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The GTPase superfamily: conserved structure and molecular mechanism
Abstract
GTPases are conserved molecular switches, built according to a common structural design. Rapidly accruing knowledge of individual GTPases--crystal structures, biochemical properties, or results of molecular genetic experiments--support and generate hypotheses relating structure to function in other members of the diverse family of GTPases.
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“Rather, due to the intrinsically low GTPase activity of G-proteins, regulatory proteins are required for spatiotemporal control of the transition between active and inactive states (Fig. 1B).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [8]
In the citing paper
“The affinity of the interaction between GTPases and either guanine nucleotides is extremely high (Kd 10−7–10−11) ensuring that these are committed states that do not spontaneously interchange; they do not respond to changes in cellular nucleotide concentrations (8).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [8]
In the citing paper
“KRAS proteins primarily bind to guanosine diphosphate (GDP) and are in an inactive conformation maintained by intrinsic guanosine triphosphate (GTP) hydrolytic activity.”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [8]
Citations
Cites
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
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
Self-citationLandis, 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
Self-citationPAI, 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
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
Self-citationComplete 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
Self-citationCassel, D., & Pfeuffer, T. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.6.2669 · Cited by 906
Flagged first, then by citations
Research works printed but not linked: 10
- Powers, S., O'Neill, K. & Wigler, M. Molec. Cell. Biol. 9, 390–395 (1989).
- Birnbaumer, L. et al. Kidney Internatn. (Suppl.) 32, S14–S37 (1987).
- Srivastava, S. K., Di Donato, A. & Lacal, J. C. Molec. cell. Biol. 9, 1779–1783 (1989).
- Mozer, B., Marlor, R., Parkhurst, S. & Corces, V. Molec. cell. Biol. 5, 885–889 (1985).
- Pizon, V., Chardin, P., Lerosey, I., Olofsson, B. & Tavitian, A. Oncogene 3, 201–204 (1988).
- Johnson, D. I. & Pringle, J. R. J. Cell Biol. (in the press).
- Miyake, S. & Yamamoto, M. EMBO J. (in the press).
- Camonis, J. H. & Jacquet, M. Molec. cell. Biol. 8, 2980–2983 (1988).
- Willumsen, B. M. et al. Molec. cell. Biol. 6, 2646–2654 (1986).
- Rey, I. et al. Molec. cell. Biol. 9, 3904–3910 (1989).
Cited by
Sorted by citations
Items 301–400 of 1,010
Aberrant function of the Ras signal transduction pathway in human breast cancer
Clark, G. J., & Der, C. J. (1995) · Breast Cancer Research and Treatment · doi:10.1007/bf00694753 · Cited by 213
Garrotes, Springs, Ratchets, and Whips: Putting Dynamin Models to the Test
Sever, S., Damke, H., & Schmid, S. L. (2000) · Traffic · doi:10.1034/j.1600-0854.2000.010503.x · Cited by 213
Fabrizio, P., Laggerbauer, B., Lauber, J., Lane, W. S., & Lührmann, R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.13.4092 · Cited by 212
Cdc42p GTPase is involved in controlling polarized cell growth in Schizosaccharomyces pombe.
Miller, P. J., & Johnson, D. I. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.2.1075 · Cited by 212
Kumagai, N., Morii, N., Fujisawa, K., Nemoto, Y., & Narumiya, S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74497-4 · Cited by 212
Crystal structure of the NG domain from the signal-recognition particle receptor FtsY.
Montoya, G., Svensson, C., Luirink, J., & Sinning, I. (1997) · Nature · doi:10.1038/385365a0 · Cited by 210
The Universally Conserved Prokaryotic GTPases
Verstraeten, N., Fauvart, M., Versées, W., & Michiels, J. J. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00009-11 · Cited by 208
The requirement for cobalt in vitamin B12: A paradigm for protein metalation
Osman, D., Cooke, A., Young, T. R., Deery, E. C., Robinson, N. J., & Warren, M. J. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118896 · Cited by 227
Ozaki, K., Tanaka, K., Imamura, H., Hihara, T., Kameyama, T., Nonaka, H., Hirano, H., Matsuura, Y., & Takai, Y. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00573.x · Cited by 209
RhoE Regulates Actin Cytoskeleton Organization and Cell Migration
Guasch, R. M., Scambler, P. J., Jones, G. E., & Ridley, A. J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.8.4761 · Cited by 209
GTP-binding proteins in plants: new members of an old family
Mā, H. (1994) · Plant Molecular Biology · doi:10.1007/bf00016493 · Cited by 208
The Rho GTPase Rho3 Has a Direct Role in Exocytosis That Is Distinct from Its Role in Actin Polarity
Adamo, J. E., Rossi, G., & Brennwald, P. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.12.4121 · Cited by 208
Two Families of GTPases Dominate the Complex Cellular Response to IFN-γ
Boehm, U., Guethlein, L. A., Klamp, T., Ozbek, K., Schaub, A., Fütterer, A., Pfeffer, K., & Howard, J. C. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.12.6715 · Cited by 208
Zavialov, A. V., Buckingham, R. H., & Ehrenberg, M. (2001) · Cell · doi:10.1016/s0092-8674(01)00508-6 · Cited by 207
Lipid modifications of G proteins
Casey, P. J. (1994) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(94)90139-2 · Cited by 207
Schmidt, S., Sohrmann, M., Hofmann, K., Woollard, A., & Simanis, V. (1997) · Genes & Development · doi:10.1101/gad.11.12.1519 · Cited by 207
Huang, H.-K., Yoon, H., Hannig, E. M., & Donahue, T. F. (1997) · Genes & Development · doi:10.1101/gad.11.18.2396 · Cited by 205
Role of heterotrimeric G proteins in membrane traffic.
Bomsel, M., & Mostov, K. E. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.12.1317 · Cited by 206
The Highly Conserved LepA Is a Ribosomal Elongation Factor that Back-Translocates the Ribosome
Qin, Y., Polacek, N., Vesper, O., Staub, E., Einfeldt, E., Wilson, D. N., & Nierhaus, K. H. (2006) · Cell · doi:10.1016/j.cell.2006.09.037 · Cited by 205
Mittal, R., Ahmadian, M. R., Goody, R. S., & Wittinghofer, A. (1996) · Science · doi:10.1126/science.273.5271.115 · Cited by 202
Mitochondrial Dynamics in Stem Cells and Differentiation
Seo, B. J., Yoon, S. H., & Tae, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123893 · Cited by 208
Regulation of cadherin-mediated cell–cell adhesion by the Rho family GTPases
Kaibuchi, K., Kuroda, S., Fukata, M., & Nakagawa, M. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)00014-9 · Cited by 204
A new family of G-protein regulators — the RGS proteins
Koelle, M. R. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80055-5 · Cited by 204
Drug-metabolizing enzymes in ligand-modulated transcription
Nebert, D. W. (1994) · Biochemical Pharmacology · doi:10.1016/0006-2952(94)90434-0 · Cited by 201
Cloning of a Rab3 isotype predominantly expressed in adipocytes.
Baldini, G., Hohl, T. M., Lin, H. Y.-F., & Lodish, H. F. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.11.5049 · Cited by 203
Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
Powers, T., & Walter, P. (1995) · Science · doi:10.1126/science.7660124 · Cited by 203
A constituent of the chloroplast import complex represents a new type of GTP‐binding protein
Seedorf, M., Waegemann, K., & Soll, J. (1995) · The Plant Journal · doi:10.1046/j.1365-313x.1995.7030401.x · Cited by 202
Intraflagellar Transport Protein 27 Is a Small G Protein Involved in Cell-Cycle Control
Qin, H., Wang, Z., Diener, D. R., & Rosenbaum, J. L. (2007) · Current Biology · doi:10.1016/j.cub.2006.12.040 · Cited by 207
Yin, Y., Zhang, B.-B., Wang, W., Fei, B., Quan, C., Zhang, J., Song, M., Bian, Z., Wang, Q., Ni, S., et al. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-1030 · Cited by 202
Plant Rac-Like GTPases Are Activated by Auxin and Mediate Auxin-Responsive Gene Expression
Tao, L., Cheung, A. Y., & Wu, H. (2002) · The Plant Cell · doi:10.1105/tpc.006320 · Cited by 201
ROP GTPases Structure-Function and Signaling Pathways
Feiguelman, G., Fu, Y., & Yalovsky, S. (2017) · PLANT PHYSIOLOGY · doi:10.1104/pp.17.01415 · Cited by 201
Garrett, M. D., Zahner, J. E., Cheney, C. M., & Novick, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06436.x · Cited by 201
The Role of GTP-Binding Proteins in Transport Along the Exocytic Pathway
Ferro‐Novick, S., & Novick, P. (1993) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.09.110193.003043 · Cited by 201
Schwacha, A., & Bell, S. P. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00389-6 · Cited by 200
Receptor and βγ Binding Sites in the α Subunit of the Retinal G Protein Transducin
Onrust, R., Herzmark, P., Chi, P., García, P. D., Lichtarge, O., Kingsley, C., & Bourne, H. R. (1997) · Science · doi:10.1126/science.275.5298.381 · Cited by 199
Self-citationInvolvement of rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in cell motility.
Takaishi, K., Kikuchi, A., Kuroda, S., Kotani, K., Sasaki, T., & Takai, Y. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.72 · Cited by 198
Nishiwaki, T., Iwasaki, H., Ishiura, M., & Kondo, T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.1.495 · Cited by 198
C-protein-regulated phospholipases C, D and A2-mediated signalling in neutrophils
Cockcroft, S. (1992) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(92)90036-a · Cited by 198
Genes and their organization in the replication origin region of the bacterial chromosome
Ogasawara, N., & Yoshikawa, H. (1992) · Molecular Microbiology · doi:10.1111/j.1365-2958.1992.tb01510.x · Cited by 197
Evidence for G-Protein Regulation of Inward K + Channel Current in Guard Cells of Fava Bean
Fairley-Grenot, K., & Assmann, S. M. (1991) · The Plant Cell · doi:10.1105/tpc.3.9.1037 · Cited by 197
Mitochondrial fusion proteins: Dual regulators of morphology and metabolism
Antonio Zorzano, A., Liesa, M., Sebastián, D., Segalés, J., & Palacín, M. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.01.002 · Cited by 204
Kiener, P. A., Rankin, B. M., Burkhardt, A. L., Schieven, G. L., Gilliland, L. K., Rowley, R. B., Bolen, J. B., & Ledbetter, J. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80545-6 · Cited by 196
G-protein diseases furnish a model for the turn-on switch
Iiri, T., Farfel, Z., & Bourne, H. R. (1998) · Nature · doi:10.1038/27831 · Cited by 195
Self-citationNucleocytoplasmic transport of macromolecules
Corbett, A. H., & Silver, P. A. (1997) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.61.2.193-211.1997 · Cited by 195
RAS mutations and clonality analysis in children with juvenile myelomonocytic leukemia (JMML)
Flotho, C., Valcamonica, S., Mach‐Pascual, S., Schmahl, G. E., Corral, L., Ritterbach, J., Hasle, H., Aricò, M., Biondi, A., & Niemeyer, C. M. (1999) · Leukemia · doi:10.1038/sj.leu.2401240 · Cited by 194
Ran/TC4: a small nuclear GTP-binding protein that regulates DNA synthesis.
Ren, M., Drivas, G., D’Eustachio, P., & Rush, M. G. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.120.2.313 · Cited by 194
Eph receptor–ephrin bidirectional signals that target Ras and Rho proteins
Hooten, N. N., & Pasquale, E. B. (2003) · Cellular Signalling · doi:10.1016/j.cellsig.2003.10.006 · Cited by 199
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Arimura, S., & Tsutsumi, N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082663299 · Cited by 194
A single amino acid change in Raf-1 inhibits Ras binding and alters Raf-1 function.
Fabian, J. R., Vojtek, A. B., Cooper, J. A., & Morrison, D. K. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.13.5982 · Cited by 193
Cell wall integrity modulates RHO1 activity via the exchange factor ROM2
Bickle, M., Delley, P., Schmidt, A., & Hall, M. N. (1998) · EMBO Journal · doi:10.1093/emboj/17.8.2235 · Cited by 198
Robinson, N. G. G., Guo, L., Imai, J., Toh‐e, A., Matsui, Y., & Tamanoi, F. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3580 · Cited by 192
Powering through ribosome assembly
Strunk, B. S., & Karbstein, K. (2009) · RNA · doi:10.1261/rna.1792109 · Cited by 191
Whitehead, I. P., Kirk, H., Tognon, C. E., Trigo‐Gonzalez, G., & Kay, R. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.31.18388 · Cited by 191
Wakasugi, K., Nakano, T., & Morishima, I. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305519200 · Cited by 190
Park, H.-O., Bi, E., Pringle, J. R., & Herskowitz, I. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4463 · Cited by 190
Mossessova, E., Gulbis, J. M., & Goldberg, J. D. (1998) · Cell · doi:10.1016/s0092-8674(00)80933-2 · Cited by 190
Maier, T., Jacobi, A., Sauter, M., & Böck, A. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.3.630-635.1993 · Cited by 189
Buyse, I. M., Shao, G. Q., & Huang, S. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4467 · Cited by 189
Identification of effector-activating residues of Gsα
Berlot, C. H., & Bourne, H. R. (1992) · Cell · doi:10.1016/0092-8674(92)90034-a · Cited by 189
Self-citationArendt, T. (2003) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2003.09.007 · Cited by 189
TrioGEF1 controls Rac- and Cdc42-dependent cell structures through the direct activation of RhoG
Blangy, A., Vignal, E., Schmidt, S., Debant, A., Gauthier‐Rouvière, C., & Fort, P. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.4.729 · Cited by 188
KRAS G12C Game of Thrones, which direct KRAS inhibitor will claim the iron throne?
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Gröb, T., Seybert, G., Massa, W., Weller, F., Palaniswami, R., Greiner, A., & Dehnicke, K. (2000) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20001201)39:23 · Cited by 33
Cheon, C.-I., Lee, N. G., Siddique, A. B., Bal, A. K., & Verma, D. P. S. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06096.x · Cited by 187
Sheng, H., Williams, C. S., Shao, J., Liang, P., DuBois, R. N., & Beauchamp, R. D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.34.22120 · Cited by 186
Hajdu-Cronin, Y. M., Chen, W. J., Patikoglou, G. A., Koelle, M. R., & Sternberg, P. W. (1999) · Genes & Development · doi:10.1101/gad.13.14.1780 · Cited by 185
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Goitre, L., Trapani, E., Trabalzini, L., & Retta, S. F. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-791-4_1 · Cited by 195
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Shirayama, M., Matsui, Y., & Toh‐e, A. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.11.7476 · Cited by 185
Miller, J. D., Wilhelm, H., Gierasch, L. M., Gilmore, R., & Walter, P. (1993) · Nature · doi:10.1038/366351a0 · Cited by 185
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Morimoto, T., Loh, P. C., Hirai, T., Asai, K., Kobayashi, K., Moriya, S., & Ogasawara, N. (2002) · Microbiology · doi:10.1099/00221287-148-11-3539 · Cited by 191
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Khosravi‐Far, R., Campbell, S. L., Rossman, K. L., & Der, C. J. (1997) · Advances in cancer research · doi:10.1016/s0065-230x(08)60700-9 · Cited by 182
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Saveanu, C., Bienvenu, D., Namane, A., Gleizes, P., Gas, N., Jacquier, A., & Fromont‐Racine, M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.22.6475 · Cited by 183
Arellano, M., Durán, A., & Pérez, P. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00836.x · Cited by 183
Medema, R. H., de Vries-Smits, A. M. M., van der Zon, G. C. M., Maassen, J. A., & Bos, J. L. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.155-162.1993 · Cited by 183
Theriot, J. A., & Mitchison, T. J. (1993) · Cell · doi:10.1016/0092-8674(93)90527-w · Cited by 183
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Pitossi, F. J., Blank, A., Schröder, A., Schwarz, A., Hüssi, P., Schwemmle, M., Pavlovic, J., & Staeheli, P. (1993) · Journal of Virology · doi:10.1128/jvi.67.11.6726-6732.1993 · Cited by 180
Geyer, M., & Wittinghofer, A. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80147-9 · Cited by 182
Kadowaki, T., Goldfarb, D. S., Spitz, L., Tartakoff, A. M., & Ohno, M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05955.x · Cited by 182
Leyte, A., Barr, F. A., Kehlenbach, R. H., & Huttner, W. Β. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05585.x · Cited by 182
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Grand, R. J. A., & Owen, D. (1991) · Biochemical Journal · doi:10.1042/bj2790609 · Cited by 181
Eastwood, M., Mudera, V., McGrouther, D. A., & Brown, R. (1998) · Cell Motility and the Cytoskeleton · doi:10.1002/(sici)1097-0169(1998)40:1 · Cited by 337
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Lichtarge, O., Bourne, H. R., & Cohen, F. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.7507 · Cited by 180
Self-citationDexamethasone Rapidly Induces a Novel Ras Superfamily Member-related Gene in AtT-20 Cells
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Clark, G. J., Kinch, M. S., Rogers-Graham, K., Sebti, S. M., Hamilton, A. D., & Der, C. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.16.10608 · Cited by 177
Barlowe, C. K., d’Enfert, C., & Schekman, R. W. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54015-1 · Cited by 178
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Maguire, J. E., Santoro, T. J., Jensen, P. N., Siebenlist, U. K., Yewdell, J. W., & Kelly, K. (1994) · Science · doi:10.1126/science.7912851 · Cited by 178
Recognizing and Defining True Ras Binding Domains I: Biochemical Analysis
Wohlgemuth, S., Kiel, C., Kraemer, A., Serrano, L. G., Wittinghofer, F., & Herrmann, C. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.048 · Cited by 180
Separate GTP Binding and GTPase Activating Domains of a Gα Subunit
Markby, D. W., Onrust, R., & Bourne, H. R. (1993) · Science · doi:10.1126/science.8266082 · Cited by 179
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Metadata
- Authors
- Bourne, H. R., Sanders, D. A., & McCormick, F.
- Affiliations
- University of California, San Francisco (US)
- Whitehead Institute for Biomedical Research (US)
- Venue
- Nature
- Published
- 1991-01-10
- Volume
- 349
- Issue
- 6305
- Pages
- 117-127
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1977598234
- Cited by
- 3,392
- References
- 149
- Citations by year
- 2026: 24 · 2025: 44 · 2024: 51 · 2023: 52 · 2022: 37 · 2021: 55 · 2020: 62 · 2019: 50 · 2018: 48 · 2017: 44 · 2016: 58 · 2015: 56 · 2014: 63 · 2013: 61 · 2012: 69
- FWCI
- 30.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- GTPase, GTPase superfamily, molecular switches, structure-function relationship, molecular mechanisms, crystal structure, molecular genetics
- MeSH terms
- Amino Acid Sequence, Animals, Guanosine Diphosphate, Guanosine Triphosphate, Humans, Molecular Sequence Data, Peptide Elongation Factors, Peptide Initiation Factors, Protein Conformation, Protein Processing, Post-Translational, Signal Transduction, Proto-Oncogene Proteins p21(ras), GTP-Binding Proteins, GTP Phosphohydrolase-Linked Elongation Factors
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