Ubiquitin Ligases: Structure, Function, and Regulation.

By N. Zheng, N. Shabek. Annual Review of Biochemistry, 2017

1,278 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/43ce931c66dd7bedd00a0c1178d30e20f6f3f239

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Citations in the corpus

RCSB Protein Data Bank: Enabling biomedical research and drug discovery (2019, background): “98 An exciting new development in this arena is the prospect of targeting the UPS to proteins of pharmacologic interest.”
The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “For instance, the acetylation of Ub at K6 and K48 inhibits the formation and elongation of Ub chains.(23,24) These characteristics further complicate the Ub codes, including the length of the Ub chain, the degree of mixing and the state of the branch.”
Post-Translational Modifications That Drive Prostate Cancer Progression (2021, background): “While there are only two E1 and 38 E2 enzymes, there are more than 600 human E3 ubiquitin ligases, which are classified according to the protein sequence homology into the largest Really Interesting New Gene (RING) finger family with more than 600 predicted members and the HECT (Homologous to the E6”
Structural insights into Cullin4-RING ubiquitin ligase remodelling by Vpr from simian immunodeficiency viruses (2021, background): “This results in recruitment of restriction factors as non-endogenous neo-substrates, inducing 57 their poly-ubiquitylation and subsequent proteasomal degradation [4-8].”
Modeling the CRL4A ligase complex to predict target protein ubiquitination induced by cereblon-recruiting PROTACs (2022, background): “CRL4A belongs to the Really Interesting New Gene (RING) E3 family, one major E3 family (29, 30).”