The GTPase superfamily: conserved structure and molecular mechanism

G PROTEINS: TRANSDUCERS OF RECEPTOR-GENERATED SIGNALS

Gilman, A. G. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.003151 · Cited by 6,405

ras GENES

Barbacid, M. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.004023 · Cited by 3,885

The GTPase superfamily: a conserved switch for diverse cell functions

Bourne, H. R., Sanders, D. A. R., & McCormick, F. P. (1990) · Nature · doi:10.1038/348125a0 · Cited by 2,336

GTPase inhibiting mutations activate the α chain of Gs and stimulate adenylyl cyclase in human pituitary tumours

Landis, C. A., Masters, S. B., Spada, A., Pace, A. M., Bourne, H. R., & Vallar, L. (1989) · Nature · doi:10.1038/340692a0 · Cited by 1,443

Refined crystal structure of the triphosphate conformation of H‐ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis.

PAI, E. F., Krengel, U., Petsko, G. A., Goody, R. S., Kabsch, W., & Wittinghofer, A. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07409.x · Cited by 1,073

Molecular Switch for Signal Transduction: Structural Differences Between Active and Inactive Forms of Protooncogenic ras Proteins

Milburn, M. V., Tong, L., deVos, A. M., Brünger, A. T., Yamaizumi, Z., Nishimura, S., & Kim, S. (1990) · Science · doi:10.1126/science.2406906 · Cited by 1,062

Two G Protein Oncogenes in Human Endocrine Tumors

Lyons, J. F., Landis, C. A., Harsh, G. R., Vallar, L., Grünewald, K., Feichtinger, H. G., Duh, Q., Clark, O. H., Kawasaki, E. S., Bourne, H. R., et al. (1990) · Science · doi:10.1126/science.2116665 · Cited by 1,036

Complete nucleotide sequences of the T24 human bladder carcinoma oncogene and its normal homologue

Capon, D. J., Chen, E. Y., Levinson, A. D., Seeburg, P. H., & Goeddel, D. V. (1983) · Nature · doi:10.1038/302033a0 · Cited by 997

G Proteins: A Family of Signal Transducers

Stryer, L., & Bourne, H. R. (1986) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.02.110186.002135 · Cited by 978

Mechanism of cholera toxin action: Covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system

Cassel, D., & Pfeuffer, T. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.6.2669 · Cited by 906

A ras-like protein is required for a post-Golgi event in yeast secretion

Salminen, A., & Novick, P. (1987) · Cell · doi:10.1016/0092-8674(87)90455-7 · Cited by 897

Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation

PAI, E. F., Kabsch, W., Krengel, U., Holmes, K. C., John, J., & Wittinghofer, A. (1989) · Nature · doi:10.1038/341209a0 · Cited by 876

Roles of G protein subunits in transmembrane signalling

Neer, E. J., & Clapham, D. E. (1988) · Nature · doi:10.1038/333129a0 · Cited by 795

Molecular cloning of five GTP-binding protein cDNA species from rat olfactory neuroepithelium.

Jones, D. T., & Reed, R. R. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47929-x · Cited by 758

Comparative biochemical properties of normal and activated human ras p21 protein

McGrath, J. P., Capon, D. J., Goeddel, D. V., & Levinson, A. D. (1984) · Nature · doi:10.1038/310644a0 · Cited by 699

Cloning of bovine GAP and its interaction with oncogenic ras p21

Vogel, U. S., Dixon, R. A. F., Schaber, M. D., Diehl, R. E., Marshall, M. S., Scolnick, E. M., Sigal, I. S., & Gibbs, W. W. (1988) · Nature · doi:10.1038/335090a0 · Cited by 649

Structure of the GDP Domain of EF-Tu and Location of the Amino Acids Homologous to ras Oncogene Proteins

JURNAK, F. A. (1985) · Science · doi:10.1126/science.3898365 · Cited by 621

ras GTPase activating protein: Signal transmitter and signal terminator

McCormick, F. (1989) · Cell · doi:10.1016/0092-8674(89)90976-8 · Cited by 607

rac, a novel ras-related family of proteins that are botulinum toxin substrates

Didsbury, J., Weber, R. F., Bokoch, G. M., Evans, T., & Snyderman, R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84716-6 · Cited by 575

The role of guanosine 5′-triphosphate in polypeptide chain elongation

Kaziro, Y. (1978) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(78)90009-5 · Cited by 557

Biological and biochemical properties of human rasH genes mutated at codon 61

Der, C. J., Finkel, T., & Cooper, G. M. (1986) · Cell · doi:10.1016/0092-8674(86)90495-2 · Cited by 536

Three-Dimensional Structure of an Oncogene Protein: Catalytic Domain of Human c-H- ras P21

de Vos, A. M., Tong, L., Milburn, M. V., Matias, P. M., Jancarik, J., Noguchi, S., Nishimura, S., Miura, K., Ohtsuka, E., & Kim, S. (1988) · Science · doi:10.1126/science.2448879 · Cited by 529

Structure and activation of the human N-ras gene

Taparowsky, E. J., Shimizu, K., Goldfarb, M. P., & Wigler, M. H. (1983) · Cell · doi:10.1016/0092-8674(83)90390-2 · Cited by 527

Guanosine Triphosphatase Activating Protein (GAP) Interacts with the p21 ras Effector Binding Domain

Adari, H. Y., Lowy, D. R., Willumsen, B. M., Der, C. J., & McCormick, F. P. (1988) · Science · doi:10.1126/science.2833817 · Cited by 506

Site of G Protein Binding to Rhodopsin Mapped with Synthetic Peptides from the α Subunit

Hamm, H. E., Deretic, D., Arendt, A., Hargrave, P. A., Koenig, B. W., & Hofmann, K. P. (1988) · Science · doi:10.1126/science.3136547 · Cited by 498

Characterization of transducin from bovine retinal rod outer segments. I. Separation and reconstitution of the subunits.

Fung, B. K.-K. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44483-8 · Cited by 491

Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis

Schlichting, I., Almo, S. C., Rapp, G., Wilson, K. S., Petratos, K., Lentfer, A., Wittinghofer, A., Kabsch, W., PAI, E. F., Petsko, G. A., et al. (1990) · Nature · doi:10.1038/345309a0 · Cited by 487

Homologies Between Signal Transducing G Proteins and ras Gene Products

Hurley, J. B., Simon, M. I., Teplow, D. B., Robishaw, J. D., & Gilman, A. G. (1984) · Science · doi:10.1126/science.6436980 · Cited by 483

The S. cerevisiae CDC25 gene product regulates the RAS/adenylate cyclase pathway

Broek, D., Toda, T., Michaeli, T., Levin, L. R., Birchmeier, C., Zoller, M. J., Powers, S., & Wigler, M. H. (1987) · Cell · doi:10.1016/0092-8674(87)90076-6 · Cited by 478

Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle

Bernstein, H. D., Poritz, M. A., Strub, K., Hoben, P. J., Brenner, S., & Walter, P. (1989) · Nature · doi:10.1038/340482a0 · Cited by 467

Genes in S. cerevisiae encoding proteins with domains homologous to the mammalian ras proteins

Powers, S., Kataoka, T., Fasano, O., Goldfarb, M. P., Strathem, J., Broach, J. R., & Wigler, M. H. (1984) · Cell · doi:10.1016/0092-8674(84)90340-4 · Cited by 460

Pertussis toxin-catalyzed ADP-ribosylation of transducin. Cysteine 347 is the ADP-ribose acceptor site.

West, R. E., Moss, J., Vaughan, M. J., Liu, T., & Liu, T. Y. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38585-x · Cited by 456

Adrenergic receptors. Models for the study of receptors coupled to guanine nucleotide regulatory proteins.

Lefkowitz, R. J., & Caron, M. G. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60663-5 · Cited by 447

A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus.

Nakano, A., & Muramatsu, M. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.6.2677 · Cited by 447

G proteins control diverse pathways of transmembrane signaling 1

Freissmuth, M., Casey, P. J., & Gilman, A. G. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.10.2546847 · Cited by 404

A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product

Gallwitz, D., Donath, C., & Sander, C. (1983) · Nature · doi:10.1038/306704a0 · Cited by 401

The yeast SCG1 gene: A Gα-like protein implicated in the a- and α-factor response pathway

Dietzel, C., & Kurjan, J. (1987) · Cell · doi:10.1016/0092-8674(87)90166-8 · Cited by 397

Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X‐ray crystallography.

la Cour, T. F. M., Nyborg, J., Thirup, S., & Clark, B. F. C. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03943.x · Cited by 396

Multicopy suppression of the cdc24 budding defect in yeast by CDC42 and three newly identified genes including the ras-related gene RSR1.

Bender, A., & Pringle, J. R. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.24.9976 · Cited by 388

The cytoplasmic protein GAP is implicated as the target for regulation by the ras gene product

Calés, C., Hancock, J. F., Marshall, C. J., & Hall, A. (1988) · Nature · doi:10.1038/332548a0 · Cited by 386

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

Krengel, U., Schlichting, I., Scherer, A., Schumann, R., Frech, M., John, J., Kabsch, W., PAI, E. F., & Wittinghofer, A. (1990) · Cell · doi:10.1016/0092-8674(90)90018-a · Cited by 386

Effects of Mg2+ and the beta gamma-subunit complex on the interactions of guanine nucleotides with G proteins.

Higashijima, T., Ferguson, K. M., Sternweis, P. C., Smigel, M. D., & Gilman, A. G. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75851-7 · Cited by 366

Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP–binding domains

Römisch, K., Webb, J. R., Herz, J., Prehn, S., Frank, R. W., Vingron, M., & Dobberstein, B. (1989) · Nature · doi:10.1038/340478a0 · Cited by 346

Signal sorting and amplification through G protein-coupled receptors

Ross, E. M. (1989) · Neuron · doi:10.1016/0896-6273(89)90027-5 · Cited by 336

Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region.

Pizon, V., Chardin, P., Janoueix‐Lerosey, I., Olofsson, B., & Tavitian, A. (1988) · PubMed · Cited by 336

Characterization of transducin from bovine retinal rod outer segments. II. Evidence for distinct binding sites and conformational changes revealed by limited proteolysis with trypsin.

Fung, B. K.-K., & Nash, C. R. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44484-x · Cited by 331

The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion.

Zahraoui, A., Touchot, N., Chardin, P., & Tavitian, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63872-4 · Cited by 330

Identification of effector residues and a neutralizing epitope of Ha-ras-encoded p21.

Sigal, I. S., Gibbs, W. W., D'Alonzo, J., & Scolnick, E. M. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4725 · Cited by 285

Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects.

Sigal, I. S., Gibbs, W. W., D'Alonzo, J., Temeles, G. L., Wolanski, B., Socher, S. H., & Scolnick, E. M. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.4.952 · Cited by 267

Developmental regulation of a dictyostelium gene encoding a protein homologous to mammalian ras protein

Reymond, C., Gomer, R. H., Mehdy, M. C., & Firtel, R. (1984) · Cell · doi:10.1016/0092-8674(84)90199-5 · Cited by 259

Characterization of two members of the rho gene family from the yeast Saccharomyces cerevisiae.

Madaule, P., Axel, R., & Myers, A. M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.3.779 · Cited by 258

Identification of receptor contact site involved in receptor–G protein coupling

Sullivan, K. A., Miller, R. T., Masters, S. B., Beiderman, B., Heideman, W., & Bourne, H. R. (1987) · Nature · doi:10.1038/330758a0 · Cited by 255

Identification of a GTP-binding protein alpha subunit that lacks an apparent ADP-ribosylation site for pertussis toxin.

Fong, H. K. W., Yoshimoto, K. K., Eversole-Cire, P., & Simon, M. I. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.9.3066 · Cited by 253

Identification of distinct cytoplasmic targets for ras/R-ras and rho regulatory proteins

Garrett, M. D., Self, A. J., van Oers, C., & Hall, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31215-2 · Cited by 252

Synthesis in Escherichia coli of GTPase-deficient mutants of Gsα

Graziano, M. P., & Gilman, A. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84854-8 · Cited by 251

Inhibition of GTPase Activating Protein Stimulation of Ras-p21 GTPase by the K rev -1 Gene Product

Frech, M., John, J., Pizon, V., Chardin, P., Tavitian, A., Clark, R., McCormick, F. P., & Wittinghofer, A. (1990) · Science · doi:10.1126/science.2164710 · Cited by 251

Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin.

Dop, C. V., Tsubokawa, M., Bourne, H. R., & Ramachandran, J. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43512-5 · Cited by 238

Functional homology between signal-coupling proteins. Cholera toxin inactivates the GTPase activity of transducin.

Abood, M. E., Hurley, J. B., Pappone, M. C., Bourne, H. R., & Stryer, L. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33851-1 · Cited by 223

Characterization, cloning and sequence analysis of the CDC25 gene which controls the cyclic AMP level of Saccharomyces cerevisiae.

Camonis, J., Kalékine, M., Gondré, B., Garreau, H., Boy‐Marcotte, E., & Jacquet, M. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04222.x · Cited by 222

Sequence analysis of cDNA and genomic DNA for a putative pertussis toxin-insensitive guanine nucleotide-binding regulatory protein alpha subunit.

Matsuoka, M., Itoh, H., Kozasa, T., & Kaziro, Y. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.15.5384 · Cited by 210

The ras oncogene--an important regulatory element in lower eucaryotic organisms

Gibbs, W. W., & Marshall, M. S. (1989) · Microbiological Reviews · doi:10.1128/mr.53.2.171-185.1989 · Cited by 205

Structure of the human and murine R-ras genes, novel genes closely related to ras proto-oncogenes

Lowe, D. G., Capon, D. J., Delwart, E., Sakaguchi, A. Y., Naylor, S. L., & Goeddel, D. V. (1987) · Cell · doi:10.1016/0092-8674(87)90364-3 · Cited by 204

Mutations in the GTP-binding site of GSα alter stimulation of adenylyl cyclase

Masters, S. B., Miller, R. T., Chi, M. H., Chang, F. H., Beiderman, B., Lopez, N. G., & Bourne, H. R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84853-6 · Cited by 202

Amino acid sequence of the alpha subunit of transducin deduced from the cDNA sequence.

Medynski, D. C., Sullivan, K. A., Smith, D. H., Dop, C. V., Chang, F. H., Fung, B. K.-K., SEEBURG, P. H., & Bourne, H. R. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.13.4311 · Cited by 202

Isolation of a second yeast Saccharomyces cerevisiae gene (GPA2) coding for guanine nucleotide-binding regulatory protein: studies on its structure and possible functions.

Nakafuku, M., Obara, T., Kaibuchi, K., Miyajima, I., Miyajima, A., Itoh, H., Nakamura, S., Arai, K., Matsumoto, K., & Kaziro, Y. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.5.1374 · Cited by 200

Family of G protein α chains: amphipathic analysis and predicted structure of functional domains

Masters, S. B., Stroud, R. M., & Bourne, H. R. (1986) · Protein Engineering Design and Selection · doi:10.1093/protein/1.1.47 · Cited by 199

Sequences of the bovine and yeast ADP-ribosylation factor and comparison to other GTP-binding proteins.

Sewell, J. L., & Kahn, R. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.13.4620 · Cited by 197

Mutational analysis of a ras catalytic domain.

Willumsen, B. M., Papageorge, A. G., Kung, H. F., Bekesi, E., Robins, T., Johnsen, M., Vass, W. C., & Lowy, D. R. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.7.2646 · Cited by 195

Mutations of Gs α Designed to Alter the Reactivity of the Protein with Bacterial Toxins

Freissmuth, M., & Gilman, A. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)88271-4 · Cited by 189

Mechanisms of muscarinic receptor action on Go in reconstituted phospholipid vesicles

Florio, V. A., & Sternweis, P. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84939-6 · Cited by 185

The drosophila ras oncogenes: Structure and nucleotide sequence

Neuman‐Silberberg, F. S., Schejter, E. D., Hoffmann, F. M., & Shilo, B. (1984) · Cell · doi:10.1016/0092-8674(84)90437-9 · Cited by 180

ras and GAP—Who's controlling whom?

Hall, A. (1990) · Cell · doi:10.1016/0092-8674(90)90054-i · Cited by 180

Carboxyl Rerminal Domain of G sα Specifies Coupling of Receptors to Stimulation of Adenylyl Cyclase

Masters, S. B., Sullivan, K. A., Miller, R. T., Beiderman, B., Lopez, N. G., Ramachandran, J., & Bourne, H. R. (1988) · Science · doi:10.1126/science.2899356 · Cited by 177

Deduced primary structure of the alpha subunit of the GTP-binding stimulatory protein of adenylate cyclase.

Robishaw, J. D., Russell, D. W., Harris, B. A., Smigel, M. D., & Gilman, A. G. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.5.1251 · Cited by 177

A mutation that prevents GTP-dependent activation of the α chain of Gs

Miller, R. T., Masters, S. B., Sullivan, K. A., Beiderman, B., & Bourne, H. R. (1988) · Nature · doi:10.1038/334712a0 · Cited by 176

The primary structure of the α subunit of human elongation factor 1

Brands, J. H. G. M., Maassen, J. A., van Hemert, F. J., Amons, R., & Möller, W. J. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb09472.x · Cited by 170

Occurrence in Saccharomyces cerevisiae of a gene homologous to the cDNA coding for the alpha subunit of mammalian G proteins.

Nakafuku, M., Itoh, H., Nakamura, S., & Kaziro, Y. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.8.2140 · Cited by 167

The Bacillus subtilis spo0B stage 0 sporulation operon encodes an essential GTP-binding protein

Trach, K. A., & Hoch, J. A. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.3.1362-1371.1989 · Cited by 161

Dominant yeast and mammalian RAS mutants that interfere with the CDC25-dependent activation of wild-type RAS in Saccharomyces cerevisiae.

Powers, S., O’Neill, K. E., & Wigler, M. H. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.2.390 · Cited by 161

Nucleotide sequence of aEuglena gracilischloroplast genome region coding for the elongation factor Tu; evidence for a spliced mRNA

Montandon, P.-E., & Stutz, E. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.17.5877 · Cited by 159

A new cell division operon inEscherichia coli

Gill, D. R., Hatfull, G. F., & Salmond, G. P. C. (1986) · Molecular and General Genetics MGG · doi:10.1007/bf02428043 · Cited by 154

Identification of two genes coding for the translation elongation factor EF‐1 alpha of S. cerevisiae.

Schirmaier, F., & Philippsen, P. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb02295.x · Cited by 150

Enhancement of the GDP-GTP Exchange of RAS Proteins by the Carboxyl-Terminal Domain of SCD25

Créchet, J., Poullet, P., Mistou, M., Parmeggiani, A., Camonis, J., Boy‐Marcotte, E., Damak, F., & Jacquet, M. (1990) · Science · doi:10.1126/science.2188363 · Cited by 148

A GTP-binding protein of Escherichia coli has homology to yeast RAS proteins.

Ahnn, J., March, P. E., Takiff, H. E., & Inouye, M. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.23.8849 · Cited by 143

Topology of signal recognition particle receptor in endoplasmic reticulum membrane

Lauffer, L., García, P. D., Harkins, R. N., Coussens, L. M., Ullrich, A., & Walter, P. (1985) · Nature · doi:10.1038/318334a0 · Cited by 140

Nucleotide sequence of human rho cDNA clone 12

Yeramian, P., Chardin, P., Madaule, P., & Tavitian, A. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.4.1869 · Cited by 139

Amino acid sequence of mammalian elongation factor 2 deduced from the cDNA sequence: homology with GTP-binding proteins.

Kohno, K., Uchida, T., Ohkubo, H., Nakanishi, S., Nakanishi, T., Fukui, T., Ohtsuka, E., Ikehara, M., & Okada, Y. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.14.4978 · Cited by 138

Molecular cloning and sequence analysis of a ras gene from Schizosaccharomyces pombe.

Fukui, Y., & Kaziro, Y. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03684.x · Cited by 136

Coding sequence of humanrhocDNAs clone 6 and clone 9

Chardin, P., Madaule, P., & Tavitian, A. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.6.2717 · Cited by 136

Molecular cloning and sequence determination of the nuclear gene coding for mitochondrial elongation factor Tu of Saccharomyces cerevisiae.

Nagata, S., Tsunetsugu‐Yokota, Y., Naito, A., & Kaziro, Y. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.20.6192 · Cited by 134

Kinetic analysis of the hydrolysis of GTP by p21N-ras. The basal GTPase mechanism.

Neal, S. E., Eccleston, J. F., Hall, A., & Webb, M. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77694-7 · Cited by 130

Characterization of transducin from bovine retinal rod outer segments. Participation of the amino-terminal region of T alpha in subunit interaction.

Navon, S. E., & Fung, B. K.-K. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47791-5 · Cited by 128

A human homologue of the yeast GST1 gene codes for a GTP‐binding protein and is expressed in a proliferation‐dependent manner in mammalian cells.

Hoshino, S.-I., Miyazawa, H., Enomoto, T., Hanaoka, F., Kikuchi, Y., Kikuchi, A., & Ui, M. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08558.x · Cited by 122

A yeast gene required for the G1‐to‐S transition encodes a protein containing an A‐kinase target site and GTPase domain.

Kikuchi, Y., Shimatake, H., & Kikuchi, A. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02928.x · Cited by 120

Characterization and Developmental Expression of a Drosophila ras Oncogene

Mozer, B. A., Marlor, R. L., Parkhurst, S. M., & Corces, V. G. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.4.885-889.1985 · Cited by 115

Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain.

Brünger, A. T., Milburn, M. V., Tong, L., Devos, A. M., Jancarik, J., Yamaizumi, Z., Nishimura, S., Ohtsuka, E., & Kim, S. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.12.4849 · Cited by 115

Identification of Small Clusters of Divergent Amino Acids that Mediate the Opposing Effects of ras and K rev -1

Zhang, K., Noda, M., Vass, W. C., Papageorge, A. G., & Lowy, D. R. (1990) · Science · doi:10.1126/science.2115210 · Cited by 111

Multiple alpha subunits of guanine nucleotide-binding proteins in Dictyostelium.

Pupillo, M., Kumagai, A., Pitt, G. S., Firtel, R., & Devreotes, P. N. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.13.4892 · Cited by 111

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.

Neal, S. E., Eccleston, J. F., & Webb, M. R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.9.3562 · Cited by 109

Structure and expression of elongation factor 1α in tomato

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Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue to the 54-kD subunit of the signal recognition particle that in S. cerevisiae is essential for growth.

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Molecular cloning, characterization, and expression of human ADP-ribosylation factors: two guanine nucleotide-dependent activators of cholera toxin.

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The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21‐K polypeptide.

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Identification of the ral and rac1 Gene Products, Low Molecular Mass GTP-binding Proteins from Human Platelets

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Xenopus oocyte germinal-vesicle breakdown induced by [Val12]Ras is inhibited by a cytosol-localized Ras mutant.

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Reactive sulfhydryl groups of alpha 39, a guanine nucleotide-binding protein from brain. Location and function.

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Organization and codon usage of the streptomycin operon in Micrococcus luteus, a bacterium with a high genomic G + C content

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Sequence analysis of bovine retinal S‐antigen

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The Mechanism of Guanosine Nucleotide Hydrolysis by p21 c-Ha-ras

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The nucleotide sequence of theEscherichta coli fusgene, coding for elongation factor G

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Cloning of ara, a putative Arabidopsis thaliana gene homologous to the ras-related gene family

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Ras interaction with the GTPase‐activating protein (GAP)

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Characterization of the lep operon of Escherichia coli. Identification of the promoter and the gene upstream of the signal peptidase I gene.

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The amino acid sequence of elongation factor Tu of Escherichia coli. The complete sequence.

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Mechanism of action of monoclonal antibodies that block the light activation of the guanyl nucleotide-binding protein, transducin.

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Molecular cloning and sequence determination of the tuf gene coding for the elongation factor Tu of Thermus thermophilus HB8

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Cloning and nucleotide sequence of the gene for an archaebacterial protein synthesis elongation factor Tu

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Topographic analysis of antigenic determinants recognized by monoclonal antibodies to the photoreceptor guanyl nucleotide-binding protein, transducin.

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Biochemical and crystallographic characterization of a complex of c-Ha-ras p21 and caged GTP with flash photolysis.

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Expression of an activated ras gene causes developmental abnormalities in transgenic Drosophila melanogaster.Preprint

Bishop, J. G., & Corces, V. G. (1988) · Genes & Development · doi:10.1101/gad.2.5.567 · Cited by 61

Characterization of the str operon genes from Spirulina platensis and their evolutionary relationship to those of other prokaryotes

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Characterization of functional domains of p21 ras by use of chimeric genes.

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Conformational changes involved in the activation of ras p21: Implications for related proteins

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Mechanism of the Nucleotide Exchange Reaction in Eukaryotic Polypeptide Chain Initiation

Dholakia, J. N., & Wahba, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31293-0 · Cited by 57

Studies on the Polypeptide Elongation Factors from E. coli

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Kinetics and thermodynamics of the interaction of elongation factor Tu with elongation factor Ts, guanine nucleotides, and aminoacyl-tRNA.

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Characterization of transducin from bovine retinal rod outer segments. Use of monoclonal antibodies to probe the structure and function of the subunit.

Navon, S. E., & Fung, B. K.-K. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57419-1 · Cited by 52

A new RAS mutation that suppresses the CDC25 gene requirement for growth of Saccharomyces cerevisiae.

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A new member of therasgene superfamily identified in a rat liver cell line

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Genes for the ribosomal proteins S12 and S7 and elongation factors EF-G and EF-Tu of the cyanobacterium, Anacystis nidulans: Structural homology between 16S rRNA and S7 mRNA

Meng, B. Y., Shinozaki, K., & Sugiura, M. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00332226 · Cited by 51

Expression of a Gαs/Gαi Chimera That Constitutively Activates Cyclic AMP Synthesis

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Mutagenesis of bacterial elongation factor Tu at lysine 136

Hwang, Y., Sanchez, A., & Miller, D. L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83183-0 · Cited by 42

Nucleotide sequence of the gene coding for the elongation factor Tu from the extremely thermophilic eubacterium Thermotoga maritima

Bachleitner, M. (1989) · FEMS Microbiology Letters · doi:10.1016/0378-1097(89)90157-2 · Cited by 40

Hydrolysis of GTP by the α‐chain of Gs and other GTP binding proteins

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The Guanine - Nucleotide Binding Proteins: Common Structural And Functional Properties

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Nucleotide sequence of the gene coding for the elongation factor Tu from the extremely thermophilic eubacteriumThermotoga maritima

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Chimeric proteins define variable and essential regions of Ha-ras-encoded protein.

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Conformation change of effector-region residues in antiparallel β-sheet of human c-Ha-ras protein on GDP→GTPγS exchange: A two-dimensional NMR study

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Structure and expression of elongation factor 2 gene during development of Dictyostelium discoideum

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Diverse Biological Functions of Small GTP-binding Proteins in YeastPreprint

Botstein, D., Segev, N., Stearns, T., Hoyt, M. A., Holden, J., & Kahn, R. (1988) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1988.053.01.072 · Cited by 30

Antibodies to Synthetic Peptide from the Residue 33 to 42 Domain of c-Ha- ras p21 Block Reconstitution of the Protein with Different Effectors

Rey, I., Soubigou, P., Debüssche, L., David, C., Morgat, A., Bost, P., Mayaux, J. F., & Tocqué, B. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3904-3910.1989 · Cited by 23

H- ras Mutants Lacking the Epitope for the Neutralizing Monoclonal Antibody Y13-259 Show Decreased Biological Activity and Are Deficient in GTPase-Activating Protein Interaction

Srivastava, S. K., Donato, A. D., & Lacal, J. C. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1779-1783.1989 · Cited by 21

Identification, cloning and sequence of the Streptococcus faecium infB (translational initiation factor IF2) gene

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A Mutation That Hinders The GTP Induced Aminoacyl-tRNA BINDING of ELONGATION Factor TU

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Mammalian Mitogen-Activated Protein Kinase Signal Transduction Pathways Activated by Stress and Inflammation

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Identification of FAP Locus Genes from Chromosome 5q21

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The GTPase superfamily: a conserved switch for diverse cell functions

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