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Volumn 1, Issue 1, 2001, Pages 63-72

The Nf2 Tumor Suppressor, Merlin, Functions in Rac-Dependent Signaling

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[No Author keywords available]

Indexed keywords

FALCO COLUMBARIUS;

EID: 18044399847     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1534-5807(01)00009-0     Document Type: Article
Times cited : (296)

References (59)
  • 2
    • 0032589269 scopus 로고    scopus 로고
    • Effectors for the Rho GTPases
    • Aspenstrom P. Effectors for the Rho GTPases. Curr. Opin. Cell Biol. 11:1999;95-102.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 95-102
    • Aspenstrom, P.1
  • 4
    • 0034695446 scopus 로고    scopus 로고
    • CD44 interaction with tiam1 promotes Rac1 signaling and hyaluronic acid-mediated breast tumor cell migration
    • Bourguignon L.Y., Zhu H., Shao L., Chen Y.W. CD44 interaction with tiam1 promotes Rac1 signaling and hyaluronic acid-mediated breast tumor cell migration. J. Biol. Chem. 275:2000;1829-1838.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1829-1838
    • Bourguignon, L.Y.1    Zhu, H.2    Shao, L.3    Chen, Y.W.4
  • 5
    • 0034524664 scopus 로고    scopus 로고
    • ERM-merlin and EBP50 protein families in plasma membrane organization and function
    • Bretscher A., Chambers D., Nguyen R., Reczek D. ERM-merlin and EBP50 protein families in plasma membrane organization and function. Ann. Rev. Cell Dev. Biol. 16:2000;113-143.
    • (2000) Ann. Rev. Cell Dev. Biol. , vol.16 , pp. 113-143
    • Bretscher, A.1    Chambers, D.2    Nguyen, R.3    Reczek, D.4
  • 6
    • 0030134625 scopus 로고    scopus 로고
    • Human Ste20 homologue hPAK1 links GTPases to the JNK, MAP kinase pathway
    • Brown J.L., Stowers L., Baer M., Trejo J., Coughlin S., Chant J. Human Ste20 homologue hPAK1 links GTPases to the JNK, MAP kinase pathway. Curr. Biol. 6:1996;598-605.
    • (1996) Curr. Biol. , vol.6 , pp. 598-605
    • Brown, J.L.1    Stowers, L.2    Baer, M.3    Trejo, J.4    Coughlin, S.5    Chant, J.6
  • 7
    • 0029890229 scopus 로고    scopus 로고
    • The 70kDa S6 kinase complexes with and is activated by the Rho family G proteins Cdc42 and Rac1
    • Chou M.M., Blenis J. The 70kDa S6 kinase complexes with and is activated by the Rho family G proteins Cdc42 and Rac1. Cell. 85:1996;573-583.
    • (1996) Cell , vol.85 , pp. 573-583
    • Chou, M.M.1    Blenis, J.2
  • 8
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso O.A., Chiariello M., Yu J.C., Teramoto H., Crespo P., Xu N., Miki T., Gutkind J.S. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell. 81:1995;1137-1146.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, J.S.8
  • 10
    • 0034595381 scopus 로고    scopus 로고
    • Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK
    • del Pozo M.A., Price L.S., Alderson N.B., Ren X.D., Schwartz M.A. Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK. EMBO J. 19:2000;2008-2014.
    • (2000) EMBO J. , vol.19 , pp. 2008-2014
    • Del Pozo, M.A.1    Price, L.S.2    Alderson, N.B.3    Ren, X.D.4    Schwartz, M.A.5
  • 11
    • 0033593337 scopus 로고    scopus 로고
    • The Dbl-related protein, Lfc, localizes to microtubules and mediates the activation of Rac signaling pathways in cells
    • Glaven J.A., Whitehead I., Bagrodia S., Kay R., Cerione R.A. The Dbl-related protein, Lfc, localizes to microtubules and mediates the activation of Rac signaling pathways in cells. J. Biol. Chem. 274:1999;2279-2285.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2279-2285
    • Glaven, J.A.1    Whitehead, I.2    Bagrodia, S.3    Kay, R.4    Cerione, R.A.5
  • 12
    • 0032947605 scopus 로고    scopus 로고
    • Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin
    • Gronholm M., Sainio M., Zhao F., Heiska L., Vaheri A., Carpen O. Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin. J. Cell Sci. 112:1999;895-904.
    • (1999) J. Cell Sci. , vol.112 , pp. 895-904
    • Gronholm, M.1    Sainio, M.2    Zhao, F.3    Heiska, L.4    Vaheri, A.5    Carpen, O.6
  • 15
    • 0032899713 scopus 로고    scopus 로고
    • Increased expression of the NF2 tumor suppressor gene product, merlin, impairs cell motility, adhesion and spreading
    • Gutmann D.H., Sherman L., Seftor L., Haipek C., Hoang Lu K., Hendrix M. Increased expression of the NF2 tumor suppressor gene product, merlin, impairs cell motility, adhesion and spreading. Hum. Mol. Genet. 8:1999;267-275.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 267-275
    • Gutmann, D.H.1    Sherman, L.2    Seftor, L.3    Haipek, C.4    Hoang Lu, K.5    Hendrix, M.6
  • 16
    • 0028225439 scopus 로고
    • Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins
    • Habets G.G., Scholtes E.H., Zuydgeest D., van der Kammen R.A., Stam J.C., Berns A., Collard J.G. Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins. Cell. 77:1994;537-549.
    • (1994) Cell , vol.77 , pp. 537-549
    • Habets, G.G.1    Scholtes, E.H.2    Zuydgeest, D.3    Van Der Kammen, R.A.4    Stam, J.C.5    Berns, A.6    Collard, J.G.7
  • 17
    • 0027423418 scopus 로고
    • Identification of an oncoprotein- And UV-responsive protein kinase that binds and potentiates the c-Jun activation domain
    • Hibi M., Lin A., Smeal T., Minden A., Karin M. Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes & Dev. 7:1993;2135-2148.
    • (1993) Genes & Dev. , vol.7 , pp. 2135-2148
    • Hibi, M.1    Lin, A.2    Smeal, T.3    Minden, A.4    Karin, M.5
  • 19
    • 0033617289 scopus 로고    scopus 로고
    • Replacement of Threonine 558, a Critical Site of Phosphorylation of Moesin in Vivo, with Aspartate activates F-actin Binding of Moesin. Regulation by conformational change
    • Huang L., Wong T.Y., Lin R.C., Furthmayr H. Replacement of Threonine 558, a Critical Site of Phosphorylation of Moesin in Vivo, with Aspartate activates F-actin Binding of Moesin. Regulation by conformational change. J. Biol. Chem. 274:1999;12803-12810.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12803-12810
    • Huang, L.1    Wong, T.Y.2    Lin, R.C.3    Furthmayr, H.4
  • 20
    • 0032054723 scopus 로고    scopus 로고
    • Signal transduction by the c-Jun N-terminal kinase (JNK)- From inflammation to development
    • Ip Y.T., Davis R.J. Signal transduction by the c-Jun N-terminal kinase (JNK)- from inflammation to development. Curr. Opin. Cell Biol. 10:1998;205-219.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 205-219
    • Ip, Y.T.1    Davis, R.J.2
  • 21
    • 0029802561 scopus 로고    scopus 로고
    • RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase
    • Erratum: Science Apr 11;276, 1997.
    • Joneson T., McDonough M., Bar-Sagi D., Van Aelst L. RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase. Science. 274:1996;1374-1376. Erratum: Science Apr 11;276, 1997.
    • (1996) Science , vol.274 , pp. 1374-1376
    • Joneson, T.1    McDonough, M.2    Bar-Sagi, D.3    Van Aelst, L.4
  • 22
    • 0031459917 scopus 로고    scopus 로고
    • Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(3)K
    • Keely P.J., Westwick J.K., Whitehead I.P., Der C.J., Parise L.V. Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(3)K. Nature. 390:1997;632-636.
    • (1997) Nature , vol.390 , pp. 632-636
    • Keely, P.J.1    Westwick, J.K.2    Whitehead, I.P.3    Der, C.J.4    Parise, L.V.5
  • 23
    • 0028800305 scopus 로고
    • Activation of Rac1, RhoA, and Mitogen-Activated Protein Kinases is required for Ras transformation
    • Khosravi-Far R., Solski P.A., Clark G., Kinch M., Der C. Activation of Rac1, RhoA, and Mitogen-Activated Protein Kinases is required for Ras transformation. Mol. Cell. Biol. 15:1995;6443-6453.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6443-6453
    • Khosravi-Far, R.1    Solski, P.A.2    Clark, G.3    Kinch, M.4    Der, C.5
  • 24
    • 0033604638 scopus 로고    scopus 로고
    • Signaling to Rho GTPases
    • Kjoller L., Hall A. Signaling to Rho GTPases. Exp. Cell. Res. 253:1999;166-179.
    • (1999) Exp. Cell. Res. , vol.253 , pp. 166-179
    • Kjoller, L.1    Hall, A.2
  • 26
    • 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., Hall A. Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade. Cell. 87:1996;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
  • 27
  • 28
    • 0033606997 scopus 로고    scopus 로고
    • Expression level, subcellular distribution and rho-GDI binding affinity of merlin in comparison with Ezrin/Radixin/Moesin proteins
    • Maeda M., Matsui T., Imamura M., Tsukita S., Tsukita S. Expression level, subcellular distribution and rho-GDI binding affinity of merlin in comparison with Ezrin/Radixin/Moesin proteins. Oncogene. 18:1999;4788-4797.
    • (1999) Oncogene , vol.18 , pp. 4788-4797
    • Maeda, M.1    Matsui, T.2    Imamura, M.3    Tsukita, S.4    Tsukita, S.5
  • 29
    • 0032498528 scopus 로고    scopus 로고
    • Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association.
    • Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K., Tsukita S., Tsukita S. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J. Cell Biol. 140:1998;647-657.
    • (1998) J. Cell Biol. , vol.140 , pp. 647-657
    • Matsui, T.1    Maeda, M.2    Doi, Y.3    Yonemura, S.4    Amano, M.5    Kaibuchi, K.6    Tsukita, S.7    Tsukita, S.8
  • 30
    • 0033523986 scopus 로고    scopus 로고
    • Activation of ERM proteins in vivo by Rho involves phosphatidyl-inositol 4-phosphate 5-kinase and not ROCK kinases
    • Matsui T., Yonemura S., Tsukita S., Tsukita S. Activation of ERM proteins in vivo by Rho involves phosphatidyl-inositol 4-phosphate 5-kinase and not ROCK kinases. Curr. Biol. 9:1999;1259-1262.
    • (1999) Curr. Biol. , vol.9 , pp. 1259-1262
    • Matsui, T.1    Yonemura, S.2    Tsukita, S.3    Tsukita, S.4
  • 31
    • 0032522603 scopus 로고    scopus 로고
    • Mice heterozygous for a mutation at the Nf2 tumor suppressor locus develop a range of highly metastatic tumors
    • McClatchey A.I., Saotome I., Mercer K., Crowley D., Gusella J.F., Bronson R.T., Jacks T. Mice heterozygous for a mutation at the Nf2 tumor suppressor locus develop a range of highly metastatic tumors. Genes Dev. 12:1998;1121-1133.
    • (1998) Genes Dev. , vol.12 , pp. 1121-1133
    • McClatchey, A.I.1    Saotome, I.2    Mercer, K.3    Crowley, D.4    Gusella, J.F.5    Bronson, R.T.6    Jacks, T.7
  • 32
    • 0030924657 scopus 로고    scopus 로고
    • The Nf2 tumor suppressor gene product is essential for extra embryonic development immediately prior to gastrulation
    • McClatchey A.I., Saotome I., Ramesh V., Gusella J.F., Jacks T. The Nf2 tumor suppressor gene product is essential for extra embryonic development immediately prior to gastrulation. Genes Dev. 11:1997;1253-1265.
    • (1997) Genes Dev. , vol.11 , pp. 1253-1265
    • McClatchey, A.I.1    Saotome, I.2    Ramesh, V.3    Gusella, J.F.4    Jacks, T.5
  • 33
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • Minden A., Lin A., Claret F., Abo A., Karin M. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell. 81:1995;1147-1157.
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.3    Abo, A.4    Karin, M.5
  • 35
    • 0039732742 scopus 로고    scopus 로고
    • Hierarchy of merlin and ezrin N- And C-terminal domain interactions in homo- And heterotypic associations and their relationship to binding of scaffolding proteins EBP50 and E3KARP
    • Nguyen R., Reczek D., Bretscher A. Hierarchy of merlin and ezrin N- and C-terminal domain interactions in homo- and heterotypic associations and their relationship to binding of scaffolding proteins EBP50 and E3KARP. J. Biol. Chem. in press:2000.
    • (2000) J. Biol. Chem.
    • Nguyen, R.1    Reczek, D.2    Bretscher, A.3
  • 36
    • 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., Hall A. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:1995;53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 37
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases Control Polarity, Protrusion, and Adhesion during Cell Movement
    • Nobes C.D., Hall A. Rho GTPases Control Polarity, Protrusion, and Adhesion during Cell Movement. J. Cell Biol. 144:1999;1235-1244.
    • (1999) J. Cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 38
    • 0034689057 scopus 로고    scopus 로고
    • Hyaluronic acid (HA) binding to CD44 activates rac1 and induces lamellipodia outgrowth
    • Oliferenko S., Kaverina I., Small J.V., Huber L.A. Hyaluronic acid (HA) binding to CD44 activates rac1 and induces lamellipodia outgrowth. J. Cell Biol. 148:2000;1159-1164.
    • (2000) J. Cell Biol. , vol.148 , pp. 1159-1164
    • Oliferenko, S.1    Kaverina, I.2    Small, J.V.3    Huber, L.A.4
  • 39
    • 0032567361 scopus 로고    scopus 로고
    • Phosphorylation of moesin by rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures
    • Oshiro N., Fukata Y., Kaibuchi K. Phosphorylation of moesin by rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures. J. Biol. Chem. 273:1998;34663-34666.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34663-34666
    • Oshiro, N.1    Fukata, Y.2    Kaibuchi, K.3
  • 40
    • 0032578798 scopus 로고    scopus 로고
    • Ruffling membrane, stress fiber, cell spreading and proliferation abnormalities in human schwannoma cells
    • Pelton P.D., Sherman L., Rizvi T., Marchionni M., Wood P., Friedman R., Ratner N. Ruffling membrane, stress fiber, cell spreading and proliferation abnormalities in human schwannoma cells. Oncogene. 17:1998;2195-2209.
    • (1998) Oncogene , vol.17 , pp. 2195-2209
    • Pelton, P.D.1    Sherman, L.2    Rizvi, T.3    Marchionni, M.4    Wood, P.5    Friedman, R.6    Ratner, N.7
  • 41
    • 0028903247 scopus 로고
    • An essential role for Rac in Ras transformation
    • Qiu R.G., Chen J., Kirn D., McCormick F., Symons M. An essential role for Rac in Ras transformation. Nature. 374:1995;457-459.
    • (1995) Nature , vol.374 , pp. 457-459
    • Qiu, R.G.1    Chen, J.2    Kirn, D.3    McCormick, F.4    Symons, M.5
  • 42
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren X.D., Kiosses W.B., Schwartz M.A. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18:1999;578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 44
    • 0033652761 scopus 로고    scopus 로고
    • Farnesyltransferase and geranylgeranyltransferase I inhibitors in cancer therapy: Important mechanistic and bench to bedside issues
    • Sebti S.M., Hamilton A.D. Farnesyltransferase and geranylgeranyltransferase I inhibitors in cancer therapy. important mechanistic and bench to bedside issues Expert Opin.Investig. Drugs. 9:2000;2767-2782.
    • (2000) Expert Opin.Investig. Drugs. , vol.9 , pp. 2767-2782
    • Sebti, S.M.1    Hamilton, A.D.2
  • 45
    • 0031456065 scopus 로고    scopus 로고
    • Activation of phosphoinositide 3-OH kinase by the alpha6beta4 integrin promotes carcinoma invasion
    • Shaw L.M., Rabinovitz I., Wang H.H., Toker A., Mercurio A.M. Activation of phosphoinositide 3-OH kinase by the alpha6beta4 integrin promotes carcinoma invasion. Cell. 91:1997;949-960.
    • (1997) Cell , vol.91 , pp. 949-960
    • Shaw, L.M.1    Rabinovitz, I.2    Wang, H.H.3    Toker, A.4    Mercurio, A.M.5
  • 46
    • 0031907484 scopus 로고    scopus 로고
    • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
    • a
    • Shaw R.J., Henry M., Solomon F., Jacks T. RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts. Mol. Biol. Cell. 9:1998;403-419. a.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 403-419
    • Shaw, R.J.1    Henry, M.2    Solomon, F.3    Jacks, T.4
  • 47
    • 0032571272 scopus 로고    scopus 로고
    • Regulation of the neurofibromatosis type 2 tumor suppressor protein, merlin, by adhesion and growth arrest stimuli
    • b
    • Shaw R.J., McClatchey A.I., Jacks T. Regulation of the neurofibromatosis type 2 tumor suppressor protein, merlin, by adhesion and growth arrest stimuli. J. Biol. Chem. 273:1998;7757-7764. b.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7757-7764
    • Shaw, R.J.1    McClatchey, A.I.2    Jacks, T.3
  • 48
    • 0031868907 scopus 로고    scopus 로고
    • Localization and functional domains of the neurofibromatosis type II tumor suppressor, merlin
    • c
    • Shaw R.J., McClatchey A.I., Jacks T. Localization and functional domains of the neurofibromatosis type II tumor suppressor, merlin. Cell Growth Diff. 9:1998;287-296. c.
    • (1998) Cell Growth Diff. , vol.9 , pp. 287-296
    • Shaw, R.J.1    McClatchey, A.I.2    Jacks, T.3
  • 49
    • 0027956397 scopus 로고
    • Hyaluronate receptors: Key players in growth, differentiation, migration and tumor progression
    • Sherman L., Sleeman J., Herrlich P., Ponta H. Hyaluronate receptors. key players in growth, differentiation, migration and tumor progression Curr. Op. Cell Biol. 6:1994;726-733.
    • (1994) Curr. Op. Cell Biol. , vol.6 , pp. 726-733
    • Sherman, L.1    Sleeman, J.2    Herrlich, P.3    Ponta, H.4
  • 51
    • 0032583447 scopus 로고    scopus 로고
    • C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton
    • Simons P.C., Pietromonaco S.F., Reczek D., Bretscher A., Elias L. C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton. Biochem. Biophys. Res. Commun. 253:1998;561-565.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 561-565
    • Simons, P.C.1    Pietromonaco, S.F.2    Reczek, D.3    Bretscher, A.4    Elias, L.5
  • 52
    • 0030846295 scopus 로고    scopus 로고
    • Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
    • Takahashi K., Sasaki T., Mammoto A., Takaishi K., Kameyama T., Tsukita S., Takai Y. Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. J. Biol. Chem. 272:1997;23371-23375.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23371-23375
    • Takahashi, K.1    Sasaki, T.2    Mammoto, A.3    Takaishi, K.4    Kameyama, T.5    Tsukita, S.6    Takai, Y.7
  • 54
    • 0028168361 scopus 로고
    • An anti-Ras function of neurofibromatosis type 2 gene product (NF2/Merlin)
    • Tikoo A., Varga M., Ramesh V., Gusella J., Maruta H. An anti-Ras function of neurofibromatosis type 2 gene product (NF2/Merlin). J. Biol. Chem. 269:1994;23387-23390.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23387-23390
    • Tikoo, A.1    Varga, M.2    Ramesh, V.3    Gusella, J.4    Maruta, H.5
  • 55
    • 84883840386 scopus 로고
    • Quantitative studies of the growth of mouse embryo cells in culture and their development into established lines
    • Todaro G.J., Green H. Quantitative studies of the growth of mouse embryo cells in culture and their development into established lines. J. Cell Biol. 17:1963;299-313.
    • (1963) J. Cell Biol. , vol.17 , pp. 299-313
    • Todaro, G.J.1    Green, H.2
  • 56
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst L., D'Souza-Schorey C. Rho GTPases and signaling networks. Genes Dev. 11:1997;2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 57
    • 0030847760 scopus 로고    scopus 로고
    • Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27
    • Vlach J., Hennecke S., Amati B. Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27. EMBO J. 16:1997;5334-5344.
    • (1997) EMBO J. , vol.16 , pp. 5334-5344
    • Vlach, J.1    Hennecke, S.2    Amati, B.3
  • 58
    • 0031026132 scopus 로고    scopus 로고
    • Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways
    • Westwick J.K., Lambert Q.T., Clark G.J., Symons M., Van Aelst L., Pestell R.G., Der C.J. Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways. Mol. Cell. Biol. 17:1997;1324-1335.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1324-1335
    • Westwick, J.K.1    Lambert, Q.T.2    Clark, G.J.3    Symons, M.4    Van Aelst, L.5    Pestell, R.G.6    Der, C.J.7
  • 59
    • 0032541613 scopus 로고    scopus 로고
    • Rho family proteins and Ras transformation: The RHOad less traveled gets congested
    • Zohn I.M., Campbell S.L., Khosravi-Far R., Rossman K.L., Der C.J. Rho family proteins and Ras transformation. the RHOad less traveled gets congested Oncogene. 17:1998;1415-1438.
    • (1998) Oncogene , vol.17 , pp. 1415-1438
    • Zohn, I.M.1    Campbell, S.L.2    Khosravi-Far, R.3    Rossman, K.L.4    Der, C.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.