MDM2 interacts with MDMX through their RING finger domains - Wikidata - wikimedia - TriplyDB

MDM2 interacts with MDMX through their RING finger domains

MDM2 interacts with MDMX through their RING finger domains

http://www.wikidata.org/entity/Q28142437

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The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link hematopoiesis and growth control Turning the RING domain protein MdmX into an active ubiquitin-protein ligase Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development.MDM4 (MDMX) overexpression enhances stabilization of stress-induced p53 and promotes apoptosis Effects of MdmX on Mdm2-mediated downregulation of pRB Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3.Caspase-2-mediated cleavage of Mdm2 creates a p53-induced positive feedback loop Identification and characterization of two novel isoforms of Pirh2 ubiquitin ligase that negatively regulate p53 independent of RING finger domains Mdmx enhances p53 ubiquitination by altering the substrate preference of the Mdm2 ubiquitin ligase MDMX regulation of p53 response to ribosomal stress An essential function of the extreme C-terminus of MDM2 can be provided by MDMX MdmX is a substrate for the deubiquitinating enzyme USP2a MDM4 (MDMX) localizes at the mitochondria and facilitates the p53-mediated intrinsic-apoptotic pathway DNA damage-induced phosphorylation of MdmX at serine 367 activates p53 by targeting MdmX for Mdm2-dependent degradation.DNA damage induces MDMX nuclear translocation by p53-dependent and -independent mechanisms.Alterations in gene expression and sensitivity to genotoxic stress following HdmX or Hdm2 knockdown in human tumor cells harboring wild-type p53 Small-molecule inhibitors of the MDM2-p53 protein-protein interaction to reactivate p53 function: a novel approach for cancer therapy Cancer-associated mutations in the MDM2 zinc finger domain disrupt ribosomal protein interaction and attenuate MDM2-induced p53 degradation Use of Immunomatrix Methods to Improve Protein-Protein Interaction Detection Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis Deubiquitinating enzyme regulation of the p53 pathway: A lesson from Otub1 Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation MDM2 promotes SUMO-2/3 modification of p53 to modulate transcriptional activity The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activity MDMX stability is regulated by p53-induced caspase cleavage in NIH3T3 mouse fibroblasts MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination MdmX binding to ARF affects Mdm2 protein stability and p53 transactivation Mutual dependence of MDM2 and MDMX in their functional inactivation of p53 Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein Activation and activities of the p53 tumour suppressor protein A synthetic form of frizzled 8-associated antiproliferative factor enhances p53 stability through USP2a and MDM2 Inhibition of the MDM2 E3 Ligase induces apoptosis and autophagy in wild-type and mutant p53 models of multiple myeloma, and acts synergistically with ABT-737 MDM2 and MDMX: Alone and together in regulation of p53 Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer.MDM4 (MDMX) and its Transcript Variants.Therapeutic considerations for Mdm2: not just a one trick pony Diaryl- and triaryl-pyrrole derivatives: inhibitors of the MDM2-p53 and MDMX-p53 protein-protein interactions†Electronic supplementary information (ESI) available: Experimental details for compound synthesis, analytical data for all compounds and in Aberrant activation of p53 due to loss of MDM2 or MDMX causes early lens dysmorphogenesis.

P2860

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P2860

MDM2 interacts with MDMX through their RING finger domains

http://www.wikidata.org/entity/Q28142437

description

1999 nî lūn-bûn

@nan

1999 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի մարտին հրատարակված գիտական հոդված

@hy

1999年の論文

@ja

1999年論文

@yue

1999年論文

@zh-hant

1999年論文

@zh-hk

1999年論文

@zh-mo

1999年論文

@zh-tw

1999年论文

@wuu

name

MDM2 interacts with MDMX through their RING finger domains

@ast

MDM2 interacts with MDMX through their RING finger domains

@en

MDM2 interacts with MDMX through their RING finger domains

@nl

type

label

MDM2 interacts with MDMX through their RING finger domains

@ast

MDM2 interacts with MDMX through their RING finger domains

@en

MDM2 interacts with MDMX through their RING finger domains

@nl

prefLabel

MDM2 interacts with MDMX through their RING finger domains

@ast

MDM2 interacts with MDMX through their RING finger domains

@en

MDM2 interacts with MDMX through their RING finger domains

@nl

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MDM2 interacts with MDMX through their RING finger domains

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P2093

A Yoshimura

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K Shirouzu

http://www.w3.org/2001/XMLSchema#string

S Ohtsuka

http://www.w3.org/2001/XMLSchema#string

S Tanimura

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P2860

Isolation and identification of the human homolog of a new p53-binding protein, Mdmx

Cloning and characterization of APS, an adaptor molecule containing PH and SH2 domains that is tyrosine phosphorylated upon B-cell receptor stimulation

BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression

ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways

Mdm2 promotes the rapid degradation of p53

Identification of a RING protein that can interact in vivo with the BRCA1 gene product

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

Regulation of p53 stability by Mdm2

p53, the cellular gatekeeper for growth and division

The Ink4a tumor suppressor gene product, p19Arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53

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5-9

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scholarly article

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3705737

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10.1016/S0014-5793(99)00254-9

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1

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13078994

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10218570

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