Consejo Nacional de Ciencia y Tecnología, CONACYT: MEYS — NPS I — LO1413, CB-256637
type: Relationship
type: BFO_0000020
type: Entity
type: Thing
type: Grant
type: Continuant
funding vehicle for: Allosteric changes in HDM2 by the ATM phosphomimetic S395D mutation: Implications on HDM2 function

Biochemical Journal
type: Collection
type: Periodical
type: Information Content Entity
type: Document
type: Journal
type: Continuant
type: Entity
publication venue for: Allosteric changes in HDM2 by the ATM phosphomimetic S395D mutation: Implications on HDM2 function
type: Generically Dependent Continuant
type: Thing

Entity
type: Class

Generically Dependent Continuant
type: Class

RDF description of Allosteric changes in HDM2 by the ATM phosphomimetic S395D mutation: Implications on HDM2 function - http://orbis.uaslp.mx/vivo/individual/scopus6056
rights: termsOfUse
date: 2026-08-27T08:17:22
publisher: vivo
type: Document

Article
type: Class

Document
type: Class

249553
type: Relationship
type: BFO_0000020
type: Entity
type: Thing
type: Grant
type: Continuant
funding vehicle for: Allosteric changes in HDM2 by the ATM phosphomimetic S395D mutation: Implications on HDM2 function

Grantová Agentura České Republiky, GA ČR: 19-03796S
type: Relationship
type: BFO_0000020
type: Entity
type: Thing
type: Grant
type: Continuant
funding vehicle for: Allosteric changes in HDM2 by the ATM phosphomimetic S395D mutation: Implications on HDM2 function

00209805
type: Relationship
type: BFO_0000020
type: Entity
type: Thing
type: Grant
type: Continuant
funding vehicle for: Allosteric changes in HDM2 by the ATM phosphomimetic S395D mutation: Implications on HDM2 function

Continuant
type: Class

Allosteric changes in HDM2 by the ATM phosphomimetic S395D mutation: Implications on HDM2 function
related by: authorship_38930
type: Entity
crisid: 6057
most specific type: Article
related by: authorship_38935
chemicalscas: proteasome, 140879-24-9; Ataxia Telangiectasia Mutated Proteins; MDM2 protein, human; Proto-Oncogene Proteins c-mdm2; TP53 protein, human; Tumor Suppressor Protein p53
related by: authorship_38937
type: Thing
volume: 476
most specific type: Document
type: Information Content Entity
origen: scopus
type: Document
has funding vehicle: 249553
related by: authorship_38932
page start: 3401
related by: authorship_38934
type: Continuant
page end: 3411
freetext keyword: ATM protein; proteasome; protein MDM2; protein p53; ATM protein; MDM2 protein, human; protein binding; protein MDM2; protein p53; TP53 protein, human; allosterism; amino acid sequence; amino terminal sequence; Article; carboxy terminal sequence; DNA damage; high performance liquid chromatography; in vitro study; interphase; mass spectrometry; mutation; nonhuman; priority journal; protein degradation; protein function; protein protein interaction; protein structure; ubiquitination; wild type; allosterism; chemistry; genetics; human; metabolism; missense mutation; phosphorylation; protein motif; Allosteric Regulation; Amino Acid Motifs; Ataxia Telangiectasia Mutated Proteins; Humans; Mutation, Missense; Phosphorylation; Protein Binding; Proto-Oncogene Proteins c-mdm2; Tumor Suppressor Protein p53
estado: published
type: Article
related by: authorship_38929
type: Generically Dependent Continuant
has publication venue: Biochemical Journal
e iscopus: 2-s2.0-85075089900
has funding vehicle: 00209805
abstract: Allosteric changes imposed by post-translational modifications regulate and differentiate the functions of proteins with intrinsic disorder regions. HDM2 is a hub protein with a large interactome and with different cellular functions. It is best known for its regulation of the p53 tumour suppressor. Under normal cellular conditions, HDM2 ubiquitinates and degrades p53 by the 26S proteasome but after DNA damage, HDM2 switches from a negative to a positive regulator of p53 by binding to p53 mRNA to promote translation of the p53 mRNA. This change in activity is governed by the ataxia telangiectasia mutated kinase via phosphorylation on serine 395 and is mimicked by the S395D phosphomimetic mutant. Here we have used different approaches to show that this event is accompanied by a specific change in the HDM2 structure that affects the HDM2 interactome, such as the N-termini HDM2–p53 protein–protein interaction. These data will give a better understanding of how HDM2 switches from a negative to a positive regulator of p53 and gain new insights into the control of the HDM2 structure and its interactome under different cellular conditions and help identify interphases as potential targets for new drug developments. © 2019 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND).
issue: 21
accesstype: All Open Access, Hybrid Gold, Green
related by: authorship_38931
related by: authorship_38933
related by: authorship_38936
doi: 10.1042/BCJ20190687
related by: authorship_38938
pmid: 31652301
date time value: article date 6057
has funding vehicle: Consejo Nacional de Ciencia y Tecnología, CONACYT: MEYS — NPS I — LO1413, CB-256637
has funding vehicle: Grantová Agentura České Republiky, GA ČR: 19-03796S

Information Content Entity
type: Class