Deciphering post-translational modification codes

被引：136

作者：

Lothrop, Adam P. ^{[1
]}

Torres, Matthew P. ^{[2
]}

Fuchs, Stephen M. ^{[1
]}

机构：

[1] Tufts Univ, Dept Biol, Medford, MA 02155 USA

[2] Georgia Inst Technol, Sch Biol, Atlanta, GA 30332 USA

来源：

FEBS LETTERS | 2013年 / 587卷 / 08期

关键词：

Post-translational modification; Histone; Phosphorylation; Epigenetic; Signaling; Methylation; ANAPHASE-PROMOTING COMPLEX/CYCLOSOME; MASS-SPECTROMETRY; HISTONE H3; HIGH-THROUGHPUT; LIQUID-CHROMATOGRAPHY; PHOSPHORYLATION SITES; PROTEIN MODIFICATIONS; NETWORK MEDICINE; II CTD; PEPTIDE;

D O I：

10.1016/j.febslet.2013.01.047

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Post-translational modifications (PTMs) occur on nearly all proteins. Many domains within proteins are modified on multiple amino acid sidechains by diverse enzymes to create a myriad of possible protein species. How these combinations of PTMs lead to distinct biological outcomes is only beginning to be understood. This manuscript highlights several examples of combinatorial PTMs in proteins, and describes recent technological developments, which are driving our ability to understand how PTM patterns may "code" for biological outcomes. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：1247 / 1257

页数：11

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