The ubiquitin code.
By D. Komander, M. Rapé. Annual Review of Biochemistry, 2012
3,488 citations recorded by the source corpus.
Subfields: Epidemiology, Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/5b2953bfd8ea399abbd4d0c58a7da91d859914e6
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Epidemiology
In Molecular Biology
- Andriy Kryshtafovych
- Torsten Schwede
- Krzysztof Fidelis
- John Moult
- Yang Zhang
- Bohdan Monastyrskyy
- Maya Topf
- Anna Tramontano
In Oncology
Citations in the corpus
- Proteolysis Targeting Chimeras as Therapeutics and Tools for Biological Discovery (2020, neutral): “These PTMs have a multitude of biological functions that are still being investigated (Komander and Rape, 2012; Yau and Rape, 2016), but the canonical role of K48 polyubiquitin is to signal a protein for destruction via the proteasome (Grice and Nathan, 2016).”
- The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “The attachment of Ub to the substrate requires an enzymatic cascade consisting of E1, E2 and E3.”
- Deubiquitylating enzymes and drug discovery: emerging opportunities (2017, background): “Some DUBs have preferences for monoubiquitylated substrates, whereas others favour specific ubiquitin chain types, chains bearing mixed linkages, or mixed chains containing ubiquitin and UBLs 230, 231 .”
- Deciphering the Molecular Signals of PINK1/Parkin Mitophagy. (2016, background): “Polyubiquitin Chains in Mitophagy Ubiquitin chains of different K linkages trigger various cellular signals (reviewed in [29]).”
- Mechanisms of Selective Autophagy (2016, neutral): “While K48-linked chains are recognized by the proteasome and therefore mediate proteasomal degradation of their substrates, K63-linked chains have also been associated with autophagy [57,58].”
- Abscisic Acid and Abiotic Stress Tolerance in Crop Plants (2016, background): “Ubiquitination can affect proteins in different ways: it can tag proteins for degradation via the proteasome, change their cellular location, and promote or prevent interactions of proteins (Komander and Rape, 2012).”
- The BioGRID database: A comprehensive biomedical resource of curated protein, genetic, and chemical interactions (2020, background): “The conjugation of ubiquitin to substrate proteins controls the stability, localization, and/or function of much if not most of the proteome.(25) The UPS project is based on an exhaustive and continuously updated list of 1,285 human genes and 299 budding yeast genes that encode the E1, E2, and E3 en”