메뉴 건너뛰기




Volumn 48, Issue 4, 2001, Pages 829-850

Structure of small G proteins and their regulators

Author keywords

GAP; GDI; GEF; GTPase; Protein tertiary structure; Protein protein interaction; Ras; Rho; Small G protein

Indexed keywords

EUKARYOTA; PROTOZOA;

EID: 0035756318     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2001_3850     Document Type: Review
Times cited : (129)

References (100)
  • 1
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H.R., Sanders, D.A. & McCormick, F. (1990) The GTPase superfamily: A conserved switch for diverse cell functions. Nature 348, 125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 0026026818 scopus 로고
    • The GTPase superfamily: A conserved structure and molecular mechanism
    • Bourne, H.R., Sanders, D.A. & McCormick, F. (1991) The GTPase superfamily: A conserved structure and molecular mechanism. Nature 349, 117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 4
    • 0025908897 scopus 로고
    • The ras protein family: Evolutionary tree and role of conserved amino acids
    • Valencia, A., Chardin, P., Wittinghofer, A. & Sander, C. (1991) The ras protein family: Evolutionary tree and role of conserved amino acids. Biochemistry 30, 4637-4648.
    • (1991) Biochemistry , vol.30 , pp. 4637-4648
    • Valencia, A.1    Chardin, P.2    Wittinghofer, A.3    Sander, C.4
  • 6
    • 0025254314 scopus 로고
    • RAS2 protein of Saccharomyces cerevisiae undergoes removal of methionine at N terminus and removal of three amino acids at C terminus
    • Fujiyama, A. & Tamanoi, F. (1990) RAS2 protein of Saccharomyces cerevisiae undergoes removal of methionine at N terminus and removal of three amino acids at C terminus. J. Biol. Chem. 265, 3362-3368.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3362-3368
    • Fujiyama, A.1    Tamanoi, F.2
  • 7
    • 0024465343 scopus 로고
    • Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis
    • Gutierrez, L., Magee, A.I., Marshall, C.J. & Hancock, J.F. (1989) Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis. EMBO J. 8, 1093-1098.
    • (1989) EMBO J. , vol.8 , pp. 1093-1098
    • Gutierrez, L.1    Magee, A.I.2    Marshall, C.J.3    Hancock, J.F.4
  • 8
    • 0024316475 scopus 로고
    • Genetic and pharmacological suppression of oncogenic mutations in ras genes of yeast and humans
    • Schafer, W.R., Kim, R., Sterne, R., Thorner, J., Kim, S.H. & Rine, J. (1989) Genetic and pharmacological suppression of oncogenic mutations in ras genes of yeast and humans. Science 245, 379-385.
    • (1989) Science , vol.245 , pp. 379-385
    • Schafer, W.R.1    Kim, R.2    Sterne, R.3    Thorner, J.4    Kim, S.H.5    Rine, J.6
  • 9
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock, J.F., Magee, A.I., Childs, J.E. & Marshall, C.J. (1989) All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57, 1167-1177.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 11
    • 0345482977 scopus 로고
    • GTP-binding domain: Three consensus sequence elements with distinct spacing
    • Dever, T.E., Glynias, M.J. & Merrick, W.C. (1987) GTP-binding domain: Three consensus sequence elements with distinct spacing. Proc. Natl. Acad. Sci. U.S.A. 84, 1814-1818.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 1814-1818
    • Dever, T.E.1    Glynias, M.J.2    Merrick, W.C.3
  • 12
    • 0022394955 scopus 로고
    • Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins
    • Jurnak, F. (1985) Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins. Science 230, 32-36.
    • (1985) Science , vol.230 , pp. 32-36
    • Jurnak, F.1
  • 13
    • 0022124319 scopus 로고
    • 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., Nyborg, J., Thirup, S. & Clark, B.F. (1985) Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography. EMBO J. 4, 2385-2388.
    • (1985) EMBO J. , vol.4 , pp. 2385-2388
    • La Cour, T.F.1    Nyborg, J.2    Thirup, S.3    Clark, B.F.4
  • 14
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman, A.G. (1987) G proteins: Transducers of receptor-generated signals. Annu. Rev. Biochem. 56, 615-649.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 15
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha-and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J. & Gay, N.J. (1982) Distantly related sequences in the alpha-and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 16
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang, S.R. (1997) G protein mechanisms: Insights from structural analysis. Annu. Rev. Biochem. 66, 639-678.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 18
    • 0029665424 scopus 로고    scopus 로고
    • Conformational transitions in p21ras and in its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP
    • Geyer, M., Schweins, T., Herrmann, C., Prisner, T., Wittinghofer, A. & Kalbitzer, H.R. (1996) Conformational transitions in p21ras and in its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP. Biochemistry 35, 10308-10320.
    • (1996) Biochemistry , vol.35 , pp. 10308-10320
    • Geyer, M.1    Schweins, T.2    Herrmann, C.3    Prisner, T.4    Wittinghofer, A.5    Kalbitzer, H.R.6
  • 19
    • 0032552972 scopus 로고    scopus 로고
    • The role of ligand binding in the kinetic folding mechanism of human p21(H-ras) protein
    • Zhang, J. & Matthews, C.R. (1998) The role of ligand binding in the kinetic folding mechanism of human p21(H-ras) protein. Biochemistry 37, 14891-14899.
    • (1998) Biochemistry , vol.37 , pp. 14891-14899
    • Zhang, J.1    Matthews, C.R.2
  • 20
    • 0032552966 scopus 로고    scopus 로고
    • Ligand binding is the principal determinant of stability for the p21(H)-ras protein
    • Zhang, J. & Matthews, C.R. (1998) Ligand binding is the principal determinant of stability for the p21(H)-ras protein. Biochemistry 37, 14881-14890.
    • (1998) Biochemistry , vol.37 , pp. 14881-14890
    • Zhang, J.1    Matthews, C.R.2
  • 22
    • 0028556994 scopus 로고
    • Structure of the human ADP-ribosylation factor 1 complexed with GDP
    • Amor, J.C., Harrison, D.H., Kahn, R.A. & Ringe, D. (1994) Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature 372, 704-708.
    • (1994) Nature , vol.372 , pp. 704-708
    • Amor, J.C.1    Harrison, D.H.2    Kahn, R.A.3    Ringe, D.4
  • 23
    • 0028929866 scopus 로고
    • Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form
    • Scheffzek, K., Klebe, C., Fritz-Wolf, K., Kabsch, W. & Wittinghofer, A. (1995) Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form. Nature 374, 378-381.
    • (1995) Nature , vol.374 , pp. 378-381
    • Scheffzek, K.1    Klebe, C.2    Fritz-Wolf, K.3    Kabsch, W.4    Wittinghofer, A.5
  • 24
    • 0029958571 scopus 로고    scopus 로고
    • The GTP binding motif: Variations on a theme
    • Kjeldgaard, M., Nyborg, J. & Clark, B.F.C. (1996) The GTP binding motif: Variations on a theme. FASEB J. 10, 1347-1368.
    • (1996) FASEB J. , vol.10 , pp. 1347-1368
    • Kjeldgaard, M.1    Nyborg, J.2    Clark, B.F.C.3
  • 30
    • 0028988578 scopus 로고
    • Interactions between the amino-and carboxyl-terminal regions of G alpha subunits: Analysis of mutated G alpha o/G alpha i2 chimeras
    • Denker, B.M., Boutin, P.M. & Neer, E.J. (1995) Interactions between the amino-and carboxyl-terminal regions of G alpha subunits: Analysis of mutated G alpha o/G alpha i2 chimeras. Biochemistry 34, 5544-5553.
    • (1995) Biochemistry , vol.34 , pp. 5544-5553
    • Denker, B.M.1    Boutin, P.M.2    Neer, E.J.3
  • 31
    • 0028960178 scopus 로고
    • Switching nucleotide specificity of Ha-Ras p21 by a single amino acid substitution at aspartate 119
    • Zhong, J.M., Chen-Hwang, M.C. & Hwang, Y.W. (1995) Switching nucleotide specificity of Ha-Ras p21 by a single amino acid substitution at aspartate 119. J. Biol Chem. 270, 10002-10007.
    • (1995) J. Biol Chem. , vol.270 , pp. 10002-10007
    • Zhong, J.M.1    Chen-Hwang, M.C.2    Hwang, Y.W.3
  • 32
    • 0030046054 scopus 로고    scopus 로고
    • Biochemical and biological consequences of changing the specificity of p21ras from guanosine to xanthosine nucleotides
    • Schmidt, G., Lenzen, C., Simon, I., Deuter, R., Cool, R.H., Goody, R.S. & Wittinghofer, A. (1996) Biochemical and biological consequences of changing the specificity of p21ras from guanosine to xanthosine nucleotides. Oncogene 12, 87-96.
    • (1996) Oncogene , vol.12 , pp. 87-96
    • Schmidt, G.1    Lenzen, C.2    Simon, I.3    Deuter, R.4    Cool, R.H.5    Goody, R.S.6    Wittinghofer, A.7
  • 33
    • 0028064521 scopus 로고
    • Elongation factor Tu D138N, a mutant with modified substrate specificity, as a tool to study energy consumption in protein biosynthesis
    • Weijland, A., Parlato, G. & Parmeggiani, A. (1994) Elongation factor Tu D138N, a mutant with modified substrate specificity, as a tool to study energy consumption in protein biosynthesis. Biochemistry 33, 10711-10717.
    • (1994) Biochemistry , vol.33 , pp. 10711-10717
    • Weijland, A.1    Parlato, G.2    Parmeggiani, A.3
  • 34
    • 0028868377 scopus 로고
    • X-ray crystal structure analysis of the catalytic domain of the oncogene product p21H-ras complexed with caged GTP and mant dGppNHp
    • Scheidig, A.J., Franken, S.M., Corrie, J.E., Reid, G.P., Wittinghofer, A., Pai, E.F. & Goody, R.S. (1995) X-ray crystal structure analysis of the catalytic domain of the oncogene product p21H-ras complexed with caged GTP and mant dGppNHp. J. Mol. Biol. 253, 132-150.
    • (1995) J. Mol. Biol. , vol.253 , pp. 132-150
    • Scheidig, A.J.1    Franken, S.M.2    Corrie, J.E.3    Reid, G.P.4    Wittinghofer, A.5    Pai, E.F.6    Goody, R.S.7
  • 37
  • 39
    • 0035282079 scopus 로고    scopus 로고
    • Substrate assisted catalysis - Application to G proteins
    • Kosloff, M. & Selinger, Z. (2001) Substrate assisted catalysis - application to G proteins. Trends Biochem. Sci. 26, 161-166.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 161-166
    • Kosloff, M.1    Selinger, Z.2
  • 40
    • 0029843561 scopus 로고    scopus 로고
    • Mechanistic analysis of the relationships in p21ras and related systems
    • Schweins, T. & Warshel, A. (1996) Mechanistic analysis of the relationships in p21ras and related systems. Biochemistry 35, 14232-14243.
    • (1996) Biochemistry , vol.35 , pp. 14232-14243
    • Schweins, T.1    Warshel, A.2
  • 41
    • 0029781354 scopus 로고    scopus 로고
    • Ras-catalyzed hydrolysis of GTP: A new perspective from model studies
    • Maegley, K.A., Admiral, S.J., Herschlag, D. (1996) Ras-catalyzed hydrolysis of GTP: A new perspective from model studies. Proc. Natl. Acad. Sci. U.S.A. 94, 8160-8166.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8160-8166
    • Maegley, K.A.1    Admiral, S.J.2    Herschlag, D.3
  • 43
    • 0035933139 scopus 로고    scopus 로고
    • The arginine finger of RasGAP helps Gin-61 align the nucleophilic water in GAP-stimulate hydrolysis of GTP
    • Resat, H., Straatsma, T.P., Dixon, D.A. & Miller, J.H. (2001) The arginine finger of RasGAP helps Gin-61 align the nucleophilic water in GAP-stimulate hydrolysis of GTP. Proc. Natl. Acad. Sci. U.S.A. 98, 6033-6038.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6033-6038
    • Resat, H.1    Straatsma, T.P.2    Dixon, D.A.3    Miller, J.H.4
  • 46
    • 0035852966 scopus 로고    scopus 로고
    • Ras catalyzes GTP hydrolysis by shifting negative charges from gamma-to beta-phosphate as revealed by time-resolved FTIR difference spectroscopy
    • Allin, C. & Gerwert, K. (2001) Ras catalyzes GTP hydrolysis by shifting negative charges from gamma-to beta-phosphate as revealed by time-resolved FTIR difference spectroscopy. Biochemistry 40, 3037-3046.
    • (2001) Biochemistry , vol.40 , pp. 3037-3046
    • Allin, C.1    Gerwert, K.2
  • 49
    • 0032589269 scopus 로고    scopus 로고
    • Effectors for the Rho GTPases
    • Aspenstrom, P. (1999) Effectors for the Rho GTPases. Curr. Opin. Cell. Biol. 11, 95-102.
    • (1999) Curr. Opin. Cell. Biol. , vol.11 , pp. 95-102
    • Aspenstrom, P.1
  • 50
    • 0033563754 scopus 로고    scopus 로고
    • Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA
    • Maesaki, R., Shimizu, T., Ihara, K., Kuroda, S., Kaibuchi, K. & Hakoshima, T. (1999) Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA. J. Struct. Biol. 126, 166-170.
    • (1999) J. Struct. Biol. , vol.126 , pp. 166-170
    • Maesaki, R.1    Shimizu, T.2    Ihara, K.3    Kuroda, S.4    Kaibuchi, K.5    Hakoshima, T.6
  • 51
    • 0028963150 scopus 로고
    • Mutagenesis of the H-ras p21 at glycine-60 residue disrupts GTP-induced conformational change
    • Sung, Y.J., Carter, M., Zhong, J.M. & Hwang, Y.W. (1995) Mutagenesis of the H-ras p21 at glycine-60 residue disrupts GTP-induced conformational change. Biochemistry 34, 3470-3477.
    • (1995) Biochemistry , vol.34 , pp. 3470-3477
    • Sung, Y.J.1    Carter, M.2    Zhong, J.M.3    Hwang, Y.W.4
  • 53
    • 0029913467 scopus 로고    scopus 로고
    • Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor
    • Herrmann, C., Horn, G., Spaargaren, M. & Wittinghofer, A. (1996) Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor. J. Biol. Chem. 271, 6794-6800.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6794-6800
    • Herrmann, C.1    Horn, G.2    Spaargaren, M.3    Wittinghofer, A.4
  • 55
    • 0031228462 scopus 로고    scopus 로고
    • Structure of the Ras-binding domain of Ral guanine-nucleotide exchange factor: Implications for Ras binding and signaling
    • Geyer, M., Herrmann, C., Wohlgemuth, S., Wittinghofer, A. & Kalbitzer, H.R. (1997) Structure of the Ras-binding domain of Ral guanine-nucleotide exchange factor: Implications for Ras binding and signaling. Nat. Struct. Biol. 4, 694-699.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 694-699
    • Geyer, M.1    Herrmann, C.2    Wohlgemuth, S.3    Wittinghofer, A.4    Kalbitzer, H.R.5
  • 57
    • 0029107760 scopus 로고
    • The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
    • Nassar, N., Horn, G., Herrmann, C., Scherer, A., McCormick, F. & Wittinghofer, A. (1995) The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature 375, 554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 59
    • 0028073606 scopus 로고
    • Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
    • Freed, E., Symons, M., MacDonald, S.G., McCormick, F. & Ruggieri, R. (1994) Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 265, 1713-1716.
    • (1994) Science , vol.265 , pp. 1713-1716
    • Freed, E.1    Symons, M.2    MacDonald, S.G.3    McCormick, F.4    Ruggieri, R.5
  • 61
    • 0029850713 scopus 로고    scopus 로고
    • KSR modulates signal propagation within the MAPK cascade
    • Therrien, M., Michaud, N.R., Rubin, G.M. & Morrison, D.K. (1996) KSR modulates signal propagation within the MAPK cascade. Genes Dev. 10, 2684-2695.
    • (1996) Genes Dev. , vol.10 , pp. 2684-2695
    • Therrien, M.1    Michaud, N.R.2    Rubin, G.M.3    Morrison, D.K.4
  • 62
    • 0032582663 scopus 로고    scopus 로고
    • CNK, a RAF-binding multidomain protein required for RAS signaling
    • Therrien, M., Wong, A.M. & Rubin, G.M. (1998) CNK, a RAF-binding multidomain protein required for RAS signaling. Cell 95, 343-353.
    • (1998) Cell , vol.95 , pp. 343-353
    • Therrien, M.1    Wong, A.M.2    Rubin, G.M.3
  • 63
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop, A.L. & Hall, A. (2000) Rho GTPases and their effector proteins. Biochem. J. 348, 241-255.
    • (2000) Biochem. J. , vol.348 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 65
    • 0034644537 scopus 로고    scopus 로고
    • Ras and Rho GTPases: A family reunion
    • Bar-Sagi, D. & Hall, A. (2000) Ras and Rho GTPases: A family reunion. Cell 103, 227-238.
    • (2000) Cell , vol.103 , pp. 227-238
    • Bar-Sagi, D.1    Hall, A.2
  • 67
    • 0030992879 scopus 로고    scopus 로고
    • C-terminal binding domain of RhoGDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases
    • Gosser, Y.Q., Nomanbhoy, T.K., Aghazadeh, B., Manor, D., Combs, C., Cerione, R.A. & Rosen, M.K. (1997) C-terminal binding domain of RhoGDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases. Nature 387, 814-819.
    • (1997) Nature , vol.387 , pp. 814-819
    • Gosser, Y.Q.1    Nomanbhoy, T.K.2    Aghazadeh, B.3    Manor, D.4    Combs, C.5    Cerione, R.A.6    Rosen, M.K.7
  • 68
    • 0343750716 scopus 로고    scopus 로고
    • The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI
    • Scheffzek, K., Stephan, I., Jensen, O.N., Illenberger, D. & Gierschik, P. (2000) The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. Nat. Struct. Biol. 7, 122-126.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 122-126
    • Scheffzek, K.1    Stephan, I.2    Jensen, O.N.3    Illenberger, D.4    Gierschik, P.5
  • 69
    • 0031570337 scopus 로고    scopus 로고
    • A modulator of rho family G proteins, RhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm
    • Keep, N.H., Barnes, M., Barsukov, I., Badii, R., Lian, L.Y., Segal, A.W., Moody, P.C.E. & Roberts, G.C.K. (1997) A modulator of rho family G proteins, RhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm. Structure 5, 623-633.
    • (1997) Structure , vol.5 , pp. 623-633
    • Keep, N.H.1    Barnes, M.2    Barsukov, I.3    Badii, R.4    Lian, L.Y.5    Segal, A.W.6    Moody, P.C.E.7    Roberts, G.C.K.8
  • 72
    • 0029951250 scopus 로고    scopus 로고
    • Defective Rho GTPase regulation by IL-1 beta-converting enzyme-mediated cleavage of D4 GDP dissociation inhibitor
    • Danley, D.E., Chuang, T.H. & Bokoch, G.M. (1996) Defective Rho GTPase regulation by IL-1 beta-converting enzyme-mediated cleavage of D4 GDP dissociation inhibitor. J. Immunol. 157, 500-503.
    • (1996) J. Immunol. , vol.157 , pp. 500-503
    • Danley, D.E.1    Chuang, T.H.2    Bokoch, G.M.3
  • 73
    • 0030001665 scopus 로고    scopus 로고
    • Characterization of the interaction between RhoGDI and Cdc42Hs using fluorescence spectroscopy
    • Nomanbhoy, T.K. & Cerione, R. (1996) Characterization of the interaction between RhoGDI and Cdc42Hs using fluorescence spectroscopy. J. Biol. Chem. 271, 10004-10009.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10004-10009
    • Nomanbhoy, T.K.1    Cerione, R.2
  • 74
    • 0029829561 scopus 로고    scopus 로고
    • Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras
    • Scheffzek, K., Lautwein, A., Kabsch, W., Ahmadian, M.R. & Wittinghofer, A. (1996) Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras. Nature 384, 591-596.
    • (1996) Nature , vol.384 , pp. 591-596
    • Scheffzek, K.1    Lautwein, A.2    Kabsch, W.3    Ahmadian, M.R.4    Wittinghofer, A.5
  • 75
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition state analog
    • Rittinger, K., Walker, P.A., Eccleston, J.F., Smerdon, S.J. & Gambin, S.J. (1997) Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition state analog. Nature 389, 758-762.
    • (1997) Nature , vol.389 , pp. 758-762
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gambin, S.J.5
  • 77
    • 0034647989 scopus 로고    scopus 로고
    • Functional specificity conferred by the unique plasticity of fully alpha-helical Ras and Rho GAPs
    • Souchet, M., Poupon, A., Callebaut, I., Leger, I., Mornon, J., Bril, A. & Calmels, T.P. (2000) Functional specificity conferred by the unique plasticity of fully alpha-helical Ras and Rho GAPs. FEBS Lett. 477, 99-105.
    • (2000) FEBS Lett. , vol.477 , pp. 99-105
    • Souchet, M.1    Poupon, A.2    Callebaut, I.3    Leger, I.4    Mornon, J.5    Bril, A.6    Calmels, T.P.7
  • 79
    • 0034634476 scopus 로고    scopus 로고
    • The Ras/p120 GTPase-activating protein (GAP) interaction is regulated by the p120 GAP pleckstrin homology domain
    • Drugan, J.K., Rogers-Graham, K., Gilmer, T., Campbell, S. & Clark, G.J. (2000) The Ras/p120 GTPase-activating protein (GAP) interaction is regulated by the p120 GAP pleckstrin homology domain. J. Biol. Chem. 275, 35021-35027.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35021-35027
    • Drugan, J.K.1    Rogers-Graham, K.2    Gilmer, T.3    Campbell, S.4    Clark, G.J.5
  • 81
    • 0035917523 scopus 로고    scopus 로고
    • Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1)
    • Renault, L., Kuhlmann, J., Henkel, A. & Wittinghofer, A. (2001) Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1). Cell 105, 245-255.
    • (2001) Cell , vol.105 , pp. 245-255
    • Renault, L.1    Kuhlmann, J.2    Henkel, A.3    Wittinghofer, A.4
  • 84
    • 0029099915 scopus 로고
    • Structure of guanine-nucleotide-exchange factor human Mss4 and identification of its Rab-interacting surface
    • Yu, H. & Schreiber, S.L. (1995) Structure of guanine-nucleotide-exchange factor human Mss4 and identification of its Rab-interacting surface. Nature 376, 788-791.
    • (1995) Nature , vol.376 , pp. 788-791
    • Yu, H.1    Schreiber, S.L.2
  • 86
    • 0033772512 scopus 로고    scopus 로고
    • Activation of Rho GEF activity by G alpha 13
    • Hart, M.J., Roscoe, W. & Bollag, G. (2000) Activation of Rho GEF activity by G alpha 13. Methods Enzymol. 325, 61-71.
    • (2000) Methods Enzymol. , vol.325 , pp. 61-71
    • Hart, M.J.1    Roscoe, W.2    Bollag, G.3
  • 87
    • 0033605294 scopus 로고    scopus 로고
    • A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho
    • Fukuhara, S., Murga, C., Zohar, M., Igishi, T. & Gutkind, J.S. (1999) A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho. J. Biol. Chem. 274, 5868-5879.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5868-5879
    • Fukuhara, S.1    Murga, C.2    Zohar, M.3    Igishi, T.4    Gutkind, J.S.5
  • 88
    • 0027958423 scopus 로고
    • Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product
    • Hart, M.J., Eva, A., Zangrilli, D., Aaronson, S.A., Evans, T., Cerione, R.A. & Zheng, Y. (1994) Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product. J. Biol. Chem. 269, 62-65.
    • (1994) J. Biol. Chem. , vol.269 , pp. 62-65
    • Hart, M.J.1    Eva, A.2    Zangrilli, D.3    Aaronson, S.A.4    Evans, T.5    Cerione, R.A.6    Zheng, Y.7
  • 89
    • 0030451173 scopus 로고    scopus 로고
    • The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factor
    • Zheng, Y., Fischer, D.J., Santos, M.F., Tigyi, G., Pasteris, N.G., Gorski, J.L. & Xu, Y. (1996) The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factor. J. Biol. Chem. 271, 33169-33172.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33169-33172
    • Zheng, Y.1    Fischer, D.J.2    Santos, M.F.3    Tigyi, G.4    Pasteris, N.G.5    Gorski, J.L.6    Xu, Y.7
  • 91
    • 0028110120 scopus 로고
    • A novel oncogene, ost, encodes a guanine nucleotide exchange factor that potentially links Rho and Rac signaling pathways
    • Horii, Y., Beeler, J.F., Sakaguchi, K., Tachibana, M. & Miki, T. (1994) A novel oncogene, ost, encodes a guanine nucleotide exchange factor that potentially links Rho and Rac signaling pathways. EMBO J. 13, 4776-4786.
    • (1994) EMBO J. , vol.13 , pp. 4776-4786
    • Horii, Y.1    Beeler, J.F.2    Sakaguchi, K.3    Tachibana, M.4    Miki, T.5
  • 93
    • 0027183541 scopus 로고
    • The PH domain: A common piece in the structural patchwork of signalling proteins
    • Musacchio, A., Gibson, T., Rice, P., Thompson, J. & Saraste, M. (1993) The PH domain: A common piece in the structural patchwork of signalling proteins. Trends Biochem. Sci. 18, 343-348.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 343-348
    • Musacchio, A.1    Gibson, T.2    Rice, P.3    Thompson, J.4    Saraste, M.5
  • 95
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. (1995) Protein modules and signalling networks. Nature 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 97
    • 0032538316 scopus 로고    scopus 로고
    • Crystal structure of the Dbl and pleckstrin homology domains from the human son of sevenless protein
    • Soisson, S.M., Nimnual, A.S., Uy, M., Bar-Sagi, D. & Kuriyan, J. (1998) Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein. Cell 95, 259-268.
    • (1998) Cell , vol.95 , pp. 259-268
    • Soisson, S.M.1    Nimnual, A.S.2    Uy, M.3    Bar-Sagi, D.4    Kuriyan, J.5
  • 98
    • 0030729024 scopus 로고    scopus 로고
    • The solution structure of the pleckstrin homology domain of human SOS1. A possible structural role for the sequential association of diffuse B cell lymphoma and pleckstrin homology domains
    • Zheng, J., Chen, R.H., Corblan-Garcia, S., Cahill, S.M., Bar-Sagi, D. & Cowburn, D. (1997) The solution structure of the pleckstrin homology domain of human SOS1. A possible structural role for the sequential association of diffuse B cell lymphoma and pleckstrin homology domains. J. Biol. Chem. 272, 30340-30344.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30340-30344
    • Zheng, J.1    Chen, R.H.2    Corblan-Garcia, S.3    Cahill, S.M.4    Bar-Sagi, D.5    Cowburn, D.6
  • 99
    • 0034682668 scopus 로고    scopus 로고
    • 2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins
    • 2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins. J. Biol. Chem. 275, 25299-25307.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25299-25307
    • Zhang, B.1    Zhang, Y.2    Wang, Z.3    Zheng, Y.4
  • 100
    • 0033179296 scopus 로고    scopus 로고
    • GEFs: Structural basis for their activation of small GTP-binding proteins
    • Cherfils, J. & Chardin, P. (1999) GEFs: Structural basis for their activation of small GTP-binding proteins. Trends Biochem. Sci. 24, 306-311.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 306-311
    • Cherfils, J.1    Chardin, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.