HECT and RING finger families of E3 ubiquitin ligases at a glance
By M. B. Metzger, V. Hristova, A. Weissman. Journal of Cell Science, 2012
637 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/db91218553e339628d94541f5c0c1fbe4383a368
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Citations in the corpus
- Post-Translational Modifications That Drive Prostate Cancer Progression (2021, background): “There are also less common Ring-Between-Ring (RBR) family [125] with 12 members as well as the U-box type E3 ligases, which create an E2 binding surface that resembles a RING finger [126].”
- Insights in Post-Translational Modifications: Ubiquitin and SUMO (2022, background): “The main mechanistical difference is that RING E3s facilitate the direct transfer of ubiquitin from the E2 to the target protein, whilst HECT and RBR E3s contain an active site cysteine that forms a thioester bond with ubiquitin before transferring it to the substrate [7,48,49] (Figure 3).”
- 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.”