HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53. - Wikidata - wikimedia - TriplyDB

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

http://www.wikidata.org/entity/Q36347917

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Regulation of MDM4 (MDMX) function by p76(MDM2): a new facet in the control of p53 activity Turning the RING domain protein MdmX into an active ubiquitin-protein ligase Glioma oncoprotein Bcl2L12 inhibits the p53 tumor suppressor Effects of MdmX on Mdm2-mediated downregulation of pRB 14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53 Phosphorylation of MDMX mediated by Akt leads to stabilization and induces 14-3-3 binding Mdmx enhances p53 ubiquitination by altering the substrate preference of the Mdm2 ubiquitin ligase 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.The first 30 years of p53: growing ever more complex Inhibition of ubiquitin-mediated degradation of MOAP-1 by apoptotic stimuli promotes Bax function in mitochondria Regulation of androgen receptor and histone deacetylase 1 by Mdm2-mediated ubiquitylation 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 Systematic Mutational Analysis of Peptide Inhibition of the p53–MDM2/MDMX Interactions D-peptide inhibitors of the p53–MDM2 interaction for targeted molecular therapy of malignant neoplasms The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme.Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation.The Double Role of p53 in Cancer and Autoimmunity and Its Potential as Therapeutic Target Dysregulation of ubiquitin ligases in cancer Intrinsic ubiquitination activity of PCAF controls the stability of the oncoprotein Hdm2 Iron-dependent regulation of MDM2 influences p53 activity and hepatic carcinogenesis MDM2 and MDMX: Alone and together in regulation of p53 Modes of p53 regulation MDM4 (MDMX) and its Transcript Variants.An observational study on the expression levels of MDM2 and MDMX proteins, and associated effects on P53 in a series of human liposarcomas The role of MDM2 and MDM4 in breast cancer development and prevention.MiR-766 induces p53 accumulation and G2/M arrest by directly targeting MDM4.MDM2/X inhibitors under clinical evaluation: perspectives for the management of hematological malignancies and pediatric cancer.microRNAs and Alu elements in the p53-Mdm2-Mdm4 regulatory network.Growth suppression induced by downregulation of E6-AP expression in human papillomavirus-positive cancer cell lines depends on p53 Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases MDM2 oligomers: antagonizers of the guardian of the genome.Radiosensitization of prostate cancer by priming the wild-type p53-dependent cellular senescence pathway.

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P2860

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

http://www.wikidata.org/entity/Q36347917

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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2003年學術文章

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name

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

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HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

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type

label

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

@ast

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

@en

prefLabel

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

@ast

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

@en

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PNAS.2030930100

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

@en

P2093

Arnd Hengstermann

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Laëtitia K Linares

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Stefan Müller

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P2860

Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein

Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53

TAK1 is a ubiquitin-dependent kinase of MKK and IKK

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5

Mdm2 promotes the rapid degradation of p53

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

Recognition of the polyubiquitin proteolytic signal

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

Structure of a BRCA1-BARD1 heterodimeric RING-RING complex

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12009-12014

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10.1073/PNAS.2030930100

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21

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Aaron Ciechanover

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9081792

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14507994

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protein ubiquitination

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218704

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