Physiological functions of the HECT family of ubiquitin ligases

By D. Rotin, Sharad Kumar. Nature reviews. Molecular cell biology, 2009

1,089 citations recorded by the source corpus.

Subfields: Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/089e15975d888ad34cd952fd4fbd425d24b2c054

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In Molecular Biology

1. Wenyi Wei
2. M. B. Metzger
3. Lei Chen
4. V. Hristova
5. A. Weissman
6. T. Meng
7. Ping Wang
8. Lu Deng

Citations in the corpus

• The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “Compared with RING E3s, there are fewer HECT E3s, with only 28 coding genes in the human genome.(59,69) The most obvious feature of HECT E3s is the HECT domain, which forms a transiently covalent bound to Ub through a conserved Cys.”
• HECT and RING finger families of E3 ubiquitin ligases at a glance (2012, background): “family (Rotin and Kumar, 2009), this involves an obligate thioester intermediate with the active-site cysteine of the E3.”
• Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein (2012, background): “WWP2 contains WW domains that are known to interact with PPXY motifs (41, 42).”