MDMX: a novel p53-binding protein with some functional properties of MDM2 - Wikidata - wikimedia - TriplyDB

MDMX: a novel p53-binding protein with some functional properties of MDM2

MDMX: a novel p53-binding protein with some functional properties of MDM2

http://www.wikidata.org/entity/Q24561971

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Turning the RING domain protein MdmX into an active ubiquitin-protein ligase Glioma oncoprotein Bcl2L12 inhibits the p53 tumor suppressor Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development.Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3.14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation Phosphorylation of MDMX mediated by Akt leads to stabilization and induces 14-3-3 binding MDMX regulation of p53 response to ribosomal stress The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex An essential function of the extreme C-terminus of MDM2 can be provided by MDMX 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.Ribosomal protein L23 activates p53 by inhibiting MDM2 function in response to ribosomal perturbation but not to translation inhibition The first 30 years of p53: growing ever more complex Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway 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 Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53 Chemical Variations on the p53 Reactivation Theme Regulation of Mutant p53 Protein Expression Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability Deubiquitinating enzyme regulation of the p53 pathway: A lesson from Otub1 Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX Structure-based Design of High Affinity Peptides Inhibiting the Interaction of p53 with MDM2 and MDMX In Vivo Activation of the p53 Tumor Suppressor Pathway by an Engineered Cyclotide An Ultrahigh Affinity d -Peptide Antagonist Of MDM2 The Double Role of p53 in Cancer and Autoimmunity and Its Potential as Therapeutic Target Molecular Mechanisms of p53 Deregulation in Cancer: An Overview in Multiple Myeloma Role of MDM2 and MDMX in DNA repair Activation and activities of the p53 tumour suppressor protein Regulation of p53 by Mdm2 E3 ligase function is dispensable in embryogenesis and development, but essential in response to DNA damage Probing Difference in Binding Modes of Inhibitors to MDMX by Molecular Dynamics Simulations and Different Free Energy Methods 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 A Novel Interaction between TFII-I and Mdm2 with a Negative Effect on TFII-I Transcriptional Activity 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 A senescence rescue screen identifies BCL6 as an inhibitor of anti-proliferative p19(ARF)-p53 signaling.ATM activates p53 by regulating MDM2 oligomerization and E3 processivity High Mdm4 levels suppress p53 activity and enhance its half-life in acute myeloid leukaemia.

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MDMX: a novel p53-binding protein with some functional properties of MDM2

http://www.wikidata.org/entity/Q24561971

description

1996 nî lūn-bûn

@nan

1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1996 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1996年の論文

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1996年学术文章

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1996年学术文章

@zh-cn

1996年学术文章

@zh-hans

1996年学术文章

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1996年学术文章

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1996年學術文章

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name

MDMX: a novel p53-binding protein with some functional properties of MDM2

@ast

MDMX: a novel p53-binding protein with some functional properties of MDM2

@en

MDMX: a novel p53-binding protein with some functional properties of MDM2

@nl

type

label

MDMX: a novel p53-binding protein with some functional properties of MDM2

@ast

MDMX: a novel p53-binding protein with some functional properties of MDM2

@en

MDMX: a novel p53-binding protein with some functional properties of MDM2

@nl

prefLabel

MDMX: a novel p53-binding protein with some functional properties of MDM2

@ast

MDMX: a novel p53-binding protein with some functional properties of MDM2

@en

MDMX: a novel p53-binding protein with some functional properties of MDM2

@nl

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The EMBO Journal

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MDMX: a novel p53-binding protein with some functional properties of MDM2

@en

P2093

A G Jochemsen

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

A J van der Eb

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

A Shvarts

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G Hateboer

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

M Bazuine

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N Riteco

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P Dekker

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R C van Ham

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T van Laar

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W T Steegenga

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P2860

Wild-type p53 binds to the TATA-binding protein and represses transcription

BS69, a novel adenovirus E1A-associated protein that inhibits E1A transactivation

Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity

Human TAFII31 protein is a transcriptional coactivator of the p53 protein

Regulation of transcription functions of the p53 tumor suppressor by the mdm-2 oncogene

The P-loop--a common motif in ATP- and GTP-binding proteins

Amplification of a gene encoding a p53-associated protein in human sarcomas

The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation

A major segment of the neurofibromatosis type 1 gene: cDNA sequence, genomic structure, and point mutations

p53 mutations in human cancers

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