(Q40774297)

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Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy

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Europe PubMed Central

PubMed publication ID

23 September 2017

Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy (English)

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Europe PubMed Central

PubMed publication ID

23 September 2017

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Fersht AR

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Europe PubMed Central

PubMed publication ID

23 September 2017

author name string

Bullock AN

1

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Europe PubMed Central

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23 September 2017

Henckel J

2

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Europe PubMed Central

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23 September 2017

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publication date

1 March 2000

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Europe PubMed Central

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23 September 2017

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Europe PubMed Central

PubMed publication ID

23 September 2017

19

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Europe PubMed Central

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23 September 2017

10

1 reference

Europe PubMed Central

PubMed publication ID

23 September 2017

1245-1256

1 reference

Europe PubMed Central

PubMed publication ID

23 September 2017

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

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Mechanisms of p53-mediated apoptosis

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Molecular epidemiology of human cancer risk: gene-environment interactions and p53 mutation spectrum in human lung cancer

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Thermodynamic stability of wild-type and mutant p53 core domain

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The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease

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p53-dependent apoptosis in the absence of transcriptional activation of p53-target genes

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14-3-3Sigma is required to prevent mitotic catastrophe after DNA damage

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In vitro analysis of the dominant negative effect of p53 mutants

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p53 mutants without a functional tetramerisation domain are not oncogenic

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

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Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation

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Folding intermediates of wild-type and mutants of barnase. I. Use of phi-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium

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Human tumor-derived p53 proteins exhibit binding site selectivity and temperature sensitivity for transactivation in a yeast-based assay

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The FHA domain is a modular phosphopeptide recognition motif.

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HSP70 Binding Sites in the Tumor Suppressor Protein p53

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Regulation of mutant p53 temperature-sensitive DNA binding.

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Calculation of protein extinction coefficients from amino acid sequence data

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Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2

1 reference

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Allosteric regulation of the thermostability and DNA binding activity of human p53 by specific interacting proteins. CRC Cell Transformation Group

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Structure and function of the p53 tumor suppressor gene: clues for rational cancer therapeutic strategies

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Mdm2 promotes the rapid degradation of p53

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Induction of apoptosis in HeLa cells by trans-activation-deficient p53

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p53 mutations in human cancers

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Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors

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Regulation of p53 protein function through alterations in protein-folding pathways

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Covalent and noncovalent modifiers of the p53 protein

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Tumor-suppressor p53: implications for tumor development and prognosis

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MOLMOL: a program for display and analysis of macromolecular structures

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p53, the cellular gatekeeper for growth and division

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p53 status and the efficacy of cancer therapy in vivo

1 reference

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p53 protein stability in tumour cells is not determined by mutation but is dependent on Mdm2 binding.

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Flexibility: the key to p53 function?

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

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Local versus nonlocal interactions in protein folding and stability--an experimentalist's point of view

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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability

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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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Determination and analysis of urea and guanidine hydrochloride denaturation curves

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Specific interaction between the p53 cellular tumour antigen and major heat shock proteins

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A model for p53-induced apoptosis

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Temperature sensitivity of human wild-type and mutant p53 proteins expressed in vivo

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From computer simulations to human disease: emerging themes in protein folding

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Correcting temperature-sensitive protein folding defects

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Analysis of p53 mutants for transcriptional activity

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Characterization of structural p53 mutants which show selective defects in apoptosis but not cell cycle arrest

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Reactivation of mutant p53 through interaction of a C-terminal peptide with the core domain.

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The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability

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Identification of a minimal transforming domain of p53: negative dominance through abrogation of sequence-specific DNA binding

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Structural aspects of the p53 protein in relation to gene evolution: a second look.

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Defective protein folding as a basis of human disease

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Distinct residues of human p53 implicated in binding to DNA, simian virus 40 large T antigen, 53BP1, and 53BP2.

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Evolutionary conservation and somatic mutation hotspot maps of p53: correlation with p53 protein structural and functional features.

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Identification of a novel p53 functional domain that is necessary for efficient growth suppression

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The XPB and XPD DNA helicases are components of the p53-mediated apoptosis pathway

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New p53-based anti-cancer therapeutic strategies

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

1 reference

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based on heuristic

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Grabbing phosphoproteins

1 reference

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A temperature-sensitive mutant of human p53.

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10.1038/SJ.ONC.1203434

1 reference

Europe PubMed Central

PubMed publication ID

23 September 2017

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PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

23 September 2017

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