期刊
JOURNAL OF PROTEOMICS
卷 81, 期 -, 页码 15-23出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jprot.2012.09.015
关键词
Multiple-reaction monitoring; Mitochondria; Phosphorylation; Cardioprotection; Quantification; Cardiac biology
资金
- NIH [HL-63901, HL-101228, HHSN268201000035C, F32 HL-099029, AHA-12PRE11610024]
We report the development of a multiple-reaction monitoring (MRM) strategy specifically tailored to the detection and quantification of mitochondrial protein phosphorylation. We recently derived 68 MRM transitions specific to protein modifications in the respiratory chain, voltage-dependent anion channel, and adenine nucleotide translocase. Here, we have now expanded the total number of MRM transitions to 176 to cover proteins from the tricarboxylic acid cycle, pyruvate dehydrogenase complex, and branched-chain alpha-keto acid dehydrogenase complex We utilized the transition set to analyze endogenous protein phosphorylation in human heart, mouse heart, and mouse liver. The data demonstrate the potential utility of the MRM workflow for studying the functional details of mitochondrial phosphorylation signaling. This article is part of a Special Issue entitled: From protein structures to clinical applications. (C) 2012 Elsevier B.V. All rights reserved.
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