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Results showed that although UBE2D1 RNA was significantly upregulated in both lung adenocarcinoma (LUAD) and lung squamous cell carcinoma (LUSC) tissues; its expression was even higher in LUAD tissues than in LUSC. UBE2D1 RNA upregulation was associated with poor survival in LUAD patients, but not in LUSC suggesting it as an independent indicator of unfavorable prognosis in LUAD, but not in LUSC.
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Upregulation of UBE2D1 promoted HCC growth in vitro and in vivo by decreasing the p53 in ubiquitination-dependent pathway. High expression of UBE2D1 was attributed to the recurrent genomic copy number gain, which was associated with high serum IL-6 level of HCC patients.
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March-I undergoes lysine-independent ubiquitination by an as yet unidentified E3 ubiquitin ligase that, together with Ube2D1, regulates March-I expression
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The anaphase-promoting complex/cyclosome C activity in human cells is tuned by the combinatorial use of three E2 ubiquitin-conjugating enzymes, namely UBE2C, UBE2S, and UBE2D.
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Data show that ubiquitin E2 enzymes UBE2D1/2/3 and E3 ligase RNF138 accumulate at DNA-damage sites and act at early resection stages by promoting CtIP protein ubiquitylation and accrual.
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The Asp17 mutation in MDM2 stimulated its discharge of the UBCH5a-ubiquitin thioester adduct.
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The SMURF2:UBCH5 complex is critical in maintaining KRAS protein stability.
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Biochemical characterization of recombinant UBTD1 and UBE2D demonstrated that the two proteins form a stable, stoichiometric complex that can be purified to near homogeneity.
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crystal structure of the dimeric RING domain of rat RNF4 in complex with E2 (UbcH5A) linked by an isopeptide bond to ubiquitin
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These data demonstrate that the ability of ICP0 to interact with cellular E2 ubiquitin-conjugating enzyme UBE2D1 is fundamentally important for its biological functions during HSV-1 infection.
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identify the IDOL-UBE2D complex as an important determinant of LDLR activity, and provide insight into molecular mechanisms underlying the regulation of cholesterol uptake
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This structure reveals an interaction between the ubiquitin surface flanking K11 and residues adjacent to the E2 catalytic cysteine and suggests a possible role for this surface in formation of K11 linkages.
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The authors demonstrate that c-IAP1 and UbcH5 family promote K11-linked polyubiquitination of receptor-interacting protein 1 (RIP1) in vitro and in vivo.
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Whereas UbcH5(A, B and C) is highly efficient in converting IkBa into monoubiquitinated forms, Cdc34 drives ubiquitin (Ub)-Ub conjugation
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conformational changes in CHIP upon binding of Hsp70, Hsp90, and their respective C-terminal EEVD peptides, and in complex with the different E2 ubiquitin-conjugating enzymes UbcH5a and Ubc13
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UbcH5A is up-regulated in the liver of iron-overloaded patients with hereditary hemochromatosis, but in vitro studies failed to show regulation in response to iron loading or chelation. Earlier in vivo mRNA expression data for SFT might be UbcH5A.
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comparison of the regional distribution of SFT/UbcH5A and DMT1 mRNA in the adult brain
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Ro52 has both cytoplasmic and nuclear substrates, and mediates ubiquitination through UBE2D1 in the cytoplasm and through UBE2E1 in the nucleus.
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Catalytically active Ubc5 is required for IRF3 activation by viral infection.
