Structural basis of restoring sequence-specific DNA binding and transactivation to mutant p53 by suppressor mutations.

[1]  S. Colowick,et al.  Methods in Enzymology , Vol , 1966 .

[2]  A. Levine,et al.  Post-translational regulation of the 54K cellular tumor antigen in normal and transformed cells , 1981, Molecular and cellular biology.

[3]  P. Mora,et al.  Quantitation of a 55K cellular protein: similar amount and instability in normal and malignant mouse cells , 1982, Molecular and cellular biology.

[4]  M. Oren,et al.  p53 cellular tumor antigen: analysis of mRNA levels in normal adult tissues, embryos, and tumors , 1985, Molecular and cellular biology.

[5]  A. Levine,et al.  Activating mutations for transformation by p53 produce a gene product that forms an hsc70-p53 complex with an altered half-life , 1988, Molecular and cellular biology.

[6]  B. Vogelstein,et al.  Suppression of human colorectal carcinoma cell growth by wild-type p53. , 1990, Science.

[7]  K. Kinzler,et al.  Oncogenic forms of p53 inhibit p53-regulated gene expression , 1992 .

[8]  K. Kinzler,et al.  Definition of a consensus binding site for p53 , 1992, Nature Genetics.

[9]  J. Shay,et al.  A transcriptionally active DNA-binding site for human p53 protein complexes , 1992, Molecular and cellular biology.

[10]  P. Cerutti,et al.  Aflatoxin B1 induces the transversion of G-->T in codon 249 of the p53 tumor suppressor gene in human hepatocytes. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[11]  J. Trent,et al.  WAF1, a potential mediator of p53 tumor suppression , 1993, Cell.

[12]  P. Jeffrey,et al.  Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. , 1994, Science.

[13]  Collaborative Computational,et al.  The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.

[14]  B. Quesnel,et al.  p53 Mutations Are Associated With Resistance to Chemotherapy and Short Survival in Hematologic Malignancies , 1994 .

[15]  G. Lozano,et al.  Characterization of a murine p53SER246 mutant equivalent to the human p53SER249 associated with hepatocellular carcinoma and aflatoxin exposure , 1995, Molecular carcinogenesis.

[16]  C. Prives,et al.  p53: puzzle and paradigm. , 1996, Genes & development.

[17]  Z. Otwinowski,et al.  [20] Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.

[18]  A. Fersht,et al.  Thermodynamic stability of wild-type and mutant p53 core domain. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[19]  A. Levine.  p53, the Cellular Gatekeeper for Growth and Division , 1997, Cell.

[20]  J. Boeke,et al.  Genetic selection of intragenic suppressor mutations that reverse the effect of common p53 cancer mutations , 1998, The EMBO journal.

[21]  K. Kinzler,et al.  Requirement for p53 and p21 to sustain G2 arrest after DNA damage. , 1998, Science.

[22]  R J Read,et al.  Crystallography & NMR system: A new software suite for macromolecular structure determination. , 1998, Acta crystallographica. Section D, Biological crystallography.

[23]  P. May,et al.  Twenty years of p53 research: structural and functional aspects of the p53 protein , 1999, Oncogene.

[24]  M. Hollstein,et al.  p53 and human cancer: the first ten thousand mutations. , 2000, Advances in cancer research.

[25]  A. Fersht,et al.  Mechanism of rescue of common p53 cancer mutations by second‐site suppressor mutations , 2000, The EMBO journal.

[26]  A. Fersht,et al.  Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy , 2000, Oncogene.

[27]  A. Levine,et al.  Surfing the p53 network , 2000, Nature.

[28]  A. Fersht,et al.  Rescuing the function of mutant p53 , 2001, Nature Reviews Cancer.

[29]  Thierry Soussi,et al.  Assessing TP53 status in human tumours to evaluate clinical outcome , 2001, Nature Reviews Cancer.

[30]  R. Marmorstein,et al.  Crystal Structure of the Mouse p53 Core DNA-binding Domain at 2.7 Å Resolution* , 2001, The Journal of Biological Chemistry.

[31]  V S Lamzin,et al.  ARP/wARP and molecular replacement. , 2001, Acta crystallographica. Section D, Biological crystallography.

[32]  Xin Lu,et al.  Live or let die: the cell's response to p53 , 2002, Nature Reviews Cancer.

[33]  W. Delano.  The PyMOL Molecular Graphics System , 2002 .

[34]  N. Tretyakova,et al.  Tobacco smoke carcinogens, DNA damage and p53 mutations in smoking-associated cancers , 2002, Oncogene.

[35]  C. Harris,et al.  The IARC TP53 database: New online mutation analysis and recommendations to users , 2002, Human mutation.

[36]  W. El-Deiry,et al.  Restoring p53-Dependent Tumor Suppression , 2003, Cancer biology & therapy.

[37]  A. Fersht,et al.  Kinetic Instability of p53 Core Domain Mutants , 2003, Journal of Biological Chemistry.

[38]  A. Inga,et al.  Functional mutants of the sequence-specific transcription factor p53 and implications for master genes of diversity , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[39]  M. Oren,et al.  Decision making by p53: life, death and cancer , 2003, Cell Death and Differentiation.

[40]  Fei Long,et al.  REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use. , 2004, Acta crystallographica. Section D, Biological crystallography.

[41]  D. Green,et al.  p53's Believe It or Not: Lessons on Transcription-Independent Death , 2003, Journal of Clinical Immunology.

[42]  Ting Wang,et al.  A global suppressor motif for p53 cancer mutants. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[43]  Kevin Cowtan,et al.  research papers Acta Crystallographica Section D Biological , 2005 .

[44]  A. Fersht,et al.  Structural distortion of p53 by the mutation R249S and its rescue by a designed peptide: implications for "mutant conformation". , 2004, Journal of molecular biology.

[45]  A. Fersht,et al.  Structures of p53 Cancer Mutants and Mechanism of Rescue by Second-site Suppressor Mutations* , 2005, Journal of Biological Chemistry.

[46]  A. Fersht,et al.  Structural basis for understanding oncogenic p53 mutations and designing rescue drugs , 2006, Proceedings of the National Academy of Sciences.

[47]  Ronen Marmorstein,et al.  Structure of the p53 Core Domain Dimer Bound to DNA*♦ , 2006, Journal of Biological Chemistry.

[48]  C. Prives,et al.  Mutational Analysis of the p53 Core Domain L1 Loop* , 2006, Journal of Biological Chemistry.

[49]  B. Vojtesek,et al.  Restoring wild-type conformation and DNA-binding activity of mutant p53 is insufficient for restoration of transcriptional activity. , 2006, Biochemical and biophysical research communications.

[50]  M. Kitayner,et al.  Structural basis of DNA recognition by p53 tetramers. , 2006, Molecular cell.

[51]  Z. Weng,et al.  A Global Map of p53 Transcription-Factor Binding Sites in the Human Genome , 2006, Cell.

[52]  A. Fersht,et al.  Quaternary structures of tumor suppressor p53 and a specific p53–DNA complex , 2007, Proceedings of the National Academy of Sciences.

[53]  Ying Wang,et al.  Structure of the human p53 core domain in the absence of DNA. , 2007, Acta crystallographica. Section D, Biological crystallography.

[54]  M. Olivier,et al.  Impact of mutant p53 functional properties on TP53 mutation patterns and tumor phenotype: lessons from recent developments in the IARC TP53 database , 2007, Human mutation.

[55]  Shunsuke Kato,et al.  The screening of the second‐site suppressor mutations of the common p53 mutants , 2007, International journal of cancer.

[56]  A. Fersht,et al.  Structure–function–rescue: the diverse nature of common p53 cancer mutants , 2007, Oncogene.

[57]  K. Wiman,et al.  Reactivation of mutant p53: molecular mechanisms and therapeutic potential , 2007, Oncogene.

[58]  A. Fersht,et al.  Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain , 2008, Proceedings of the National Academy of Sciences.