메뉴 건너뛰기




Volumn 18, Issue 8, 1998, Pages 4761-4771

RhoE regulates actin cytoskeleton organization and cell migration

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; AMINO ACID; CELL CYCLE PROTEIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; RHO FACTOR; SCATTER FACTOR;

EID: 0031877714     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.8.4761     Document Type: Article
Times cited : (197)

References (55)
  • 2
    • 0030940218 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages
    • Allen, W. E., G. E. Jones, J. W. Pollard, and A. J. Ridley. 1997. Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages. J. Cell Sci. 110:707-720.
    • (1997) J. Cell Sci. , vol.110 , pp. 707-720
    • Allen, W.E.1    Jones, G.E.2    Pollard, J.W.3    Ridley, A.J.4
  • 4
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski, M. S., and F. McCormick. 1993. Proteins regulating Ras and its relatives. Nature 366:643-654.
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 5
    • 0024361531 scopus 로고
    • Colony-stimulating factor-1 induces rapid behavioural responses in the mouse macrophage cell line, BAC1.2F5
    • Boocock, C. A., G. E. Jones, E. R. Stanley, and J. W. Pollard. 1989. Colony-stimulating factor-1 induces rapid behavioural responses in the mouse macrophage cell line, BAC1.2F5. J. Cell Sci. 93:447-456.
    • (1989) J. Cell Sci. , vol.93 , pp. 447-456
    • Boocock, C.A.1    Jones, G.E.2    Stanley, E.R.3    Pollard, J.W.4
  • 6
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., D. A. Sanders, and F. McCormick. 1991. The GTPase superfamily: 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
  • 7
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga, V. M., L. M. Machesky, A. Hall, and N. A. Hotchin. 1997. The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J. Cell Biol. 137:1421-1431.
    • (1997) J. Cell Biol. , vol.137 , pp. 1421-1431
    • Braga, V.M.1    Machesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 8
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • Bretscher, A. 1991. Microfilament structure and function in the cortical cytoskeleton. Annu. Rev. Cell Biol. 7:337-374.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 337-374
    • Bretscher, A.1
  • 10
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., K. Fath, T. Kelly, G. Nuckolls, and C. Turner. 1988. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4:487-525.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 12
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M., and K. Burridge. 1996. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133:1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 13
    • 0025982039 scopus 로고
    • The role of actin polymerization in cell motility
    • Cooper, J. A. 1991. The role of actin polymerization in cell motility. Annu. Rev. Physiol. 53:585-605.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 585-605
    • Cooper, J.A.1
  • 14
    • 0026195967 scopus 로고
    • Scatter factor affects major changes in the cytoskeletal organization of epithelial cells
    • Dowrick, P. G., A. R. Prescott, and R. M. Warn. 1991. Scatter factor affects major changes in the cytoskeletal organization of epithelial cells. Cytokine 3:299-310.
    • (1991) Cytokine , vol.3 , pp. 299-310
    • Dowrick, P.G.1    Prescott, A.R.2    Warn, R.M.3
  • 15
    • 0028108358 scopus 로고
    • Optimizing the performance of confocal point scanning laser microscopes over the full field of view
    • Entwistle, A., and M. Noble. 1994. Optimizing the performance of confocal point scanning laser microscopes over the full field of view. J. Microsc. 175:238-251.
    • (1994) J. Microsc. , vol.175 , pp. 238-251
    • Entwistle, A.1    Noble, M.2
  • 16
    • 0029894664 scopus 로고    scopus 로고
    • Identification of a novel human Rho protein with unusual properties: GT-Pase deficiency and in vivo farnesylation
    • Foster, R., K. Q. Hu, Y. Lu, K. M. Nolan, J. Thissen, and J. Settleman. 1996. Identification of a novel human Rho protein with unusual properties: GT-Pase deficiency and in vivo farnesylation. Mol. Cell. Biol. 16:2689-2699.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2689-2699
    • Foster, R.1    Hu, K.Q.2    Lu, Y.3    Nolan, K.M.4    Thissen, J.5    Settleman, J.6
  • 17
    • 0029814413 scopus 로고    scopus 로고
    • Rac "insert region" is a novel effector region that is implicated in the activation of NADPH oxidase, but not PAK65
    • Freeman, J. L., A. Abo, and J. D. Lambeth. 1996. Rac "insert region" is a novel effector region that is implicated in the activation of NADPH oxidase, but not PAK65. J. Biol. Chem. 271:19794-19801.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19794-19801
    • Freeman, J.L.1    Abo, A.2    Lambeth, J.D.3
  • 18
    • 0025362712 scopus 로고
    • Amino acid 61 is a determinant of sensitivity of rap proteins to the ras GTPase activating protein
    • Hart, P. A., and C. J. Marshall. 1990. Amino acid 61 is a determinant of sensitivity of rap proteins to the ras GTPase activating protein. Oncogene 5:1099-1101.
    • (1990) Oncogene , vol.5 , pp. 1099-1101
    • Hart, P.A.1    Marshall, C.J.2
  • 19
    • 0031034136 scopus 로고    scopus 로고
    • The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue
    • Hirshberg, M., R. W. Stockley, G. Dodson, and M. R. Webb. 1997. The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue. Nat. Struct. Biol. 4:147-152.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 147-152
    • Hirshberg, M.1    Stockley, R.W.2    Dodson, G.3    Webb, M.R.4
  • 20
    • 0030615004 scopus 로고    scopus 로고
    • p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions
    • Ishizaki, T., M. Naito, K. Fujisawa, M. Maekawa, N. Watanabe, Y. Saito, and S. Narumiya. 1997. p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions. FEBS Lett. 404:118-124.
    • (1997) FEBS Lett. , vol.404 , pp. 118-124
    • Ishizaki, T.1    Naito, M.2    Fujisawa, K.3    Maekawa, M.4    Watanabe, N.5    Saito, Y.6    Narumiya, S.7
  • 21
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- And thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho
    • Jalink, K., E. J. van Corven, T. Hengeveld, N. Morii, S. Narumiya, and W. H. Moolenaar. 1994. Inhibition of lysophosphatidate-and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho. J. Cell Biol. 126:801-810.
    • (1994) J. Cell Biol. , vol.126 , pp. 801-810
    • Jalink, K.1    Van Corven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiya, S.5    Moolenaar, W.H.6
  • 23
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma, R., S. Ahmed, A. Best, and L. Lim. 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
  • 24
    • 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., N. Tapon, L. Stowers, P. D. Burbelo, P. Aspenstrom, T. Bridges, J. Chant, and A. Hall. 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
  • 25
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D. A., and A. F. Horwitz. 1996. Cell migration: a physically integrated molecular process. Cell 84:359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 26
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK α is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung, T., X. Q. Chen, E. Manser, and L. Lim. 1996. The p160 RhoA-binding kinase ROK α 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
  • 27
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes
    • Leung, T., E. Manser, L. Tan, and L. Lim. 1995. A novel serine/threonine kinase binding 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
  • 28
    • 0024451875 scopus 로고
    • p21H-ras-induced morphological transformation and increases in c-myc expression are independent of functional protein kinase C
    • Lloyd, A. C., H. F. Paterson, J. D. Morris, A. Hall, and C. J. Marshall. 1989. p21H-ras-induced morphological transformation and increases in c-myc expression are independent of functional protein kinase C. EMBO J. 8:1099-1104.
    • (1989) EMBO J. , vol.8 , pp. 1099-1104
    • Lloyd, A.C.1    Paterson, H.F.2    Morris, J.D.3    Hall, A.4    Marshall, C.J.5
  • 29
    • 0030222377 scopus 로고    scopus 로고
    • Rho: A connection between membrane receptor signalling and the cytoskeleton
    • Machesky, L. M., and A. Hall. 1996. Rho: a connection between membrane receptor signalling and the cytoskeleton. Trends Cell Biol. 6:304-310.
    • (1996) Trends Cell Biol. , vol.6 , pp. 304-310
    • Machesky, L.M.1    Hall, A.2
  • 30
    • 0030872949 scopus 로고    scopus 로고
    • Rho- And rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    • Mackay, D. J., F. Esch, H. Furthmayr, and A. Hall. 1997. Rho-and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. J. Cell Biol. 138:927-938.
    • (1997) J. Cell Biol. , vol.138 , pp. 927-938
    • Mackay, D.J.1    Esch, F.2    Furthmayr, H.3    Hall, A.4
  • 31
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison, T. J., and L. P. Cramer. 1996. Actin-based cell motility and cell locomotion. Cell 84:371-379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 32
    • 0023090444 scopus 로고
    • Isolation and characterization of a cloned growth factor dependent macrophage cell line, BAC1.2F5
    • Morgan, C., J. W. Pollard, and E. R. Stanley. 1987. Isolation and characterization of a cloned growth factor dependent macrophage cell line, BAC1.2F5. J. Cell. Physiol. 130:420-427.
    • (1987) J. Cell. Physiol. , vol.130 , pp. 420-427
    • Morgan, C.1    Pollard, J.W.2    Stanley, E.R.3
  • 33
    • 0030612748 scopus 로고    scopus 로고
    • Rho effectors and reorganization of actin cytoskeleton
    • Narumiya, S., T. Ishizaki, and N. Watanabe. 1997. Rho effectors and reorganization of actin cytoskeleton. FEBS Lett. 410:68-72.
    • (1997) FEBS Lett. , vol.410 , pp. 68-72
    • Narumiya, S.1    Ishizaki, T.2    Watanabe, N.3
  • 34
    • 0028258943 scopus 로고
    • Rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- and 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells
    • Nishiyama, T., T. Sasaki, K. Takaishi, M. Kato, H. Yaku, K. Araki, Y. Matsuura, and Y. Takai. 1994. rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor-and 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells. Mol. Cell. Biol. 14:2447-2456.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2447-2456
    • Nishiyama, T.1    Sasaki, T.2    Takaishi, K.3    Kato, M.4    Yaku, H.5    Araki, K.6    Matsuura, Y.7    Takai, Y.8
  • 35
    • 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 A. Hall. 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
  • 36
    • 0025765496 scopus 로고
    • Characterisation in vitro of luminal and myoepithelial cells isolated from the human mammary gland by cell sorting
    • O'Hare, M. J., M. G. Omerod, P. Monaghan, E. B. Lane, and B. A. Gusterson. 1991. Characterisation in vitro of luminal and myoepithelial cells isolated from the human mammary gland by cell sorting. Differentiation 46: 209-221.
    • (1991) Differentiation , vol.46 , pp. 209-221
    • O'Hare, M.J.1    Omerod, M.G.2    Monaghan, P.3    Lane, E.B.4    Gusterson, B.A.5
  • 37
    • 0023721977 scopus 로고
    • Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region
    • Pizon, V., P. Chardin, I. Lerosey, B. Olofsson, and A. Tavilian. 1988. Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region. Oncogene 3:201-204.
    • (1988) Oncogene , vol.3 , pp. 201-204
    • Pizon, V.1    Chardin, P.2    Lerosey, I.3    Olofsson, B.4    Tavilian, A.5
  • 38
    • 0029879915 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate rapidly induces Rho-dependent neurite retraction: Action through a specific cell surface receptor
    • Postma, F. R., K. Jalink, T. Hengeveld, and W. H. Moolenaar. 1996. Sphingosine-1-phosphate rapidly induces Rho-dependent neurite retraction: action through a specific cell surface receptor. EMBO J. 15:2388-2392.
    • (1996) EMBO J. , vol.15 , pp. 2388-2392
    • Postma, F.R.1    Jalink, K.2    Hengeveld, T.3    Moolenaar, W.H.4
  • 39
    • 0027741390 scopus 로고
    • Rad: A member of the Ras family overexpressed in muscle of type II diabetic humans
    • Reynet, C., and C. R. Kahn. 1993. Rad: a member of the Ras family overexpressed in muscle of type II diabetic humans. Science 262:1441-1444.
    • (1993) Science , vol.262 , pp. 1441-1444
    • Reynet, C.1    Kahn, C.R.2
  • 40
    • 0030267458 scopus 로고    scopus 로고
    • Rho: Theme and variations
    • Ridley, A. J. 1996. Rho: theme and variations. Curr. Biol. 6:1256-1264.
    • (1996) Curr. Biol. , vol.6 , pp. 1256-1264
    • Ridley, A.J.1
  • 41
    • 0028894787 scopus 로고
    • Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac, and Rho in MDCK cells
    • Ridley, A. J., P. M. Comoglio, and A. Hall. 1995. Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac, and Rho in MDCK cells. Mol. Cell. Biol. 15:1110-1122.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1110-1122
    • Ridley, A.J.1    Comoglio, P.M.2    Hall, A.3
  • 42
    • 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 A. Hall. 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
  • 43
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., H. F. Paterson, C. L. Johnston, D. Diekman, and A. Hall. 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    Diekman, D.4    Hall, A.5
  • 44
    • 0025153070 scopus 로고
    • Studies on the mechanism of scatter factor. Effects of agents that modulate intracellular signal transduction, macromolecule synthesis and cytoskeleton assembly
    • Rosen, E. M., L. Meromsky, I. Goldberg, M. Bhargava, and E. Setter. 1990. Studies on the mechanism of scatter factor. Effects of agents that modulate intracellular signal transduction, macromolecule synthesis and cytoskeleton assembly. J. Cell Sci. 96:639-649.
    • (1990) J. Cell Sci. , vol.96 , pp. 639-649
    • Rosen, E.M.1    Meromsky, L.2    Goldberg, I.3    Bhargava, M.4    Setter, E.5
  • 46
    • 0029118307 scopus 로고
    • Measurement of intrinsic nucleotide exchange and GTP hydrolysis rates
    • Self, A. J., and A. Hall. 1995. Measurement of intrinsic nucleotide exchange and GTP hydrolysis rates. Methods Enzymol. 256:67-76.
    • (1995) Methods Enzymol. , vol.256 , pp. 67-76
    • Self, A.J.1    Hall, A.2
  • 47
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in E. coli as fusions with glutathione S-transferase
    • Smith, D. S., and K. S. Johnson. 1988. Single-step purification of polypeptides expressed in E. coli as fusions with glutathione S-transferase. Gene 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.S.1    Johnson, K.S.2
  • 48
    • 0022269174 scopus 로고
    • An epithelial scatter factor released by embryo fibroblasts
    • Stoker, M., and M. Perryman. 1985. An epithelial scatter factor released by embryo fibroblasts. J. Cell Sci. 77:209-223.
    • (1985) J. Cell Sci. , vol.77 , pp. 209-223
    • Stoker, M.1    Perryman, M.2
  • 49
    • 0029131982 scopus 로고
    • Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows
    • Takaishi, K., T. Sasaki, T. Kameyama, S. Tsukita, S. Tsukita, and Y. Takai. 1995. Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene 11:39-48.
    • (1995) Oncogene , vol.11 , pp. 39-48
    • Takaishi, K.1    Sasaki, T.2    Kameyama, T.3    Tsukita, S.4    Tsukita, S.5    Takai, Y.6
  • 50
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells
    • Takaishi, K., T. Sasaki, H. Kotani, H. Nishioka, and Y. Takai. 1997. Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells. J. Cell Biol. 139:1047-1059.
    • (1997) J. Cell Biol. , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 51
    • 0031081475 scopus 로고    scopus 로고
    • ERM proteins: Head-to-tail regulation of actin-plasma membrane interaction
    • Tsukita, S., S. Yonemura, and S. Tsukita. 1997. ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem. Sci. 22:53-58.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 53-58
    • Tsukita, S.1    Yonemura, S.2    Tsukita, S.3
  • 52
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and C. D'Souza-Schorey. 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
  • 54
    • 0030785342 scopus 로고    scopus 로고
    • Rho-stimulated contractility contributes to the fibroblastic phenotype of Ras-transformed epithelial cells
    • Zhong, C., M. S. Kinch, and K. Burridge. 1997. Rho-stimulated contractility contributes to the fibroblastic phenotype of Ras-transformed epithelial cells. Mol. Biol. Cell. 8:2329-2344.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 2329-2344
    • Zhong, C.1    Kinch, M.S.2    Burridge, K.3
  • 55
    • 0028935733 scopus 로고
    • Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity
    • Zhu, J., C. Reynet, J. S. Caldwell, and C. R. Kahn. 1995. Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity. J. Biol. Chem. 270:4805-4812.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4805-4812
    • Zhu, J.1    Reynet, C.2    Caldwell, J.S.3    Kahn, C.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.