Chemical Methods for Encoding and Decoding of Posttranslational Modifications

被引：69

作者：

Chuh, Kelly N. ^{[1
]}

Batt, Anna R. ^{[1
]}

Pratt, Matthew R. ^{[1
,2
]}

机构：

[1] Univ So Calif, Dept Chem, Los Angeles, CA 90089 USA

[2] Univ So Calif, Dept Mol & Computat Biol, Los Angeles, CA 90089 USA

来源：

CELL CHEMICAL BIOLOGY | 2016年 / 23卷 / 01期

基金：

美国国家科学基金会;

关键词：

EXPRESSED PROTEIN LIGATION; GLCNAC-MODIFIED PROTEINS; SOLID-PHASE SYNTHESIS; N-METHYL-LYSINE; UNNATURAL NUCLEOTIDE SPECIFICITY; UBIQUITIN-LIKE MODIFIERS; O-LINKED GLYCOSYLATION; ACTIVITY-BASED PROBES; TYROSINE PHOSPHORYLATION; RECOMBINANT PROTEINS;

D O I：

10.1016/j.chembiol.2015.11.006

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：

A large array of posttranslational modifications can dramatically change the properties of proteins and influence different aspects of their biological function such as enzymatic activity, binding interactions, and proteostasis. Despite the significant knowledge that has been gained about the function of posttranslational modifications using traditional biological techniques, the analysis of the site-specific effects of a particular modification, the identification of the full complement of modified proteins in the proteome, and the detection of new types of modifications remains challenging. Over the years, chemical methods have contributed significantly in both of these areas of research. This review highlights several posttranslational modifications where chemistry-based approaches have made significant contributions to our ability to both prepare homogeneously modified proteins and identify and characterize particular modifications in complex biological settings. As the number and chemical diversity of documented posttranslational modifications continues to rise, we believe that chemical strategies will be essential to advance the field in years to come.

引用

页码：86 / 107

页数：22

共 41 条

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Hirano, Kiriko ;

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