UbiBrowser 2.0: a comprehensive resource for proteome-wide known and predicted ubiquitin ligase/deubiquitinase-substrate interactions in eukaryotic species

(database[TitleAbstract]) AND (Nucleic acids research[Journal]) 2022-02-01

Summary:

As an important post-translational modification, ubiquitination mediates ∼80% of protein degradation in eukaryotes. The degree of protein ubiquitination is tightly determined by the delicate balance between specific ubiquitin ligase (E3)-mediated ubiquitination and deubiquitinase-mediated deubiquitination. In 2017, we developed UbiBrowser 1.0, which is an integrated database for predicted human proteome-wide E3-substrate interactions. Here, to meet the urgent requirement of proteome-wide...

Link:

https://pubmed.ncbi.nlm.nih.gov/34669962/?utm_source=Other&utm_medium=rss&utm_campaign=pubmed-2&utm_content=1VsHRGSo3HX0CgC40wRgBdaScQKv8CRE2sO_GaWJzhPEXTSQfX&fc=20220129230418&ff=20220201092200&v=2.17.5

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📚BioDBS Bibliography » (database[TitleAbstract]) AND (Nucleic acids research[Journal])

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Authors:

Xun Wang, Yang Li, Mengqi He, Xiangren Kong, Peng Jiang, Xi Liu, Lihong Diao, Xinlei Zhang, Honglei Li, Xinping Ling, Simin Xia, Zhongyang Liu, Yuan Liu, Chun-Ping Cui, Yan Wang, Liujun Tang, Lingqiang Zhang, Fuchu He, Dong Li

Date tagged:

02/01/2022, 09:22

Date published:

10/20/2021, 06:00