Posttranslational protein modifications
Posttranslational protein modifications
复制标题
DOI:
10.1097/01.ccm.0000191712.96336.51
复制
发表时间:
2005-12-01
影响因子:
8.8
通讯作者:
Jenkins, LW
中科院分区:
文献类型:
--
作者:
Clark, RSB;Bayir, H;Jenkins, LW
There are> 300 different protein posttranslational modifications (PTMs), which include such diverse processes as proteolysis, phosphorylation, lipidation, S-nitrosylation, nitration, oxidation, glycosylation, methylation, adenosine diphosphate (ADP)-ribosylation, acylation (acetylation, isoprenylation, myristoylation), ubiquitination, sumoylation, sulfation, farnesylation, and many, many others (1). PTMs change the size, charge, structure and conformation of proteins. As a result, characteristics of proteins, such as enzyme activity, binding affinity, and protein hydrophobicity, are altered. PTMs cannot only directly change the proteins’ function but also indirectly affect function by leading to cell compartmentalization, sequestration, degradation, elimination, and protein–protein interactions (Fig. 1). Individual proteins can undergo multiple and different PTMs.