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Application of mass spectrometry to study proteomics and interactomics in cystic fibrosis

Academic Article
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Overview

authors

  • Balch, William E.
  • Yates III, John

publication date

  • 2011

journal

  • Methods in Molecular Biology  Journal

abstract

  • The cystic fibrosis transmembrane conductance regulator (CFTR) does not function in isolation, but rather in a complex network of protein-protein interactions that dictate the physiology of a healthy cell and tissue and, when defective, the pathophysiology characteristic of cystic fibrosis (CF) disease. To begin to address the organization and operation of the extensive cystic fibrosis protein network dictated by simultaneous and sequential interactions, it will be necessary to understand the global protein environment (the proteome) in which CFTR functions in the cell and the local network that dictates CFTR folding, trafficking, and function at the cell surface. Emerging mass spectrometry (MS) technologies and methodologies offer an unprecedented opportunity to fully characterize both the proteome and the protein interactions directing normal CFTR function and to define what goes wrong in disease. Below we provide the CF investigator with a general introduction to the capabilities of modern mass spectrometry technologies and methodologies with the goal of inspiring further application of these technologies for development of a basic understanding of the disease and for the identification of novel pathways that may be amenable to therapeutic intervention in the clinic.

subject areas

  • Chromatography, Liquid
  • Cystic Fibrosis
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • Electrophoresis, Gel, Two-Dimensional
  • Humans
  • Metabolic Networks and Pathways
  • Protein Folding
  • Protein Interaction Mapping
  • Protein Transport
  • Proteomics
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Identity

International Standard Serial Number (ISSN)

  • 1940-6029 (Electronic) 1064-3745 (Linking)

Digital Object Identifier (DOI)

  • 10.1007/978-1-61779-120-8_14

PubMed ID

  • 21547736
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Additional Document Info

start page

  • 227

end page

  • 247

volume

  • 742

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