The emerging complexity of protein ubiquitination.
By D. Komander. Biochemical Society Transactions, 2009
835 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/1417d60f26c4215e068888d6fa170ce242a0c189
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Citations in the corpus
- RCSB Protein Data Bank: Enabling biomedical research and drug discovery (2019, background): “The UPS pathway is regulated by sequential action of three classes of activating enzymes: E1 (two human enzymes), E2 ( 40 human enzymes), and E3 (>600 human enzymes) (Figure 4a).(97) The end result of this combinatorial three-step enzyme cascade is an ubiquitinated substrate that is in turn recogniz”
- HECT and RING finger families of E3 ubiquitin ligases at a glance (2012, background): “Ubiquitylation occurs through the sequential action of three classes of protein: ubiquitinactivating enzymes (E1s), ubiquitinconjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs), and ubiquitin-protein ligases (E3s) (Komander, 2009).”
- Mammalian Krüppel-Like Factors in Health and Diseases (2010, background): “Polyubiquitination provides a signal for the degradation of substrate proteins by the 26S proteasomal complex, whereas monoubiquitination usually alters the activity of a protein (227).”
- Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences (2012, neutral): “…other lysine residues and mono-ubiquitination or multiple mono-ubiquitination are implicated in numerous regulatory processes, such as signal transduction, trafficking, DNA damage response, DNA repair, and autophagy (reviewed in Komander, 2009; Ikeda et al , 2010; and Behrends and Harper, 2011).”
- Systematic and quantitative assessment of the ubiquitin modified proteome (2011, positive): “K63-based signaling is likely occurring constitutively in cells without stimuli that are known to produce acute K63-linked polyubiquitylation of specific proteins (DNA damage, TNFα, and EGF) (Komander, 2009).”