Ubiquitin-Conjugating Enzymes in Cancer [PDF]
Cells, 2021 The ubiquitin-mediated degradation system is responsible for controlling various tumor-promoting processes, including DNA repair, cell cycle arrest, cell proliferation, apoptosis, angiogenesis, migration and invasion, metastasis, and drug resistance. The
Quyen Thu Bui +4 more
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Genome-wide identification and expression analysis of E2 ubiquitin-conjugating enzymes in tomato [PDF]
Scientific Reports, 2017 The ubiquitin-proteasomal degradation mechanism has gained the attention over the past decade. The E2 ubiquitin conjugating enzymes are the crucial part of ubiquitination mechanism and they are believed to hold imperative association for plant ...
Bhaskar Sharma, Tarun Kumar Bhatt
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E2 ubiquitin-conjugating enzymes regulate the deubiquitinating activity of OTUB1. [PDF]
Nat Struct Mol Biol, 2013 OTUB1 is a Lys48-specific deubiquitinating enzyme that forms a complex in vivo with E2 ubiquitin (Ub)-conjugating enzymes including UBC13 and UBCH5.
Wiener R +6 more
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A conserved asparagine has a structural role in ubiquitin-conjugating enzymes. [PDF]
Nat Chem Biol, 2013 It is widely accepted that ubiquitin conjugating enzymes (E2) contain an active site asparagine that serves as an oxyanion hole, thereby stabilizing a negatively charged transition state intermediate and promoting ubiquitin transfer. Using structural and
Berndsen CE +4 more
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The Molecular Basis of Ubiquitin-Conjugating Enzymes (E2s) as a Potential Target for Cancer Therapy. [PDF]
Int J Mol Sci, 2021 Ubiquitin-conjugating enzymes (E2s) are one of the three enzymes required by the ubiquitin-proteasome pathway to connect activated ubiquitin to target proteins via ubiquitin ligases.
Du X, Song H, Shen N, Hua R, Yang G.
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Multi-tiered pairing selectivity between E2 ubiquitin-conjugating enzymes and E3 ligases. [PDF]
J Biol Chem, 2018 Ubiquitination is a prevalent post-translational modification involved in all aspects of cell physiology. It is mediated by an enzymatic cascade and the E2 ubiquitin–conjugating enzymes (UBCs) lie at its heart.
Turek I +3 more
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Creation of a Pluripotent Ubiquitin-Conjugating Enzyme [PDF]
Molecular and Cellular Biology, 2001 We describe the creation of a pluripotent ubiquitin-conjugating enzyme (E2) generated through a single amino acid substitution within the catalytic domain of RAD6 (UBC2). This RAD6 derivative carries out the stress-related function of UBC4 and the cell cycle function of CDC34 while maintaining its own DNA repair function.
Christopher P. Ptak +5 more
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Ubiquitin conjugating enzymes participate in polyglutamine protein aggregation [PDF]
BMC Cell Biology, 2007 Background Protein aggregation is a hallmark of several neurodegenerative diseases including Huntington's disease and Parkinson's disease. Proteins containing long, homopolymeric stretches of glutamine are especially prone to form aggregates. It has long
Caldwell Guy A +7 more
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A Subset of Ubiquitin-Conjugating Enzymes Is Essential for Plant Immunity1[OPEN] [PDF]
Plant Physiology, 2016 Of the three classes of enzymes involved in ubiquitination, ubiquitin-conjugating enzymes (E2) have been often incorrectly considered to play merely an auxiliary role in the process, and few E2 enzymes have been investigated in plants. To reveal the role of E2 in plant innate immunity, we identified and cloned 40 tomato genes encoding ubiquitin E2 ...
Bangjun Zhou +7 more
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E2 superfamily of ubiquitin-conjugating enzymes: constitutively active or activated through phosphorylation in the catalytic cleft. [PDF]
Sci Rep, 2015 Protein phosphorylation is a modification that offers a dynamic and reversible mechanism to regulate the majority of cellular processes. Numerous diseases are associated with aberrant regulation of phosphorylation-induced switches.
Valimberti I +4 more
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