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Multiple Reaction Monitoring to Identify Site-Specific Troponin I Phosphorylated Residues in the Failing Human Heart
Author(s) -
Pingbo Zhang,
Jonathan A. Kirk,
Weihua Ji,
Cristobal G. dos Remedios,
David A. Kass,
Jennifer E. Van Eyk,
Anne M. Murphy
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.112.096388
Subject(s) - phosphorylation , heart failure , troponin i , troponin , medicine , kinase , cardiology , protein phosphorylation , heart transplantation , protein kinase a , biochemistry , chemistry , myocardial infarction
Human cardiac troponin I is known to be phosphorylated at multiple amino acid residues by several kinases. Advances in mass spectrometry allow sensitive detection of known and novel phosphorylation sites and measurement of the level of phosphorylation simultaneously at each site in myocardial samples.

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