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Rho修饰的C3样ADP核糖基转移酶。

Rho-modifying C3-like ADP-ribosyltransferases.

作者信息

Aktories K, Wilde C, Vogelsgesang M

机构信息

Institute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs University Freiburg, Otto-Krayer-Haus, Albertstr. 25, Freiburg, Germany.

出版信息

Rev Physiol Biochem Pharmacol. 2004;152:1-22. doi: 10.1007/s10254-004-0034-4. Epub 2004 Sep 15.

Abstract

C3-like exoenzymes comprise a family of seven bacterial ADP-ribosyltransferases, which selectively modify RhoA, B, and C at asparagine-41. Crystal structures of C3 exoenzymes are available, allowing novel insights into the structure-function relationships of these exoenzymes. Because ADP-ribosylation specifically inhibits the biological functions of the low-molecular mass GTPases, C3 exoenzymes are established pharmacological tools to study the cellular functions of Rho GTPases. Recent studies, however, indicate that the functional consequences of C3-induced ADP-ribosylation are more complex than previously suggested. In the present review the basic properties of C3 exoenzymes are briefly summarized and new findings are reviewed.

摘要

C3样外切酶由七种细菌ADP核糖基转移酶组成的家族,它们选择性地在天冬酰胺-41位点修饰RhoA、B和C。C3外切酶的晶体结构已可得,这使得人们能够对这些外切酶的结构-功能关系有新的认识。由于ADP核糖基化特异性抑制低分子量GTP酶的生物学功能,C3外切酶是研究Rho GTP酶细胞功能的既定药理学工具。然而,最近的研究表明,C3诱导的ADP核糖基化的功能后果比以前认为的更为复杂。在本综述中,简要总结了C3外切酶的基本特性,并对新发现进行了综述。

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