Hot-spot mutants of p53 core domain evince characteristic local structural changes. - Wikidata - awgldk - TriplyDB

Hot-spot mutants of p53 core domain evince characteristic local structural changes.

Hot-spot mutants of p53 core domain evince characteristic local structural changes.

http://www.wikidata.org/entity/Q35549859

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Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants Two sequence motifs from HIF-1alpha bind to the DNA-binding site of p53.Array-based karyotyping for prognostic assessment in chronic lymphocytic leukemia: performance comparison of Affymetrix 10K2.0, 250K Nsp, and SNP6.0 arrays PDBSite: a database of the 3D structure of protein functional sites Oncogenic Intra-p53 Family Member Interactions in Human Cancers Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations Activation of the p53-p21(Cip1) pathway is required for CDK2 activation and S-phase entry in primary rat hepatocytes Integrating mutation data and structural analysis of the TP53 tumor-suppressor protein.Factors governing loss and rescue of DNA binding upon single and double mutations in the p53 core domain.A fast method for predicting amino acid mutations that lead to unfolding.A stochastic algorithm for global optimization and for best populations: a test case of side chains in proteins.Defining the p53 DNA-binding domain/Bcl-x(L)-binding interface using NMR.The p53 core domain is a molten globule at low pH: functional implications of a partially unfolded structure.Childhood adrenocortical tumours: a review.Powerful workhorses for antimicrobial peptide expression and characterization.p53 Interacts with RNA polymerase II through its core domain and impairs Pol II processivity in vivo.CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90.Proteasomal degradation of p53 by human papillomavirus E6 oncoprotein relies on the structural integrity of p53 core domain.Strategies for manipulating the p53 pathway in the treatment of human cancer.Effects of temperature on the p53-DNA binding interactions and their dynamical behavior: comparing the wild type to the R248Q mutant.P53 mutations in thyroid carcinoma: tidings from an old foe.Core domain interactions in full-length p53 in solution The biological impact of the human master regulator p53 can be altered by mutations that change the spectrum and expression of its target genes.Assessing TP53 status in human tumours to evaluate clinical outcome.Allele-specific p53 mutant reactivation.Transcriptional role of p53 in interferon-mediated antiviral immunity.The client protein p53 adopts a molten globule-like state in the presence of Hsp90.Structural basis for understanding oncogenic p53 mutations and designing rescue drugs.Utilizing NMR to study the structure of growth-inhibitory proteins.Folic acid inhibits COLO-205 colon cancer cell proliferation through activating the FRα/c-SRC/ERK1/2/NFκB/TP53 pathway: in vitro and in vivo studies.Investigating DNA Binding and Conformational Variation in Temperature Sensitive p53 Cancer Mutants Using QM-MM Simulations.Mutant p53: one name, many proteins.Hepatitis B virus X protein represses miRNA-148a to enhance tumorigenesis.Restoration of DNA-binding and growth-suppressive activity of mutant forms of p53 via a PCAF-mediated acetylation pathway p53 alterations in human cancer: more questions than answers.Are interactions with p63 and p73 involved in mutant p53 gain of oncogenic function?Reactivation of mutant p53: molecular mechanisms and therapeutic potential.Rescue of mutants of the tumor suppressor p53 in cancer cells by a designed peptide p53 SUMOylation promotes its nuclear export by facilitating its release from the nuclear export receptor CRM1

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P2860

Hot-spot mutants of p53 core domain evince characteristic local structural changes.

http://www.wikidata.org/entity/Q35549859

description

1999 nî lūn-bûn

@nan

1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի հուլիսին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

Hot-spot mutants of p53 core domain evince characteristic local structural changes.

@ast

Hot-spot mutants of p53 core domain evince characteristic local structural changes.

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type

label

Hot-spot mutants of p53 core domain evince characteristic local structural changes.

@ast

Hot-spot mutants of p53 core domain evince characteristic local structural changes.

@en

prefLabel

Hot-spot mutants of p53 core domain evince characteristic local structural changes.

@ast

Hot-spot mutants of p53 core domain evince characteristic local structural changes.

@en

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PNAS.96.15.8438

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

P1476

Hot-spot mutants of p53 core domain evince characteristic local structural changes

@en

P2093

A R Fersht

http://www.w3.org/2001/XMLSchema#string

B S DeDecker

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M Bycroft

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M R Proctor

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S M Freund

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P2860

Thermodynamic stability of wild-type and mutant p53 core domain

Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

p53 mutations in human cancers

Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels

1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

p53: a transdominant regulator of transcription whose function is ablated by mutations occurring in human cancer.

A proteolytic fragment from the central region of p53 has marked sequence-specific DNA-binding activity when generated from wild-type but not from oncogenic mutant p53 protein.

A mutant p53 that discriminates between p53-responsive genes cannot induce apoptosis

Analysis of the most representative tumour-derived p53 mutants reveals that changes in protein conformation are not correlated with loss of transactivation or inhibition of cell proliferation.

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