Cancer-associated p53 tetramerization domain mutants: quantitative analysis reveals a low threshold for tumor suppressor inactivation

Cancer-associated p53 tetramerization domain mutants: quantitative analysis reveals a low threshold for tumor suppressor inactivation

Item
http://www.wikidata.org/entity/Q34452519
Oligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation.Mutant TP53 posttranslational modifications: challenges and opportunities.Structure-based predictions broadly link transcription factor mutations to gene expression changes in cancers.Fuse binding protein antagonizes the transcription activity of tumor suppressor protein p53.Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiationGenomic profiling of multiple sequentially acquired tumor metastatic sites from an "exceptional responder" lung adenocarcinoma patient reveals extensive genomic heterogeneity and novel somatic variants driving treatment responseTP53 mutations in human cancer: database reassessment and prospects for the next decade.Further evidence for pathogenicity of the TP53 tetramerization domain mutation p.Arg342Pro in Li-Fraumeni syndrome.Transcriptional Regulation by Wild-Type and Cancer-Related Mutant Forms of p53.Effects of biomineralization peptide topology on the structure and catalytic activity of Pd nanomaterials.C-terminal region of human p53 attenuates buffalo p53 N-terminal-specific transactivation of p21 promoter by modulating tetramerization of the protein.Insights into the Effect of the G245S Single Point Mutation on the Structure of p53 and the Binding of the Protein to DNA.The curcumin analog HO-3867 selectively kills cancer cells by converting mutant p53 protein to transcriptionally active wildtype p53.Heterochiral Jun and Fos bZIP peptides form a coiled-coil heterodimer that is competent for DNA binding.Wild-type and cancer-related p53 proteins are preferentially degraded by MDM2 as dimers rather than tetramers.
P2860

Cancer-associated p53 tetramerization domain mutants: quantitative analysis reveals a low threshold for tumor suppressor inactivation

Item
http://www.wikidata.org/entity/Q34452519
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Cancer-associated p53 tetramer ...... tumor suppressor inactivation
@ast
Cancer-associated p53 tetramer ...... tumor suppressor inactivation
@en
Cancer-associated p53 tetramer ...... tumor suppressor inactivation
@nl
type
label
Cancer-associated p53 tetramer ...... tumor suppressor inactivation
@ast
Cancer-associated p53 tetramer ...... tumor suppressor inactivation
@en
Cancer-associated p53 tetramer ...... tumor suppressor inactivation
@nl
prefLabel
Cancer-associated p53 tetramer ...... tumor suppressor inactivation
@ast
Cancer-associated p53 tetramer ...... tumor suppressor inactivation
@en
Cancer-associated p53 tetramer ...... tumor suppressor inactivation
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P932
P356
P1433
P1476
Cancer-associated p53 tetramer ...... tumor suppressor inactivation
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P932