Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 17, Issue 1, Pages 12-19Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2012.12.023
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Funding
- National Science Foundation (NSF) Early Faculty CAREER award
- NSF [CBET-091143]
- NIH Innovator grant from the Office of the Director, National Institutes of Health [DP2OD007447]
- Eli Lilly
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1262672] Funding Source: National Science Foundation
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [0941143] Funding Source: National Science Foundation
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Protein methylation is a post-translational modification (PTM) which modulates cellular and biological processes including transcription, RNA processing, protein interactions and protein dynamics. Methylation, catalyzed by highly specific methyltransferase enzymes, occurs on several amino acids including arginine, lysine, histidine and dicarboxylic amino acids like glutamate. Mass spectrometry (MS)-based techniques continue to be the methods of choice for the study of protein PTMs. These approaches are powerful and sensitive tools that have been used to identify, quantify and characterize protein methylation. In addition, metabolic labeling strategies can be coupled to MS detection in order to measure dynamic and differential in vivo protein methylation rates. In this review, different applications of mass spectrometry technologies and methods to study protein methylation are discussed.
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