The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo.
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Identification of a second Nutlin-3 responsive interaction site in the N-terminal domain of MDM2 using hydrogen/deuterium exchange mass spectrometryRFWD3-Mdm2 ubiquitin ligase complex positively regulates p53 stability in response to DNA damageRibosomal protein S27-like and S27 interplay with p53-MDM2 axis as a target, a substrate and a regulatorRegulation of Mutant p53 Protein ExpressionTranscription factor TAFII250 promotes Mdm2-dependent turnover of p53The proline repeat domain of p53 binds directly to the transcriptional coactivator p300 and allosterically controls DNA-dependent acetylation of p53.DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing.A novel p53 phosphorylation site within the MDM2 ubiquitination signal: I. phosphorylation at SER269 in vivo is linked to inactivation of p53 function.SCH529074, a small molecule activator of mutant p53, which binds p53 DNA binding domain (DBD), restores growth-suppressive function to mutant p53 and interrupts HDM2-mediated ubiquitination of wild type p53Insulin receptor tyrosine kinase substrate enhances low levels of MDM2-mediated p53 ubiquitination.Molecular basis of Bcl-X(L)-p53 interaction: insights from molecular dynamics simulations.Proteasomal degradation of p53 by human papillomavirus E6 oncoprotein relies on the structural integrity of p53 core domain.A novel p53 phosphorylation site within the MDM2 ubiquitination signal: II. a model in which phosphorylation at SER269 induces a mutant conformation to p53The central region of HDM2 provides a second binding site for p53.Binding of Translationally Controlled Tumour Protein to the N-terminal domain of HDM2 is inhibited by nutlin-3.Making sense of ubiquitin ligases that regulate p53.Molecular mechanism of mutant p53 stabilization: the role of HSP70 and MDM2.Stabilization of p53 by CP-31398 inhibits ubiquitination without altering phosphorylation at serine 15 or 20 or MDM2 binding.Inhibition of p53 DNA binding function by the MDM2 protein acidic domain.Critical contribution of the MDM2 acidic domain to p53 ubiquitination.Targeting the p53-MDM2 interaction to treat cancer.It Takes 15 to Tango: Making Sense of the Many Ubiquitin Ligases of p53.The Roles of MDM2 and MDMX Phosphorylation in Stress Signaling to p53.The functional domains in p53 family proteins exhibit both common and distinct properties.Protein methylation: a new mechanism of p53 tumor suppressor regulation.Functional characterization of p53 pathway components in the ancient metazoan Trichoplax adhaerensDual function of MDM2 and MDMX toward the tumor suppressors p53 and RB.p53-based cancer therapyThe relevance of protein-protein interactions for p53 function: the CPE contribution.Inhibitors of MDM2 and MDMX: a structural perspective.The p53 isoforms are differentially modified by Mdm2.MDM2 protein-mediated ubiquitination of numb protein: identification of a second physiological substrate of MDM2 that employs a dual-site docking mechanismCritical role for a central part of Mdm2 in the ubiquitylation of p53.A function for the RING finger domain in the allosteric control of MDM2 conformation and activity.Ubiquitination and degradation of mutant p53.The MDM2 ubiquitination signal in the DNA-binding domain of p53 forms a docking site for calcium calmodulin kinase superfamily members.Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation.Destabilizing missense mutations in the tumour suppressor protein p53 enhance its ubiquitination in vitro and in vivo.Controlled access of p53 to the nucleus regulates its proteasomal degradation by MDM2.Allosteric effects mediate CHK2 phosphorylation of the p53 transactivation domain.
P2860
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P2860
The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
The conformationally flexible ...... ubiquitination of p53 in vivo.
@en
The conformationally flexible ...... ubiquitination of p53 in vivo.
@nl
type
label
The conformationally flexible ...... ubiquitination of p53 in vivo.
@en
The conformationally flexible ...... ubiquitination of p53 in vivo.
@nl
prefLabel
The conformationally flexible ...... ubiquitination of p53 in vivo.
@en
The conformationally flexible ...... ubiquitination of p53 in vivo.
@nl
P2093
P2860
P356
P1476
The conformationally flexible ...... ubiquitination of p53 in vivo.
@en
P2093
Amanda J Smith
David Dornan
Harumi Shimizu
Kathryn L Ball
Lindsay R Burch
Maura Wallace
Ted R Hupp
P2860
P304
28446-28458
P356
10.1074/JBC.M202296200
P407
P577
2002-03-29T00:00:00Z