Three-dimensional structures of H-ras p21 mutants: Molecular basis for their inability to function as signal switch molecules

[1]  S H Kim,et al.  Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. , 1992, Science.

[2]  W. Kabsch,et al.  Refined crystal structure of the triphosphate conformation of H‐ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. , 1990, The EMBO journal.

[3]  A. Wittinghofer,et al.  Inhibition of GTPase activating protein stimulation of Ras-p21 GTPase by the Krev-1 gene product. , 1990, Science.

[4]  R. Goody,et al.  Kinetics of interaction of nucleotides with nucleotide-free H-ras p21. , 1990, Biochemistry.

[5]  Steven C. Almo,et al.  Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis , 1990, Nature.

[6]  J. Eccleston,et al.  Hydrolysis of GTP by p21NRAS, the NRAS protooncogene product, is accompanied by a conformational change in the wild-type protein: use of a single fluorescent probe at the catalytic site. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[7]  M. Moran,et al.  Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases , 1990, Nature.

[8]  I. Schlichting,et al.  Proton NMR studies of transforming and nontransforming H-ras p21 mutants. , 1990, Biochemistry.

[9]  T. Fleming,et al.  PDGF induction of tyrosine phosphorylation of GTPase activating protein , 1989, Nature.

[10]  E. Jacquet,et al.  Substitution of Val20 by Gly in elongation factor Tu. Effects on the interaction with elongation factors Ts, aminoacyl-tRNA and ribosomes. , 1989, European journal of biochemistry.

[11]  E. E. Gresch Genetic Alterations During Colorectal-Tumor Development , 1989 .

[12]  I. Schlichting,et al.  Biochemical and crystallographic characterization of a complex of c-Ha-ras p21 and caged GTP with flash photolysis. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[13]  W. Kabsch,et al.  Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation , 1989, Nature.

[14]  J. L. Bos,et al.  ras oncogenes in human cancer: a review. , 1989, Cancer research.

[15]  I. Schlichting,et al.  C-terminal truncation of p21H preserves crucial kinetic and structural properties. , 1989, The Journal of biological chemistry.

[16]  S. Kim,et al.  Structure of ras proteins. , 1989, Science.

[17]  R. Goody,et al.  The mechanism of guanosine nucleotide hydrolysis by p21 c-Ha-ras. The stereochemical course of the GTPase reaction. , 1989, The Journal of biological chemistry.

[18]  E. Pai,et al.  Crystallization and preliminary X-ray analysis of the human c-H-ras-oncogene product p21 complexed with GTP analogues. , 1989, Journal of molecular biology.

[19]  Frank McCormick,et al.  ras GTPase activating protein: Signal transmitter and signal terminator , 1989, Cell.

[20]  G. A. Martin,et al.  Molecular cloning of two types of GAP complementary DNA from human placenta. , 1988, Science.

[21]  Wolfgang Kabsch,et al.  Evaluation of Single-Crystal X-ray Diffraction Data from a Position-Sensitive Detector , 1988 .

[22]  Irving S. Sigal,et al.  Cloning of bovine GAP and its interaction with oncogenic ras p21 , 1988, Nature.

[23]  R. Goody,et al.  Biochemical properties of Ha-ras encoded p21 mutants and mechanism of the autophosphorylation reaction. , 1988, The Journal of biological chemistry.

[24]  J B Gibbs,et al.  Purification of ras GTPase activating protein from bovine brain. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[25]  G. Cooper,et al.  Relationship among guanine nucleotide exchange, GTP hydrolysis, and transforming potential of mutated ras proteins , 1988, Molecular and cellular biology.

[26]  D. Lowy,et al.  Guanosine triphosphatase activating protein (GAP) interacts with the p21 ras effector binding domain. , 1988, Science.

[27]  C. Marshall,et al.  The cytoplasmic protein GAP is implicated as the target for regulation by the ras gene product , 1988, Nature.

[28]  Wolfgang Kabsch,et al.  Automatic indexing of rotation diffraction patterns , 1988 .

[29]  J B Gibbs,et al.  Structure/function studies of the ras protein. , 1988, Cold Spring Harbor symposia on quantitative biology.

[30]  F. McCormick,et al.  A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants. , 1987, Science.

[31]  R. Goody,et al.  Preparation and characterization of nucleotide-free and metal ion-free p21 "apoprotein". , 1987, The Journal of biological chemistry.

[32]  S. Harrison,et al.  A system for collection and on-line integration of X-ray diffraction data from a multiwire area detector , 1987 .

[33]  M. Karplus,et al.  Crystallographic R Factor Refinement by Molecular Dynamics , 1987, Science.

[34]  G. Schulz,et al.  The glycine‐rich loop of adenylate kinase forms a giant anion hole , 1986, FEBS letters.

[35]  R. Goody,et al.  Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide‐binding site. , 1986, The EMBO journal.

[36]  E. Scolnick,et al.  /sup 31/P-NMR of the binary, one-to-one complex of ras p21 with guanosine-5'-diphosphate , 1986 .

[37]  S. Aaronson,et al.  Monoclonal antibody Y13-259 recognizes an epitope of the p21 ras molecule not directly involved in the GTP-binding activity of the protein , 1986, Molecular and cellular biology.

[38]  E. Scolnick,et al.  Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[39]  A. Mildvan,et al.  ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[40]  C. Der,et al.  Biological and biochemical properties of human ras H genes mutated at codon 61 , 1986, Cell.

[41]  M. Pincus,et al.  Conformational analysis of biologically active polypeptides with application to oncogenesis , 1985 .

[42]  B. Clark,et al.  A model for the tertiary structure of p21, the product of the ras oncogene. , 1985, Science.

[43]  M. Wigler,et al.  Purification and characterization of human H-ras proteins expressed in Escherichia coli , 1985, Molecular and cellular biology.

[44]  E. Scolnick,et al.  Viral Harvey ras p21 expressed in Escherichia coli purifies as a binary one-to-one complex with GDP. , 1985, The Journal of biological chemistry.

[45]  P. Seeburg,et al.  Biological properties of human c-Ha-ras1 genes mutated at codon 12 , 1984, Nature.

[46]  J. Feramisco,et al.  The product of ras is a GTPase and the T24 oncogenic mutant is deficient in this activity , 1984, Nature.

[47]  J B Gibbs,et al.  Intrinsic GTPase activity distinguishes normal and oncogenic ras p21 molecules. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[48]  M. Pincus,et al.  Prediction of the three-dimensional structure of the transforming region of the EJ/T24 human bladder oncogene product and its normal cellular homologue. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[49]  Wim G. J. Hol,et al.  Predicted nucleotide-binding properties of p21 protein and its cancer-associated variant , 1983, Nature.

[50]  N. Gay,et al.  Homology between human bladder carcinoma oncogene product and mitochondrial ATP-synthase , 1983, Nature.

[51]  E. Scolnick,et al.  Monoclonal antibodies to the p21 products of the transforming gene of Harvey murine sarcoma virus and of the cellular ras gene family , 1982, Journal of virology.

[52]  T. A. Jones,et al.  A graphics model building and refinement system for macromolecules , 1978 .