메뉴 건너뛰기




Volumn 4, Issue 5, 1999, Pages 793-803

The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE; RHO FACTOR;

EID: 0033231561     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80389-5     Document Type: Article
Times cited : (141)

References (65)
  • 1
    • 0033609388 scopus 로고    scopus 로고
    • Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein
    • Abdul-Manan, N., Aghazadeh, B., Liu, G.A., Majumdar, A., Ouerfelli, O., Siminovitch, K.A., and Rosen, M.K. (1999). Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein. Nature 399, 379-383.
    • (1999) Nature , vol.399 , pp. 379-383
    • Abdul-Manan, N.1    Aghazadeh, B.2    Liu, G.A.3    Majumdar, A.4    Ouerfelli, O.5    Siminovitch, K.A.6    Rosen, M.K.7
  • 2
    • 0032502680 scopus 로고    scopus 로고
    • Analysis of RhoA binding proteins reveals an interaction domain conserved in heterotrimeric G protein β subunits and the yeast response regulator protein Skn7
    • Alberts, A.S., Bouquin, N., Johnston, L.H., and Treisman, R. (1998). Analysis of RhoA binding proteins reveals an interaction domain conserved in heterotrimeric G protein β subunits and the yeast response regulator protein Skn7. J. Biol. Chem. 273, 8616-8622.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8616-8622
    • Alberts, A.S.1    Bouquin, N.2    Johnston, L.H.3    Treisman, R.4
  • 5
    • 0021062575 scopus 로고
    • Solvent-induced distortions and the curvature of α helices
    • Blundell, T., Barlow, D., Borkakoti, N.S., and Thornton, J. (1983). Solvent-induced distortions and the curvature of α helices. Nature 306, 281-283.
    • (1983) Nature , vol.306 , pp. 281-283
    • Blundell, T.1    Barlow, D.2    Borkakoti, N.S.3    Thornton, J.4
  • 7
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo, P.D., Drechsel, D., and Hall, A. (1995). A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270, 29071-29074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 8
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-b2-Ran. GppNHp
    • Chook, Y.M., and Blobel, G. (1999). Structure of the nuclear transport complex karyopherin-b2-Ran. GppNHp. Nature 399, 230-237.
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 9
    • 0025043116 scopus 로고
    • A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å
    • Cusack, S., Berthet-Colominas, C., Hartlein, M., Nassar, N., and Leberman, R. (1990). A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å. Nature 347, 249-255.
    • (1990) Nature , vol.347 , pp. 249-255
    • Cusack, S.1    Berthet-Colominas, C.2    Hartlein, M.3    Nassar, N.4    Leberman, R.5
  • 10
  • 12
    • 0032579489 scopus 로고    scopus 로고
    • Multiple interactions of PRK1 with RhoA: Functional assignment of the HR1 repeat motif
    • Flynn, P., Mellor, H., Palmer, R., Panayotou, G., and Parker, P.J. (1998). Multiple interactions of PRK1 with RhoA: functional assignment of the HR1 repeat motif. J. Biol. Chem. 273, 2698-2705.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2698-2705
    • Flynn, P.1    Mellor, H.2    Palmer, R.3    Panayotou, G.4    Parker, P.J.5
  • 14
    • 0031228462 scopus 로고    scopus 로고
    • Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signaling
    • Geyer, M., Herrmann, C., Wohlgemuth, S., Wittinghofer, A., and Kalbitzer, H.R. (1997). Structure of the Ras-binding domain of RalGEF and 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
  • 15
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. (1998). Rho GTPases and the actin cytoskeleton. Science 279, 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 16
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L., and Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 17
    • 0030570801 scopus 로고    scopus 로고
    • Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor
    • Hotta, K., Tanaka, K., Mino, A., Kohno, H., and Takai, Y. (1996). Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor. Biochem. Biophys. Res. Commun. 225, 69-74.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 69-74
    • Hotta, K.1    Tanaka, K.2    Mino, A.3    Kohno, H.4    Takai, Y.5
  • 18
    • 0030863611 scopus 로고    scopus 로고
    • Three-dimensional structure of the Ras-interacting domain of ralgds
    • Huang, L., Weng, X., Hofer, F., Martin, G.S., and Kim, S.-H. (1997). Three-dimensional structure of the Ras-interacting domain of RalGDS. Nat. Struct. Biol. 4, 609-615.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 609-615
    • Huang, L.1    Weng, X.2    Hofer, F.3    Martin, G.S.4    Kim, S.-H.5
  • 19
    • 0031778630 scopus 로고    scopus 로고
    • Structural basis for the interaction of Ras with RaIGDS
    • Huang, L., Hofer, F., Martin, G.S., and Kim, S.-H. (1998). Structural basis for the interaction of Ras with RalGDS. Nat. Struct. Biol. 5, 422-426.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 422-426
    • Huang, L.1    Hofer, F.2    Martin, G.S.3    Kim, S.-H.4
  • 22
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 23
    • 0029802561 scopus 로고    scopus 로고
    • Rac regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase
    • Joneson, T., McDonough, M., Bar Sagi, D., and Van Aelst, L. (1996). Rac regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase. Science 274, 1374-1376.
    • (1996) Science , vol.274 , pp. 1374-1376
    • Joneson, T.1    McDonough, M.2    Bar Sagi, D.3    Van Aelst, L.4
  • 24
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells
    • Kaibuchi, K., Kuroda, S., and Amano, M. (1999). Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Annu. Rev. Biochem. 68, 459-486.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 459-486
    • Kaibuchi, K.1    Kuroda, S.2    Amano, M.3
  • 25
    • 0032530750 scopus 로고    scopus 로고
    • A protein kinase, PKN, accumulates in Alzheimer neurofibrillary tangles and associated endoplasmic reticulum-derived vesicles and phosphorylates tau protein
    • Kawamata, T., Taniguchi, T., Mukai, H., Kitagawa, M., Hashimoto, T., Maeda, K., Ono, Y., and Tanaka, C. (1998). A protein kinase, PKN, accumulates in Alzheimer neurofibrillary tangles and associated endoplasmic reticulum-derived vesicles and phosphorylates tau protein. J. Neurosci. 18, 7402-7410.
    • (1998) J. Neurosci. , vol.18 , pp. 7402-7410
    • Kawamata, T.1    Taniguchi, T.2    Mukai, H.3    Kitagawa, M.4    Hashimoto, T.5    Maeda, K.6    Ono, Y.7    Tanaka, C.8
  • 26
    • 0029996517 scopus 로고    scopus 로고
    • The role of the unique motifs in the amino-terminal region of PKN on its enzymatice activity
    • Kitagawa, M., Shibata, H., Toshimori, M., Mukai, H., and Ono, Y. (1996). The role of the unique motifs in the amino-terminal region of PKN on its enzymatice activity. Biochem. Biophys. Res. Commun. 220, 963-968.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 963-968
    • Kitagawa, M.1    Shibata, H.2    Toshimori, M.3    Mukai, H.4    Ono, Y.5
  • 27
    • 10544228528 scopus 로고    scopus 로고
    • Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae
    • Kohno, H., Tanaka, K., Mino, A., Umikawa, M., Imamura, H., Fujiwara, T., Fujita, Y., Hotta, K., Qadota, H., Watanabe, T., et al. (1996). Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae. EMBO J. 15, 6060-6068.
    • (1996) EMBO J. , vol.15 , pp. 6060-6068
    • Kohno, H.1    Tanaka, K.2    Mino, A.3    Umikawa, M.4    Imamura, H.5    Fujiwara, T.6    Fujita, Y.7    Hotta, K.8    Qadota, H.9    Watanabe, T.10
  • 28
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma, R., Ahmed, S., Best, A., and Lim, L. (1995). The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell. Biol. 15, 1942-1952.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 0030298138 scopus 로고    scopus 로고
    • Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade
    • Lamarche, N., Tapon, N., Stowers, L., Burbelo, P.D., Aspenstrom, P., Bridges, T., Chant, J., and Hall, A. (1996). Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade. Cell 87, 519-529.
    • (1996) Cell , vol.87 , pp. 519-529
    • Lamarche, N.1    Tapon, N.2    Stowers, L.3    Burbelo, P.D.4    Aspenstrom, P.5    Bridges, T.6    Chant, J.7    Hall, A.8
  • 31
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 32
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding of the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes
    • Leung, T., Manser, E., Tan, L., and Lim, L. (1995). A novel serine/threonine kinase binding of the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J. Biol. Chem. 270, 29051-29054.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29051-29054
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 33
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROKα is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung, T., Chen, X.Q., Manser, E., and Lim, L. (1996). The p160 RhoA-binding kinase ROKα is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16, 5313-5327.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 34
    • 0033135283 scopus 로고    scopus 로고
    • The Drosophila Pkn protein kinase is a Rho/Rac effector target required for dorsal closure during embryogenesis
    • Lu, Y., and Settleman, J. (1999). The Drosophila Pkn protein kinase is a Rho/Rac effector target required for dorsal closure during embryogenesis. Genes Dev. 13, 1168-1180.
    • (1999) Genes Dev. , vol.13 , pp. 1168-1180
    • Lu, Y.1    Settleman, J.2
  • 36
    • 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., and 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
  • 38
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras products
    • Milburn, M.V., Tong, L., De Vos, A.M., Brunger, A., Yamaizumi, Z., Nishimura, S., and Kim, S.-H. (1990). Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras products. Science 247, 939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    De Vos, A.M.3    Brunger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.-H.7
  • 39
    • 0033609335 scopus 로고    scopus 로고
    • Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK
    • Mott, H.R., Qwen, D., Nietlispach, D., Lowe, P.N., Manser, E., Lim, L., and Laue, E.D. (1999). Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK. Nature 399, 384-388.
    • (1999) Nature , vol.399 , pp. 384-388
    • Mott, H.R.1    Qwen, D.2    Nietlispach, D.3    Lowe, P.N.4    Manser, E.5    Lim, L.6    Laue, E.D.7
  • 41
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T., and Chothia, C. (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 42
    • 0030603119 scopus 로고    scopus 로고
    • ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice
    • Nakagawa, O., Fujisawa, K., Ishizaki, T., Saito, Y., Nakao, K., and Narumiya, S. (1996). ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice. FEBS Lett. 392, 189-193.
    • (1996) FEBS Lett. , vol.392 , pp. 189-193
    • Nakagawa, O.1    Fujisawa, K.2    Ishizaki, T.3    Saito, Y.4    Nakao, K.5    Narumiya, S.6
  • 43
    • 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., and 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
  • 44
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 45
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholis, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholis, A.1    Sharp, K.A.2    Honig, B.3
  • 46
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka, Y. (1995). Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9, 484-496.
    • (1995) FASEB J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 47
    • 0028961293 scopus 로고
    • Rho, Rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C.D., and Hall, A. (1995). Rho, Rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 48
    • 0033525215 scopus 로고    scopus 로고
    • Structural basis of Rab effector specificity: Crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A
    • Ostermeier, C., and Brunger, A.T. (1999). Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A. Cell 96, 363-374.
    • (1999) Cell , vol.96 , pp. 363-374
    • Ostermeier, C.1    Brunger, A.T.2
  • 49
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 50
    • 0028815490 scopus 로고
    • Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family
    • Palmer, R.H., Ridden, J., and Parker, P.J. (1995). Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family. Eur. J. Biochem. 227, 344-351.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 344-351
    • Palmer, R.H.1    Ridden, J.2    Parker, P.J.3
  • 51
    • 0029889591 scopus 로고    scopus 로고
    • Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain
    • Reid, T., Furuyashiki, T., Ishizaki, T., Watanabe, G., Watanabe, N., Fujisawa, K., Morii, N., Madaule, P., and Narumiya, S. (1996). Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain. J. Biol. Chem. 271, 13556-13560.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13556-13560
    • Reid, T.1    Furuyashiki, T.2    Ishizaki, T.3    Watanabe, G.4    Watanabe, N.5    Fujisawa, K.6    Morii, N.7    Madaule, P.8    Narumiya, S.9
  • 52
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A.J., and Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 53
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J., Paterson, H.F., Johnston, C.L., Diekmann, D., and Hall, A. (1992). The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70, 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 55
    • 0032473351 scopus 로고    scopus 로고
    • RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation
    • Sahai, E., Alberts, A.S., and Treisman, R. (1998). RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation. EMBO J. 17, 1350-1361.
    • (1998) EMBO J. , vol.17 , pp. 1350-1361
    • Sahai, E.1    Alberts, A.S.2    Treisman, R.3
  • 56
    • 0024353843 scopus 로고
    • Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase
    • Sekine, A., Fujiwara, M., and Narumiya, S. (1989). Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 264, 8602-8605.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8602-8605
    • Sekine, A.1    Fujiwara, M.2    Narumiya, S.3
  • 58
    • 0028840106 scopus 로고
    • Crystal structure of the GreA transcript cleavage factor from Escherichia coli
    • Stebbins, C.E., Borukhov, S., Orlova, M., Polyakov, A., Goldfarb, A., and Darst, S.A. (1995). Crystal structure of the GreA transcript cleavage factor from Escherichia coli. Nature 373, 636-640.
    • (1995) Nature , vol.373 , pp. 636-640
    • Stebbins, C.E.1    Borukhov, S.2    Orlova, M.3    Polyakov, A.4    Goldfarb, A.5    Darst, S.A.6
  • 60
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and D'Souza-Schorey, C. (1997). Rho GTPases and signaling networks. Genes Dev. 11, 2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 61
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-importin β interaction at 2.3 Å resolution
    • Vetter, I.R., Arndt, A., Kutay, U., Georlich, D., and Wittinghofer, A. (1999). Structural view of the Ran-importin β interaction at 2.3 Å resolution. Cell 97, 635-646.
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Georlich, D.4    Wittinghofer, A.5
  • 63
  • 65
    • 0033582473 scopus 로고    scopus 로고
    • Loop 6 of RhoA confers specificity for effector binding, stress fiber formation, and cellular transformation
    • Zong, H., Raman, N., Mickelson-Young, L.A., Atkinson, S.J., and Quilliam, L.A. (1999). Loop 6 of RhoA confers specificity for effector binding, stress fiber formation, and cellular transformation. J. Biol. Chem. 274, 4551-4560.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4551-4560
    • Zong, H.1    Raman, N.2    Mickelson-Young, L.A.3    Atkinson, S.J.4    Quilliam, L.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.