Difference: ZimeiBu (1 vs. 7)

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• NysbcIntro - your introduction to NYSBC
• NetLiterate - short introduction to the style of this intranet

Personal Preferences

Uncomment preferences variables to activate them (remove the #-sign). Help and details on preferences variables are available in TWikiPreferences.

• Show tool-tip topic info on mouse-over of WikiWord links, on or off:
  • #Set LINKTOOLTIPINFO = off
• Horizontal size of text edit box:
  • #Set EDITBOXWIDTH = 70
• Vertical size of text edit box:
  • #Set EDITBOXHEIGHT = 22
• Style of text edit box. width: 99% for full window width (default), width: auto to disable.
  • #Set EDITBOXSTYLE = width: 99%
• Write protect your home page: (set it to your WikiName)
  • #Set ALLOWTOPICCHANGE = ZimeiBu

Related Topics

• ChangePassword for changing your password
• ChangeEmailAddress for changing your email address
• TWikiUsers has a list of other Intranet users
• UserDocumentationCategory is a list of Intranet user documentation
• UserToolsCategory lists all Intranet user tools

Abstract: DESCRIPTION (provided by applicant): Cystic fibrosis is a devastating, chronic, progressive, and frequently fatal genetic disease that is particularly manifest in the lungs. The major cause is an abnormality in ion transport across cell membranes by the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR is the dominant chloride ion transporter in several epithelial tissues. Two adapter proteins-Na+/H+ exchanger regulator factor (NHERF) and ezrin-regulate the cell surface concentrations of CFTR, organize the macromolecular interactions of CFTR with a network of signaling proteins for efficient transduction, and ultimately control the strength of chloride ion transport. The goal of this research is to determine the molecular mechanisms by which adapter proteins work in coordination to regulate the macromolecular assembly of CFTR. The central hypothesis to be tested is that NHERF is a signal transducer whose specific intra-molecular interactions, which are modulated by ezrin, control the ability of NHERF to assemble CFTR. By studying the architecture, energetics, and dynamics of the formation of CFTR macromolecular complexes assembled by multivalent adapter proteins, this research will provide a quantitative analysis of the molecular mechanisms by which adapter proteins interact to assembly CFTR channels. A molecular understanding of the macromolecular interactions with CFTR is an essential element for developing a therapeutic strategy for the cure of cystic fibrosis.

Public Health Relevance: This Public Health Relevance is not available.

Thesaurus Terms: chloride channel, cystic fibrosis, cytoskeletal protein, molecular assembly /self assembly, protein protein interaction, sodium hydrogen exchanger binding site, biological signal transduction, phosphorylation, protein binding, protein kinase C, stoichiometry, structural biology cell line, low angle X ray diffraction analysis, surface plasmon resonance

Institution: INSTITUTE FOR CANCER RESEARCH

1. Cottman Avenue PHILADELPHIA, PA 191112434

My Links

• NysbcIntro - your introduction to NYSBC
• NetLiterate - short introduction to the style of this intranet

Personal Preferences

Uncomment preferences variables to activate them (remove the #-sign). Help and details on preferences variables are available in TWikiPreferences.

• Show tool-tip topic info on mouse-over of WikiWord links, on or off:
  • #Set LINKTOOLTIPINFO = off
• Horizontal size of text edit box:
  • #Set EDITBOXWIDTH = 70
• Vertical size of text edit box:
  • #Set EDITBOXHEIGHT = 22
• Style of text edit box. width: 99% for full window width (default), width: auto to disable.
  • #Set EDITBOXSTYLE = width: 99%
• Write protect your home page: (set it to your WikiName)
  • #Set ALLOWTOPICCHANGE = ZimeiBu

Related Topics

• ChangePassword for changing your password
• ChangeEmailAddress for changing your email address
• TWikiUsers has a list of other Intranet users
• UserDocumentationCategory is a list of Intranet user documentation
• UserToolsCategory lists all Intranet user tools

Abstract: DESCRIPTION (provided by applicant): Cystic fibrosis is a devastating, chronic, progressive, and frequently fatal genetic disease that is particularly manifest in the lungs. The major cause is an abnormality in ion transport across cell membranes by the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR is the dominant chloride ion transporter in several epithelial tissues. Two adapter proteins-Na+/H+ exchanger regulator factor (NHERF) and ezrin-regulate the cell surface concentrations of CFTR, organize the macromolecular interactions of CFTR with a network of signaling proteins for efficient transduction, and ultimately control the strength of chloride ion transport. The goal of this research is to determine the molecular mechanisms by which adapter proteins work in coordination to regulate the macromolecular assembly of CFTR. The central hypothesis to be tested is that NHERF is a signal transducer whose specific intra-molecular interactions, which are modulated by ezrin, control the ability of NHERF to assemble CFTR. By studying the architecture, energetics, and dynamics of the formation of CFTR macromolecular complexes assembled by multivalent adapter proteins, this research will provide a quantitative analysis of the molecular mechanisms by which adapter proteins interact to assembly CFTR channels. A molecular understanding of the macromolecular interactions with CFTR is an essential element for developing a therapeutic strategy for the cure of cystic fibrosis.

Public Health Relevance: This Public Health Relevance is not available.

Thesaurus Terms: chloride channel, cystic fibrosis, cytoskeletal protein, molecular assembly /self assembly, protein protein interaction, sodium hydrogen exchanger binding site, biological signal transduction, phosphorylation, protein binding, protein kinase C, stoichiometry, structural biology cell line, low angle X ray diffraction analysis, surface plasmon resonance

Institution: INSTITUTE FOR CANCER RESEARCH

1. Cottman Avenue PHILADELPHIA, PA 191112434

My Links

• NysbcIntro - your introduction to NYSBC
• NetLiterate - short introduction to the style of this intranet

Personal Preferences

Uncomment preferences variables to activate them (remove the #-sign). Help and details on preferences variables are available in TWikiPreferences.

• Show tool-tip topic info on mouse-over of WikiWord links, on or off:
  • #Set LINKTOOLTIPINFO = off
• Horizontal size of text edit box:
  • #Set EDITBOXWIDTH = 70
• Vertical size of text edit box:
  • #Set EDITBOXHEIGHT = 22
• Style of text edit box. width: 99% for full window width (default), width: auto to disable.
  • #Set EDITBOXSTYLE = width: 99%
• Write protect your home page: (set it to your WikiName)
  • #Set ALLOWTOPICCHANGE = ZimeiBu

Related Topics

• ChangePassword for changing your password
• ChangeEmailAddress for changing your email address
• TWikiUsers has a list of other Intranet users
• UserDocumentationCategory is a list of Intranet user documentation
• UserToolsCategory lists all Intranet user tools

Abstract: DESCRIPTION (provided by applicant): Cystic fibrosis is a devastating, chronic, progressive, and frequently fatal genetic disease that is particularly manifest in the lungs. The major cause is an abnormality in ion transport across cell membranes by the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR is the dominant chloride ion transporter in several epithelial tissues. Two adapter proteins-Na+/H+ exchanger regulator factor (NHERF) and ezrin-regulate the cell surface concentrations of CFTR, organize the macromolecular interactions of CFTR with a network of signaling proteins for efficient transduction, and ultimately control the strength of chloride ion transport. The goal of this research is to determine the molecular mechanisms by which adapter proteins work in coordination to regulate the macromolecular assembly of CFTR. The central hypothesis to be tested is that NHERF is a signal transducer whose specific intra-molecular interactions, which are modulated by ezrin, control the ability of NHERF to assemble CFTR. By studying the architecture, energetics, and dynamics of the formation of CFTR macromolecular complexes assembled by multivalent adapter proteins, this research will provide a quantitative analysis of the molecular mechanisms by which adapter proteins interact to assembly CFTR channels. A molecular understanding of the macromolecular interactions with CFTR is an essential element for developing a therapeutic strategy for the cure of cystic fibrosis.

Public Health Relevance: This Public Health Relevance is not available.

Thesaurus Terms: chloride channel, cystic fibrosis, cytoskeletal protein, molecular assembly /self assembly, protein protein interaction, sodium hydrogen exchanger binding site, biological signal transduction, phosphorylation, protein binding, protein kinase C, stoichiometry, structural biology cell line, low angle X ray diffraction analysis, surface plasmon resonance

Institution: INSTITUTE FOR CANCER RESEARCH

1. Cottman Avenue PHILADELPHIA, PA 191112434

My Links

• NysbcIntro - your introduction to NYSBC
• NetLiterate - short introduction to the style of this intranet

Personal Preferences

Uncomment preferences variables to activate them (remove the #-sign). Help and details on preferences variables are available in TWikiPreferences.

• Show tool-tip topic info on mouse-over of WikiWord links, on or off:
  • #Set LINKTOOLTIPINFO = off
• Horizontal size of text edit box:
  • #Set EDITBOXWIDTH = 70
• Vertical size of text edit box:
  • #Set EDITBOXHEIGHT = 22
• Style of text edit box. width: 99% for full window width (default), width: auto to disable.
  • #Set EDITBOXSTYLE = width: 99%
• Write protect your home page: (set it to your WikiName)
  • #Set ALLOWTOPICCHANGE = ZimeiBu

Related Topics

• ChangePassword for changing your password
• ChangeEmailAddress for changing your email address
• TWikiUsers has a list of other Intranet users
• UserDocumentationCategory is a list of Intranet user documentation
• UserToolsCategory lists all Intranet user tools

Abstract: DESCRIPTION (provided by applicant): Cystic fibrosis is a devastating, chronic, progressive, and frequently fatal genetic disease that is particularly manifest in the lungs. The major cause is an abnormality in ion transport across cell membranes by the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR is the dominant chloride ion transporter in several epithelial tissues. Two adapter proteins-Na+/H+ exchanger regulator factor (NHERF) and ezrin-regulate the cell surface concentrations of CFTR, organize the macromolecular interactions of CFTR with a network of signaling proteins for efficient transduction, and ultimately control the strength of chloride ion transport. The goal of this research is to determine the molecular mechanisms by which adapter proteins work in coordination to regulate the macromolecular assembly of CFTR. The central hypothesis to be tested is that NHERF is a signal transducer whose specific intra-molecular interactions, which are modulated by ezrin, control the ability of NHERF to assemble CFTR. By studying the architecture, energetics, and dynamics of the formation of CFTR macromolecular complexes assembled by multivalent adapter proteins, this research will provide a quantitative analysis of the molecular mechanisms by which adapter proteins interact to assembly CFTR channels. A molecular understanding of the macromolecular interactions with CFTR is an essential element for developing a therapeutic strategy for the cure of cystic fibrosis.

Public Health Relevance: This Public Health Relevance is not available.

Thesaurus Terms: chloride channel, cystic fibrosis, cytoskeletal protein, molecular assembly /self assembly, protein protein interaction, sodium hydrogen exchanger binding site, biological signal transduction, phosphorylation, protein binding, protein kinase C, stoichiometry, structural biology cell line, low angle X ray diffraction analysis, surface plasmon resonance

Institution: INSTITUTE FOR CANCER RESEARCH

1. Cottman Avenue PHILADELPHIA, PA 191112434

My Links

• NysbcIntro - your introduction to NYSBC
• NetLiterate - short introduction to the style of this intranet

Personal Preferences

Uncomment preferences variables to activate them (remove the #-sign). Help and details on preferences variables are available in TWikiPreferences.

• Show tool-tip topic info on mouse-over of WikiWord links, on or off:
  • #Set LINKTOOLTIPINFO = off
• Horizontal size of text edit box:
  • #Set EDITBOXWIDTH = 70
• Vertical size of text edit box:
  • #Set EDITBOXHEIGHT = 22
• Style of text edit box. width: 99% for full window width (default), width: auto to disable.
  • #Set EDITBOXSTYLE = width: 99%
• Write protect your home page: (set it to your WikiName)
  • #Set ALLOWTOPICCHANGE = ZimeiBu

Related Topics

• ChangePassword for changing your password
• ChangeEmailAddress for changing your email address
• TWikiUsers has a list of other Intranet users
• UserDocumentationCategory is a list of Intranet user documentation
• UserToolsCategory lists all Intranet user tools

My Links

• NysbcIntro - your introduction to NYSBC
• NetLiterate - short introduction to the style of this intranet

Personal Preferences

Uncomment preferences variables to activate them (remove the #-sign). Help and details on preferences variables are available in TWikiPreferences.

• Show tool-tip topic info on mouse-over of WikiWord links, on or off:
  • #Set LINKTOOLTIPINFO = off
• Horizontal size of text edit box:
  • #Set EDITBOXWIDTH = 70
• Vertical size of text edit box:
  • #Set EDITBOXHEIGHT = 22
• Style of text edit box. width: 99% for full window width (default), width: auto to disable.
  • #Set EDITBOXSTYLE = width: 99%
• Write protect your home page: (set it to your WikiName)
  • #Set ALLOWTOPICCHANGE = ZimeiBu

Related Topics

• ChangePassword for changing your password
• ChangeEmailAddress for changing your email address
• TWikiUsers has a list of other Intranet users
• UserDocumentationCategory is a list of Intranet user documentation
• UserToolsCategory lists all Intranet user tools

My Links

• NysbcIntro - your introduction to NYSBC
• NetLiterate - short introduction to the style of this intranet

Personal Preferences

Uncomment preferences variables to activate them (remove the #-sign). Help and details on preferences variables are available in TWikiPreferences.

• Show tool-tip topic info on mouse-over of WikiWord links, on or off:
  • #Set LINKTOOLTIPINFO = off
• Horizontal size of text edit box:
  • #Set EDITBOXWIDTH = 70
• Vertical size of text edit box:
  • #Set EDITBOXHEIGHT = 22
• Style of text edit box. width: 99% for full window width (default), width: auto to disable.
  • #Set EDITBOXSTYLE = width: 99%
• Write protect your home page: (set it to your WikiName)
  • #Set ALLOWTOPICCHANGE = ZimeiBu

Related Topics

• ChangePassword for changing your password
• ChangeEmailAddress for changing your email address
• TWikiUsers has a list of other Intranet users
• UserDocumentationCategory is a list of Intranet user documentation
• UserToolsCategory lists all Intranet user tools