Three-dimensional structures of H-ras p21 mutants: Molecular basis for their inability to function as signal switch molecules
暂无分享,去创建一个
W. Kabsch | I. Schlichting | E. Pai | J. John | A. Wittinghofer | U. Krengel | A. Scherer | M. Frech | R. Schumann
[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 .