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Proteomic mapping provides powerful insights into functional myelin biology
Author(s) -
Christopher M. Taylor,
Cecilia B. Marta,
Robert Claycomb,
David K. Han,
Matthew N. Rasband,
Timothy Coetzee,
S. E. Pfeiffer
Publication year - 2004
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0400922101
Subject(s) - cytoarchitecture , myelin , proteomics , biology , peptide mapping , proteome , two dimensional gel electrophoresis , computational biology , membrane protein , gel electrophoresis , microbiology and biotechnology , neuroscience , bioinformatics , biochemistry , central nervous system , peptide sequence , membrane , gene
Myelin is a dynamic, functionally active membrane necessary for rapid action potential conduction, axon survival, and cytoarchitecture. The number of debilitating neurological disorders that occur when myelin is disrupted emphasizes its importance. Using high-resolution 2D gel electrophoresis, mass spectrometry, and immunoblotting, we have developed an extensive proteomic map of proteins present in myelin, identifying 98 proteins corresponding to at least 130 of the approximately 200 spots on the map. This proteomic map has been applied to analyses of the localization and function of selected proteins, providing a powerful tool to investigate the diverse functions of myelin.

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