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Keywords: deubiquitinase
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Biochem J (2022) 479 (10): 1103–1119.
Published: 24 May 2022
... made by ubiquitin ligases that modulates protein abundance, localization, and/or activity. For example, some ubiquitin chains target proteins for degradation, while others function as scaffolds for the assembly of signaling complexes. Deubiquitinases (DUBs) are the proteases that counteract ubiquitin...
Biochem J (2015) 471 (2): 155–165.
Published: 02 October 2015
...Yi Wen; Li Shi; Yiluan Ding; Rong Cui; Wen-tian He; Hong-yu Hu; Naixia Zhang The deubiquitinase ubiquitin-specific protease 28 (Usp28) contains a ubiquitin-binding region (UBR) composed of one ubiquitin-associated domain (UBA) and one ubiquitin-interacting motif (UIM) at its N-terminus...
Includes: Supplementary data
Biochem J (2015) 467 (2): 345–352.
Published: 02 April 2015
... an enzymatic system for the large-scale assembly of Lys 33 chains by combining the HECT (homologous to the E6–AP C-terminus) E3 ligase AREL1 (apoptosis-resistant E3 Ub protein ligase 1) with linkage selective deubiquitinases (DUBs). Moreover, this first characterization of the chain selectivity of AREL1...
Includes: Supplementary data
Biochem J (2015) 465 (1): 1–26.
Published: 12 December 2014
...Johanna Heideker; Ingrid E. Wertz The post-translational modification of proteins with ubiquitin represents a complex signalling system that co-ordinates essential cellular functions, including proteolysis, DNA repair, receptor signalling and cell communication. DUBs (deubiquitinases), the enzymes...