Chemical methods for the proteome-wide identification of posttranslationally modified proteins.

Chemical methods for the proteome-wide identification of posttranslationally modified proteins.
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DOI:
10.1016/j.cbpa.2014.10.020
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发表时间:
2015-02
影响因子:
7.8
通讯作者:
Pratt, Matthew R.
Pratt, Matthew R.
中科院分区:
生物学2区
文献类型:
--
作者:
Chuh, Kelly N.;Pratt, Matthew R.

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数以千计的蛋白质进行翻译后修饰,可以对其功能产生显着影响。传统的生物学方法一直在努力解决某些翻译后修饰的无偏见鉴定中继承的一些挑战。与许多领域的生物发现一样,化学选择性和生物正交反应以及化学探针的发展已经改变了我们选择性标记和富集各种翻译后修饰的能力。总的来说,这些努力正在为绘制蛋白质修饰景观的目标做出重大贡献。
Thousands of proteins are subjected to posttranslational modifications that can have dramatic effects on their functions. Traditional biological methods have struggled to address some of the challenges inherit in the unbiased identification of certain posttranslational modifications. As with many areas of biological discovery, the development of chemoselective and bioorthogonal reactions and chemical probes has transformed our ability to selectively label and enrich a wide variety of posttranslational modifications. Collectively, these efforts are making significant contributions to the goal of mapping the protein modification landscape.
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