles interact with aqueous detergents used in application of agrochemicals, and how suberin or related polyphenols are synthesized during the hardening process that degrades potato texture. Ultimately, this research should have both agricultural and economic impact, aiding in the design of essential crop protection strategies. More broadly, the microstructural and molecular insights developed from this work may assist the development of synthetic waterproofing materials for industrial or cosmetic use. Finally, this project will serve to introduce methods such as solid-state NMR and AFM to the community of plant scientists.

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• Name: Ruth Stark
• Email: stark@mail.csi.cuny.edu
• Company Name: CUNY
• Company URL: http://www.chem.csi.cuny.edu/mma
• Location: CUNYCSIOffice
• Country: USA
• Comment:

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• Name: Ruth Stark
• Email: stark@mail.csi.cuny.edu
• Company Name: CUNY
• Company URL: http://www.chem.csi.cuny.edu/mma
• Location: CUNYCSIOffice
• Country: USA
• Comment:

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