Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase
about
The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complexStabilization and activation of p53 by the coactivator protein TAFII31TRIAD1 inhibits MDM2-mediated p53 ubiquitination and degradationTurning the RING domain protein MdmX into an active ubiquitin-protein ligaseThe deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2Critical role for Daxx in regulating Mdm2A novel p53-inducible apoptogenic gene, PRG3, encodes a homologue of the apoptosis-inducing factor (AIF)Caspase-2-mediated cleavage of Mdm2 creates a p53-induced positive feedback loopKaposi's sarcoma-associated herpesvirus viral interferon regulatory factor 4 targets MDM2 to deregulate the p53 tumor suppressor pathwayMdmx enhances p53 ubiquitination by altering the substrate preference of the Mdm2 ubiquitin ligaseEfficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entitiesATM augments nuclear stabilization of DYRK2 by inhibiting MDM2 in the apoptotic response to DNA damageMdmX is a substrate for the deubiquitinating enzyme USP2aNARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF)HECT and RING finger families of E3 ubiquitin ligases at a glanceInvolvement of the DNA repair protein hHR23 in p53 degradationCancer-associated mutations in the MDM2 zinc finger domain disrupt ribosomal protein interaction and attenuate MDM2-induced p53 degradationRegulation of the MDM2-p53 pathway by ribosomal protein L11 involves a post-ubiquitination mechanismResponses of genes involved in cell cycle control to diverse DNA damaging chemicals in human lung adenocarcinoma A549 cells.Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathwayRINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesisClinical utility of anti-p53 auto-antibody: systematic review and focus on colorectal cancerStructure of human MDM2 complexed with RPL11 reveals the molecular basis of p53 activationThe predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradationIn vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation.Transcription factor TAFII250 promotes Mdm2-dependent turnover of p53Evidence for direct interaction between Sprouty and CblThe BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activityThe RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutationOligomerization of the human ARF tumor suppressor and its response to oxidative stressMdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitinationSumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymesA RING finger protein Praja1 regulates Dlx5-dependent transcription through its ubiquitin ligase activity for the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1The ubiquitin-proteasome pathway and proteasome inhibitorsAutoubiquitylation of the V(D)J recombinase protein RAG1Regulation of p53 by Mdm2 E3 ligase function is dispensable in embryogenesis and development, but essential in response to DNA damageEstablishment of a Wheat Cell-Free Synthesized Protein Array Containing 250 Human and Mouse E3 Ubiquitin Ligases to Identify Novel Interaction between E3 Ligases and Substrate ProteinsRegulation of expression of the rat orthologue of mouse double minute 2 (MDM2) by H(2)O(2)-induced oxidative stress in neonatal rat cardiac myocytesHAUSP, a deubiquitinating enzyme for p53, is polyubiquitinated, polyneddylated, and dimerizedEssential role of synoviolin in embryogenesis
P2860
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P2860
Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase
description
2000 nî lūn-bûn
@nan
2000 թուականի Մարտին հրատարակուած գիտական յօդուած
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2000 թվականի մարտին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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Activity of MDM2, a ubiquitin ...... NG finger domain of the ligase
@ast
Activity of MDM2, a ubiquitin ...... NG finger domain of the ligase
@en
Activity of MDM2, a ubiquitin ...... NG finger domain of the ligase
@nl
type
label
Activity of MDM2, a ubiquitin ...... NG finger domain of the ligase
@ast
Activity of MDM2, a ubiquitin ...... NG finger domain of the ligase
@en
Activity of MDM2, a ubiquitin ...... NG finger domain of the ligase
@nl
prefLabel
Activity of MDM2, a ubiquitin ...... NG finger domain of the ligase
@ast
Activity of MDM2, a ubiquitin ...... NG finger domain of the ligase
@en
Activity of MDM2, a ubiquitin ...... NG finger domain of the ligase
@nl
P2860
P3181
P356
P1433
P1476
Activity of MDM2, a ubiquitin ...... NG finger domain of the ligase
@en
P2093
P2860
P2888
P304
P3181
P356
10.1038/SJ.ONC.1203464
P407
P577
2000-03-09T00:00:00Z
P5875
P6179
1029110575