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Targeted Proteomics for Determining Phosphorylation Site-Specific Associations in Cardiovascular Disease
Author(s) -
Stuart J. Cordwell,
Melanie Y. White
Publication year - 2012
Publication title -
circulation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.795
H-Index - 607
eISSN - 1524-4539
pISSN - 0009-7322
DOI - 10.1161/circulationaha.112.136507
Subject(s) - proteomics , phosphorylation , protein function , medicine , function (biology) , bioinformatics , computational biology , biochemistry , chemistry , biology , genetics , gene
Post-translational modifications (PTMs) are chemical or physical changes to proteins that can alter structure/function relationships and thus influence catalysis, cell localization and interactions with other proteins and biomolecules. There are over 200 recognized PTMs, generating a vast scope for altering protein function and increasing the potential for complex regulatory cross-talk between diverse modifications. Protein phosphorylation is of major significance since 30-50% of all cellular proteins may be targeted1,2. Phosphorylation is a transient means of amplifying environmental signals to rapidly alter protein structure, interactions and ultimately, function.

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