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Quantitative proteomic research and integrative analysis of endogenous S-nitrosated proteins in diab
  • 所属机构名称：中国科学院生物物理研究所
  • 会议名称：Systems Biology: Networks. Cold Spring Harbor Laboratory.
  • 成果类型：会议
  • 相关项目：一氧化氮对SUMO修饰调控的分子机制
作者： 陈畅|
同会议论文项目
一氧化氮对SUMO修饰调控的分子机制
期刊论文 17 会议论文 6
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Protein S-nitros(yl)ation in nuclear protein export regulation.
Repression of Classical Nuclear Export by S-Nitrosylation of CRM1
The redox-based post-translational modification of proteins: S-nitros(yl)ation as an example.
A novel crosstalk between S-nitrosation, ubiquitination, and sumoylation: NO regulates sumoylation t
“S-nitrosation and nuclear export”.