Results 51 to 60 of about 381,302 (291)
Phosphorylation of ubiquitin-activating enzyme in cultured cells.
Ubiquitin-activating enzyme, E1, is the first enzyme in the pathway leading to formation of ubiquitin-protein conjugates. E1 exists as two isoforms in human cells which are separable by electrophoresis. These isoforms migrate with apparent molecular sizes of 110 kDa and 117 kDa in SDS/polyacrylamide gels.
J C, Cook, P B, Chock
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Ubiquitin-activating enzyme UBA1 is required for cellular response to DNA damage [PDF]
The cellular DNA damage response (DDR) machinery that maintains genomic integrity and prevents severe pathologies, including cancer, is orchestrated by signaling through protein modifications. Protein ubiquitylation regulates repair of DNA double-strand breaks (DSBs), toxic lesions caused by various metabolic as well as environmental insults such as ...
Pavel Moudry +6 more
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The ubiquitin–proteasome system: A potential target for the MASLD
Metabolic dysfunction-associated steatotic liver disease (MASLD), the most prevalent chronic liver condition globally, lacks adequate and effective therapeutic remedies in clinical practice.
Yue Liu +9 more
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Ubiquitination and the Proteasome as Drug Targets in Trypanosomatid Diseases
The eukaryotic pathogens Trypanosoma brucei, Trypanosoma cruzi and Leishmania are responsible for debilitating diseases that affect millions of people worldwide.
Marie-José Bijlmakers
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The origin and loss of the ubiquitin activating enzyme gene on the mammalian Y chromosome [PDF]
Mammalian sex chromosomes are thought to be descended from a homologous pair of autosomes: a testis-determining allele which defined the Y chromosome arose, recombination between the nascent X and Y chromosomes became restricted and the Y chromosome gradually lost its non-essential genetic functions.
M J, Mitchell +8 more
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P53: Stability from the Ubiquitin–Proteasome System and Specific 26S Proteasome Inhibitors
Protein p53 is degraded by the 26S proteasome, a protein complex that breaks down cellular proteins. Degradation begins with activation of the protein ubiquitin (Ub) by the ubiquitin-activating E1 enzymes, ubiquitin-conjugating E2 enzymes, and ubiquitin ...
Andressa Barban do Patrocinio +2 more
semanticscholar +1 more source
The ubiquitin‐activating enzyme (E1) gene family in Arabidopsis thaliana [PDF]
Conjugation of multiple ubiquitins serves as a committed step in the degradation of a variety of intracellular eukaryotic proteins by the 26S proteasome. Conjugates are formed via a three‐enzyme cascade; the initial step requires ubiquitin‐activating enzyme (E1), which couples ubiquitin activation to ATP hydrolysis.
P M, Hatfield +3 more
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Urm1 (ubiquitin related modifier 1) is a molecular fossil in the class of ubiquitin-like proteins (UBLs). It encompasses characteristics of classical UBLs, such as ubiquitin or SUMO (small ubiquitin-related modifier), but also of bacterial sulfur-carrier
Martin Termathe, Sebastian A. Leidel
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Ubiquitination is an essential process regulating turnover of proteins for basic cellular processes such as the cell cycle and cell death (apoptosis). Ubiquitination is initiated by ubiquitin-activating enzymes (E1), which activate and transfer ubiquitin
Tom V. Lee +7 more
semanticscholar +1 more source
Nuclear localization of the ubiquitin-activating enzyme, E1, is cell-cycle-dependent [PDF]
The mechanisms that regulate ubiquitin-mediated degradation of proteins such as the mitotic cyclins at defined stages of the cell cycle are poorly understood. The initial step in the conjugation of ubiquitin to substrate proteins involves the activation of ubiquitin by the ubiquitin-activating enzyme, E1.
S J, Grenfell +4 more
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