High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
about
Peptides from the amino terminal mdm-2-binding domain of p53, designed from conformational analysis, are selectively cytotoxic to transformed cellsp53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damageCytoplasmic p53 polypeptide is associated with ribosomesTraditional biomolecular structure determination by NMR spectroscopy allows for major errors.Magnetic resonance force microscopyThe rebel angel: mutant p53 as the driving oncogene in breast cancer.Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstromsIdentifying and Visualizing Macromolecular Flexibility in Structural Biologyp53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure-Function Continuum ConceptA role for Groucho tetramerization in transcriptional repressionp53 oligomerization and DNA looping are linked with transcriptional activationThe dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA bindingInteraction of p53 with its consensus DNA-binding siteEvolutionary conservation and somatic mutation hotspot maps of p53: correlation with p53 protein structural and functional features.Development of an accurate classification system of proteins into structured and unstructured regions that uncovers novel structural domains: its application to human transcription factors.Cooperativity dominates the genomic organization of p53-response elements: a mechanistic viewFour p53 DNA-binding domain peptides bind natural p53-response elements and bend the DNA.Structure of lambda CII: implications for recognition of direct-repeat DNA by an unusual tetrameric organizationRetinoid X receptor alpha forms tetramers in solution.Comparison of the protein-protein interfaces in the p53-DNA crystal structures: towards elucidation of the biological interface.Augmented DNA-binding activity of p53 protein encoded by a carboxyl-terminal alternatively spliced mRNA is blocked by p53 protein encoded by the regularly spliced form.Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain.The carboxyl-terminal domain of the p53 protein regulates sequence-specific DNA binding through its nonspecific nucleic acid-binding activityThe role of tetramerization in p53 function.Li-Fraumeni syndrome--a molecular and clinical review.Recognition of RNA by the p53 tumor suppressor protein in the yeast three-hybrid system.The DNA binding activity of p53 displays reaction-diffusion kinetics.Determination of the structures of symmetric protein oligomers from NMR chemical shifts and residual dipolar couplings.Epstein-Barr virus nuclear antigen 3C targets p53 and modulates its transcriptional and apoptotic activities.Stochastic modeling and simulation of the p53-MDM2/MDMX loopUnderstanding the function-structure and function-mutation relationships of p53 tumor suppressor protein by high-resolution missense mutation analysis.p53 mutations and expression in breast carcinoma in situ.Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 ORF50/Rta lytic switch protein functions as a tetramerFunctional Diversification after Gene Duplication: Paralog Specific Regions of Structural Disorder and Phosphorylation in p53, p63, and p73The 1995 Walter Hubert Lecture--molecular epidemiology of human cancer: insights from the mutational analysis of the p53 tumour-suppressor gene.P53 tumour-suppressor gene mutations are mainly localised on exon 7 in human primary and metastatic prostate cancer.p53 mutation is associated with high S-phase fraction in primary fallopian tube adenocarcinoma.Backbone dynamics of the oligomerization domain of p53 determined from 15N NMR relaxation measurements.4-Oxalocrotonate tautomerase, a 41-kDa homohexamer: backbone and side-chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy.Mouse bites dogma: how mouse models are changing our views of how P53 is regulated in vivo.
P2860
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P2860
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
description
1994 nî lūn-bûn
@nan
1994 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
@ast
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
@en
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
@nl
type
label
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
@ast
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
@en
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
@nl
prefLabel
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
@ast
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
@en
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
@nl
P2093
P3181
P356
P1433
P1476
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
@en
P2093
A M Gronenborn
H Sakamoto
J G Omichinski
K Sakaguchi
P304
P3181
P356
10.1126/SCIENCE.8023159
P407
P577
1994-07-15T00:00:00Z