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化学方法用于翻译后修饰的编码和解码。

Chemical Methods for Encoding and Decoding of Posttranslational Modifications.

机构信息

Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.

Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA; Department of Molecular and Computational Biology, University of Southern California, Los Angeles, CA 90089, USA.

出版信息

Cell Chem Biol. 2016 Jan 21;23(1):86-107. doi: 10.1016/j.chembiol.2015.11.006.

DOI:10.1016/j.chembiol.2015.11.006
PMID:26933738
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4779183/
Abstract

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.

摘要

大量的翻译后修饰可以显著改变蛋白质的性质,并影响其生物学功能的不同方面,如酶活性、结合相互作用和蛋白质稳态。尽管使用传统的生物学技术已经获得了关于翻译后修饰功能的大量知识,但特定修饰的特异性分析、蛋白质组中完整修饰蛋白的鉴定以及新类型修饰的检测仍然具有挑战性。多年来,化学方法在这两个研究领域都做出了重要贡献。这篇综述重点介绍了几种翻译后修饰,其中基于化学的方法为我们在复杂的生物环境中制备均一修饰的蛋白质以及鉴定和表征特定修饰做出了重要贡献。随着有文献记载的翻译后修饰数量和化学多样性的不断增加,我们相信化学策略对于未来几年的领域发展将是必不可少的。

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本文引用的文献

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O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease.O-连接的N-乙酰葡糖胺修饰可阻止与帕金森病相关的蛋白质α-突触核蛋白的聚集和毒性。
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