Reactivation of mutant p53: molecular mechanisms and therapeutic potential

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Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound

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Activating mutations in p53 produce a common conformational effect. A monoclonal antibody specific for the mutant form.

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The Rb/E2F pathway and cancer

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Pharmacological Rescue of Mutant p53 Conformation and Function

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Presence of a Potent Transcription Activating Sequence in the p53 Protein

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Differential induction of transcriptionally active p53 following UV or lonizing radiation: Defects in chromosome instability syndromes?

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Inhibiting the p53–MDM2 interaction: an important target for cancer therapy

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ASPP Proteins Specifically Stimulate the Apoptotic Function of p53

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Structure of the p53 Tumor Suppressor Bound to the Ankyrin and SH3 Domains of 53BP2

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A common polymorphism acts as an intragenic modifier of mutant p53 behaviour

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A subset of tumor-derived mutant forms of p53 down-regulate p63 and p73 through a direct interaction with the p53 core domain

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Transcriptional Regulation by p53 through Intrinsic DNA/Chromatin Binding and Site-Directed Cofactor Recruitment

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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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Thermodynamic stability of wild-type and mutant p53 core domain

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The pathological response to DNA damage does not contribute to p53-mediated tumour suppression

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Structural basis for understanding oncogenic p53 mutations and designing rescue drugs

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Cancer gene therapy: fringe or cutting edge?

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Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain

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Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90.

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Inhibitors of the HSP90 Molecular Chaperone: Current Status

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Allosteric activation of latent p53 tetramers

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Pharmacologic activation of p53 elicits Bax-dependent apoptosis in the absence of transcription

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Selenomethionine regulation of p53 by a ref1-dependent redox mechanism

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p53 Contains Large Unstructured Regions in its Native State

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A peptide that binds and stabilizes p53 core domain: Chaperone strategy for rescue of oncogenic mutants

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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.Preprint

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PRIMA-1MET synergizes with cisplatin to induce tumor cell apoptosis

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An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo

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Reactivation of Mutant p53 and Induction of Apoptosis in Human Tumor Cells by Maleimide Analogs

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Physical and Functional Interaction between p53 Mutants and Different Isoforms of p73

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

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Conformational shifts propagate from the oligomerization domain of p53 to its tetrameric DNA binding domain and restore DNA binding to select p53 mutants.

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Treatment of Terminal Peritoneal Carcinomatosis by a Transducible p53-Activating Peptide

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p53 Linear Diffusion along DNA Requires Its C Terminus

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Structure, Function, and Aggregation of the Zinc-Free Form of the p53 DNA Binding Domain

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Activation of the cryptic DNA binding function of mutant forms of p53

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p53 gene mutation: software and database

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Characterization of the p53-rescue drug CP-31398 in vitro and in living cells

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Temporal dissection of p53 function in vitro and in vivo

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Structures of p53 Cancer Mutants and Mechanism of Rescue by Second-site Suppressor Mutations

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Inhibition of MDM2 by hsp90 Contributes to Mutant p53 Stabilization

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Crystal Structure of a Superstable Mutant of Human p53 Core Domain

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Solution structure of p53 core domain: Structural basis for its instability

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Mutant p53-dependent growth suppression distinguishes PRIMA-1 from known anticancer drugs: a statistical analysis of information in the National Cancer Institute database

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