Crystal Structure of Human RhoA in a Dominantly Active Form Complexed with a GTP Analogue*
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M. Shirakawa | S. Kuroda | K. Kaibuchi | Masato Kato | T. Hakoshima | Toshiyuki Shimizu | K. Ihara | Sachiko Muraguchi
[1] J. Cherfils,et al. Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPγS , 1997, The EMBO journal.
[2] W. Minor,et al. Crystal structure of RhoA–GDP and its functional implications , 1997, Nature Structural Biology.
[3] S. Smerdon,et al. Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP , 1997, Nature.
[4] K. Aktories,et al. Rho proteins: targets for bacterial toxins. , 1997, Trends in microbiology.
[5] M. Rosen,et al. C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases , 1997, Nature.
[6] C. Fiorentini,et al. Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine , 1997, Nature.
[7] M. Mann,et al. Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1 , 1997, Nature.
[8] K. Nakao,et al. p140mDia, a mammalian homolog of Drosophila diaphanous,is a target protein for Rho small GTPase and is a ligand for profilin , 1997, The EMBO journal.
[9] G. Roberts,et al. A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm. , 1997, Structure.
[10] K. Kaibuchi,et al. Formation of Actin Stress Fibers and Focal Adhesions Enhanced by Rho-Kinase , 1997, Science.
[11] Y. Zheng,et al. Residues of the Rho Family GTPases Rho and Cdc42 That Specify Sensitivity to Dbl-like Guanine Nucleotide Exchange Factors* , 1997, The Journal of Biological Chemistry.
[12] M. Hirshberg,et al. The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue , 1997, Nature Structural Biology.
[13] X. Q. Chen,et al. The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton , 1996, Molecular and cellular biology.
[14] K. Fujisawa,et al. Identification of the Rho-binding Domain of p160ROCK, a Rho-associated Coiled-coil Containing Protein Kinase* , 1996, The Journal of Biological Chemistry.
[15] Yoshiharu Matsuura,et al. Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)* , 1996, The Journal of Biological Chemistry.
[16] A. Abo,et al. Rac “Insert Region” Is a Novel Effector Region That Is Implicated in the Activation of NADPH Oxidase, but Not PAK65* , 1996, The Journal of Biological Chemistry.
[17] A. Hall,et al. Rho: a connection between membrane receptor signalling and the cytoskeleton. , 1996, Trends in cell biology.
[18] S. Narumiya. The small GTPase Rho: cellular functions and signal transduction. , 1996, Journal of biochemistry.
[19] Ralf Janknecht,et al. Ras/Rap effector specificity determined by charge reversal , 1996, Nature Structural Biology.
[20] Kozo Kaibuchi,et al. Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase) , 1996, Science.
[21] K. Fujisawa,et al. Rhotekin, a New Putative Target for Rho Bearing Homology to a Serine/Threonine Kinase, PKN, and Rhophilin in the Rho-binding Domain* , 1996, The Journal of Biological Chemistry.
[22] T. Yamamoto,et al. Rho‐associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho. , 1996, The EMBO journal.
[23] Y. Zheng,et al. The Dbl family of oncogenes. , 1996, Current opinion in cell biology.
[24] K. Fujisawa,et al. The small GTP‐binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. , 1996, The EMBO journal.
[25] G. Bokoch,et al. Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. , 1996, Molecular biology of the cell.
[26] K. Kaibuchi,et al. Identification of a Putative Target for Rho as the Serine-Threonine Kinase Protein Kinase N , 1996, Science.
[27] K. Fujisawa,et al. Protein Kinase N (PKN) and PKN-Related Protein Rhophilin as Targets of Small GTPase Rho , 1996, Science.
[28] K D Cowtan,et al. Phase combination and cross validation in iterated density-modification calculations. , 1996, Acta crystallographica. Section D, Biological crystallography.
[29] Shuh Narumiya,et al. A novel partner for the GTP‐bound forms of rho and rac , 1995, FEBS letters.
[30] S. Sprang,et al. Tertiary and Quaternary Structural Changes in Giα1 Induced by GTP Hydrolysis , 1995, Science.
[31] A. Wittinghofer,et al. The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with RaplA and a GTP analogue , 1995, Nature.
[32] M. Mann,et al. Glucosylation of Rho proteins by Clostridium difficile toxin B , 1995, Nature.
[33] T. Sasaki,et al. Rho as a regulator of the cytoskeleton. , 1995, Trends in biochemical sciences.
[34] M. Olson,et al. Direct Involvement of the Small GTP-binding Protein Rho in lbc Oncogene Function (*) , 1995, The Journal of Biological Chemistry.
[35] W. Kabsch,et al. Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form , 1995, Nature.
[36] D. Ringe,et al. Structure of the human ADP-ribosylation factor 1 complexed with GDP , 1994, Nature.
[37] L. Chong,et al. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells , 1994, Cell.
[38] S. Sprang,et al. Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. , 1994, Science.
[39] Heidi E. Hamm,et al. Structural determinants for activation of the α-subunit of a heterotrimeric G protein , 1994, Nature.
[40] Jonathan A. Cooper,et al. A single amino acid change in Raf-1 inhibits Ras binding and alters Raf-1 function. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[41] K. Aktories,et al. Probing the action of Clostridium difficile toxin B in Xenopus laevis oocytes. , 1994, Journal of cell science.
[42] John G. Collard,et al. Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins , 1994, Cell.
[43] J. Navaza,et al. AMoRe: an automated package for molecular replacement , 1994 .
[44] T. Sasaki,et al. The Dbl oncogene product as a GDP/GTP exchange protein for the Rho family: its properties in comparison with those of Smg GDS. , 1994, Biochemical and biophysical research communications.
[45] L. Lim,et al. A brain serine/threonine protein kinase activated by Cdc42 and Rac1 , 1994, Nature.
[46] Heidi E. Hamm,et al. The 2.2 Å crystal structure of transducin-α complexed with GTPγS , 1993, Nature.
[47] R. Hilgenfeld,et al. Crystal structure of active elongation factor Tu reveals major domain rearrangements , 1993, Nature.
[48] M. Marshall,et al. The effector interactions of p21ras. , 1993, Trends in biochemical sciences.
[49] L. Lim,et al. A non-receptor tyrosine kinase that inhibits the GTPase activity of p21cdc42 , 1993, Nature.
[50] J. Thornton,et al. PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .
[51] A. Hall,et al. Different structural organization of Ras and Rho effector domains. , 1993, Oncogene.
[52] T. Sasaki,et al. Functional interactions of stimulatory and inhibitory GDP/GTP exchange proteins and their common substrate small GTP-binding protein. , 1992, The Journal of biological chemistry.
[53] J. Vandekerckhove,et al. Purification and characterization of an ADP-ribosyltransferase produced by Clostridium limosum. , 1992, The Journal of biological chemistry.
[54] J. Spudich,et al. Control of nonmuscle myosins by phosphorylation. , 1992, Annual review of biochemistry.
[55] S. Aaronson,et al. Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbloncogene product , 1991, Nature.
[56] K. Kaibuchi,et al. Molecular cloning of the cDNA for stimulatory GDP/GTP exchange protein for smg p21s (ras p21-like small GTP-binding proteins) and characterization of stimulatory GDP/GTP exchange protein. , 1991, Molecular and cellular biology.
[57] S. Narumiya,et al. Purification of GTPase-activating protein specific for the rho gene products. , 1991, The Journal of biological chemistry.
[58] J. Zou,et al. Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.
[59] S H Kim,et al. Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP. , 1991, Journal of molecular biology.
[60] S H Kim,et al. Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. , 1992, Science.
[61] W. Kabsch,et al. Three-dimensional structures of H-ras p21 mutants: Molecular basis for their inability to function as signal switch molecules , 1990, Cell.
[62] Y. Hata,et al. Regulation of reversible binding of smg p25A, a ras p21-like GTP-binding protein, to synaptic plasma membranes and vesicles by its specific regulatory protein, GDP dissociation inhibitor. , 1990, The Journal of biological chemistry.
[63] 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.
[64] A T Brünger,et al. Slow-cooling protocols for crystallographic refinement by simulated annealing. , 1990, Acta crystallographica. Section A, Foundations of crystallography.
[65] 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.
[66] S. Narumiya,et al. Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. , 1989, The Journal of biological chemistry.
[67] K. Nakao,et al. Purification and properties of the cytosolic substrate for botulinum ADP-ribosyltransferase. Identification as an Mr 22,000 guanine nucleotide-binding protein. , 1988, The Journal of biological chemistry.
[68] Y. Takai,et al. Purification and characterization of a GTP-binding protein with a molecular weight of 20,000 in bovine brain membranes. Identification as the rho gene product. , 1988, The Journal of biological chemistry.
[69] C. Der,et al. Biological and biochemical properties of human ras H genes mutated at codon 61 , 1986, Cell.
[70] R. Axel,et al. A novel ras-related gene family , 1985, Cell.