期刊
CURRENT OPINION IN CHEMICAL BIOLOGY
卷 58, 期 -, 页码 112-120出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2020.07.012
关键词
Genetic code expansion; Unnatural amino acids; Proximity-triggered crosslinking; Photocrosslinking; Photocaging; Post-translational modifications
资金
- Excellence Initiative CIPSM
- DFG through the SFB1035 program (German Research Foundation DFG) [Sonderforschungsbereich 1035, 201302640]
- Excellence Initiative
- EUMarie Curie COFUND Program
In recent years it has become possible to genetically encode an expanded set of designer amino acids with tailored chemical and physical properties (dubbed unnatural amino acids, UAAs) into proteins in living cells by expanding the genetic code. Together with developments in chemistries that are amenable to and selective within physiological settings, these strategies have started to have a big impact on biological studies, as they enable exciting in cellulo applications. Here we highlight recent advances to covalently stabilize transient protein-protein interactions and capture enzyme substrate complexes in living cells using proximity-triggered and residue-selective photo-induced crosslinking approaches. Furthermore, we describe recent efforts in controlling enzyme activity with photocaged UAAs and in extending their application to a variety of enzymatic scaffolds. In addition, we discuss the site specific incorporation of UAAs mimicking post-translational modifications (PTMs) and approaches to generate natively-linked ubiquitin-protein conjugates to probe the role of PTMs in modulating complex cellular networks.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据