RING domain E3 ubiquitin ligases.
By R. Deshaies, C. Joazeiro. Annual Review of Biochemistry, 2009
2,688 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/bad3f08c363426e09b0089582deb2cecfa364e86
How researchers see this paper
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In Molecular Biology
- C. Crews
- George M. Burslem
- Wenyi Wei
- D. C. Chan
- C. Lima
- M. B. Metzger
- Lei Chen
- Michael J. Sweredoski
In Oncology
Citations in the corpus
- Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences (2012, neutral): “…from an E2 conjugating enzyme at a cysteine residue within the HECT domain to form a thioester, whereas RING-type ligases act as bridging proteins that bring the ubiquitin-charged E2 in close proximity to the substrate, but are not ubiquitinated themselves (reviewed in Deshaies and Joazeiro, 2009).”
- The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “An E3 can bind directly to the substrate without the assistance of other proteins in catalyzing the ubiquitination of the substrate.(58,59) For example, Mdm2 (murine double minute2)/Hdm2 (HDM2 being the human enzyme) and RNF152 (ring finger protein 152) belong to this class of E3s.”
- HECT and RING finger families of E3 ubiquitin ligases at a glance (2012, background): “The vast majority of E3 ligases belong to the group of really interesting new gene (RING) and RING-related E3s – such as plant homeodomain (PHD) and leukemia associated protein (LAP) finger proteins, and members of the U-box family (Deshaies and Joazeiro, 2009).”
- The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition (2010, background): “Although it is unclear whether automodification represents a general mechanism to regulate SUMO E3 ligases, it is attractive to consider because E3 automodification is a common theme for the regulation of E3 enzymes in the ubiquitin pathwa”
- ncRNA- and Pc2 Methylation-Dependent Gene Relocation between Nuclear Structures Mediates Gene Activation Programs (2011, neutral): “CDCA7L possesses a conserved RING finger domain, a characteristic of RING-class E3 ubiquitin protein ligases (Deshaies and Joazeiro, 2009).”