Breaking the chains: structure and function of the deubiquitinases

By D. Komander, M. J. Clague, S. Urbé. Nature reviews. Molecular cell biology, 2009

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The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “DUBs belong to the family of Cys proteases and cleave the isopeptide bond (the attachment of Ub to lysine) or the peptide bond (the connection of Ub to the Nterminal methionine of the protein) with high specificity.(70,109) Currently, the human genome encodes no less than 100 DUBs (Fig.”
The ubiquitin code. (2012, background): “Indeed to prevent ubiq-uitylation from being constitutively on, modi-ﬁcations are reversed by DUBs.”
Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein (2017, background): “Some host USPs (with a fold similar to the CoV PL) also include one or more Ub-like domain(s), which is/are used to regulate the catalytic activity as well as to interact with partners (Komander et al., 2009; Faesen et al., 2012; Pfoh et al., 2015).”
The Molecular Mechanisms Regulating the KEAP1-NRF2 Pathway (2020, background): “In a variety of cellular signaling contexts, the output of ubiquitin conjugation reactions is fine-tuned by the parallel activity of deubiquitinating enzymes (DUBs) (82).”