메뉴 건너뛰기




Volumn 138, Issue 2, 1997, Pages 363-374

Regulation of actin polymerization in cell-free systems by GTPγS and Cdc42

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; GUANOSINE TRIPHOSPHATE;

EID: 0030849454     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.138.2.363     Document Type: Article
Times cited : (145)

References (54)
  • 1
    • 0028299331 scopus 로고
    • Activation of NADPH oxidase involves the dissociation of p21rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane
    • Abo, A., M.R. Webb, A. Grogan, and A.W. Segal. 1994. Activation of NADPH oxidase involves the dissociation of p21rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane. Biochem. J. 298:585-591.
    • (1994) Biochem. J. , vol.298 , pp. 585-591
    • Abo, A.1    Webb, M.R.2    Grogan, A.3    Segal, A.W.4
  • 2
    • 0029954225 scopus 로고    scopus 로고
    • Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein
    • Barkalow, K.W., K.J. Witke, D.J. Kwiatkowshi, and J.H. Hartwig. 1996. Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein. J. Cell Biol. 134:389-399.
    • (1996) J. Cell Biol. , vol.134 , pp. 389-399
    • Barkalow, K.W.1    Witke, K.J.2    Kwiatkowshi, D.J.3    Hartwig, J.H.4
  • 3
    • 0025264696 scopus 로고
    • Involvement of GTP-binding proteins in actin polymerization in human neutrophils
    • Bengtsson, T., E. Sarndahl, O. Stendahl, and T. Andersson. 1990. Involvement of GTP-binding proteins in actin polymerization in human neutrophils. Proc. Natl. Acad. Sci. USA. 87:2921-2925.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2921-2925
    • Bengtsson, T.1    Sarndahl, E.2    Stendahl, O.3    Andersson, T.4
  • 4
    • 0028198653 scopus 로고
    • Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins
    • Bokoch, G.M.S. 1994. Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins. Curr. Opin. Cell Biol. 6:212-218.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 212-218
    • Bokoch, G.M.S.1
  • 5
    • 0028081350 scopus 로고
    • Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins
    • Bokoch, G.M., B.P. Bohl, and T.-H. Chuang. 1994. Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins. J. Biol. Chem. 269:31674-31679.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31674-31679
    • Bokoch, G.M.1    Bohl, B.P.2    Chuang, T.-H.3
  • 6
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo, P.D., D. Drechsel, and A. Hall. 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
  • 7
    • 0026045382 scopus 로고
    • Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysales indicates that chemoattractant stimulation increases actin filament number without altering filament length distribution
    • Cano, M., D.A. Lauffenburger, and S.H. Zigmond. 1991. Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysales indicates that chemoattractant stimulation increases actin filament number without altering filament length distribution. J. Cell Biol. 115:677-687.
    • (1991) J. Cell Biol. , vol.115 , pp. 677-687
    • Cano, M.1    Lauffenburger, D.A.2    Zigmond, S.H.3
  • 11
    • 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. 133:1403-1416.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1416
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 12
    • 0027442667 scopus 로고
    • Biologically active lipids are regulators of rac-GDI complexation
    • Chuang, T.-H., B.P. Bohl, and G.M. Bokoch. 1993. Biologically active lipids are regulators of rac-GDI complexation. J. Biol. Chem. 268:26206-26211.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26206-26211
    • Chuang, T.-H.1    Bohl, B.P.2    Bokoch, G.M.3
  • 13
    • 0024147085 scopus 로고
    • Chemotaxis in eukaryotic cells: A focus on leukocytes and Dictyostelium
    • Devreotes, P.N., and S.H. Zigmond. 1988. Chemotaxis in eukaryotic cells: a focus on leukocytes and Dictyostelium. Annu. Rev. Cell Biol. 4:649-686.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 649-686
    • Devreotes, P.N.1    Zigmond, S.H.2
  • 15
    • 0024439874 scopus 로고
    • Actin assembly in electro-permeabilized neutrophils: Role of G-proteins
    • Downey, G.P., C.K. Chan, and S. Grinstein. 1989. Actin assembly in electro-permeabilized neutrophils: role of G-proteins. Biochem. Biophys. Res. Commun. 164:700-705.
    • (1989) Biochem. Biophys. Res. Commun. , vol.164 , pp. 700-705
    • Downey, G.P.1    Chan, C.K.2    Grinstein, S.3
  • 16
    • 0030458493 scopus 로고    scopus 로고
    • Roles for Racl and Cdc42 in planar polarization and hair outgrowth in the wing of Drosophila
    • Eaton, S., R. Wepf, and K. Simons. 1996. Roles for Racl and Cdc42 in planar polarization and hair outgrowth in the wing of Drosophila. J. Cell Biol. 135:1277-1289.
    • (1996) J. Cell Biol. , vol.135 , pp. 1277-1289
    • Eaton, S.1    Wepf, R.2    Simons, K.3
  • 18
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate
    • Gilmore, A.P., and K. Burridge. 1996. Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate. Nature (Lond.). 381:531-535.
    • (1996) Nature (Lond.) , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 19
    • 0029891491 scopus 로고    scopus 로고
    • IQGAP1, A calmodulin-binding protein with a rasGAP-related domain, is a potential effector for Cdc42Hs
    • Hart, M.J., M.G. Callow, B. Souza, and P. Polakis. 1996. IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for Cdc42Hs. EMBO (Eur. Mol. Biol. Organ.) J. 15:2997-3005.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 2997-3005
    • Hart, M.J.1    Callow, M.G.2    Souza, B.3    Polakis, P.4
  • 20
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J.H., G.M. Bokoch, C.L. Carpenter, P.A. Janmey, L.A. Taylor, A. Toker, and T.P. Stossel. 1995. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell. 82:643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 21
    • 0027467339 scopus 로고
    • Requirement for postranstational processing of Rac GTP-binding proteins for activation of human neutrophil NADPH oxidase
    • Heyworth, P.G., U.G. Knaus, X. Xu, D.J. Uhlinger, L. Conroy, G.M. Bokoch, and J.T. Curnutte. 1993. Requirement for postranstational processing of Rac GTP-binding proteins for activation of human neutrophil NADPH oxidase. Mol. Biol. Cell. 4:261-269.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 261-269
    • Heyworth, P.G.1    Knaus, U.G.2    Xu, X.3    Uhlinger, D.J.4    Conroy, L.5    Bokoch, G.M.6    Curnutte, J.T.7
  • 22
    • 0022293456 scopus 로고
    • A method for quantifying F-actin in chemolactic peptide activated neutrophils: Study of the effects of tBOC peptide
    • Howard, T.H., and C.O. Oresajo. 1985. A method for quantifying F-actin in chemolactic peptide activated neutrophils: study of the effects of tBOC peptide. Cell Motil. 5:545-557.
    • (1985) Cell Motil. , vol.5 , pp. 545-557
    • Howard, T.H.1    Oresajo, C.O.2
  • 23
    • 0029802561 scopus 로고    scopus 로고
    • RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase
    • Joneson, T., M. McDonough, D. Bar-Sagi, and L.V. Aelst. 1996. RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase. Science (Wash. DC). 274:1374-1376.
    • (1996) Science (Wash. DC) , vol.274 , pp. 1374-1376
    • Joneson, T.1    McDonough, M.2    Bar-Sagi, D.3    Aelst, L.V.4
  • 24
    • 0022608267 scopus 로고
    • Components of the actin-based cytoskeleton
    • Academic Press, Inc., Orlando, FL.
    • Kane, R.E. 1986. Components of the actin-based cytoskeleton. In Methods in Cell Biology. Academic Press, Inc., Orlando, FL. 229-242.
    • (1986) Methods in Cell Biology , pp. 229-242
    • Kane, R.E.1
  • 25
    • 9444242736 scopus 로고    scopus 로고
    • Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)
    • Kimura, K., and M. Ito. 1996. Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science (Wash. DC). 273:245-248.
    • (1996) Science (Wash. DC) , vol.273 , pp. 245-248
    • Kimura, K.1    Ito, M.2
  • 26
    • 0027067903 scopus 로고
    • Purification and characterization of Rac 2: A cytosolic GTP-binding protein that regulates human neutrophil NADPH oxidase
    • Knaus, U.G., P.G. Heyworth, B.T. Kinsella, J.T. Curnutte, and G.M. Bokoch. 1992. Purification and characterization of Rac 2: a cytosolic GTP-binding protein that regulates human neutrophil NADPH oxidase. J. Biol. Chem. 267:23575-23582.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23575-23582
    • Knaus, U.G.1    Heyworth, P.G.2    Kinsella, B.T.3    Curnutte, J.T.4    Bokoch, G.M.5
  • 28
    • 0030059222 scopus 로고    scopus 로고
    • Role of Rho in chemoattractant-activated leukocyte adhesion through integrins
    • Laudanna, C., J.J. Campbell, and E.C. Butcher. 1996. Role of Rho in chemoattractant-activated leukocyte adhesion through integrins. Science (Wash. DC). 271:981-983.
    • (1996) Science (Wash. DC) , vol.271 , pp. 981-983
    • Laudanna, C.1    Campbell, J.J.2    Butcher, E.C.3
  • 29
    • 0028871169 scopus 로고
    • Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast
    • Li, R., Y. Zheng, and D.G. Drubin. 1995. Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast. J. Cell Biol. 128:599-615.
    • (1995) J. Cell Biol. , vol.128 , pp. 599-615
    • Li, R.1    Zheng, Y.2    Drubin, D.G.3
  • 30
    • 0028086441 scopus 로고
    • Distinct morphogenetic functions of similar small GTPases: Drosophila Dracl is involved in axonal outgrowth and myoblast fusion
    • Luo, L., Y.J. Liao, L.Y. Jan, and Y.N. Jan. 1994. Distinct morphogenetic functions of similar small GTPases: Drosophila Dracl is involved in axonal outgrowth and myoblast fusion. Genes Dev. 8:1787-1802.
    • (1994) Genes Dev. , vol.8 , pp. 1787-1802
    • Luo, L.1    Liao, Y.J.2    Jan, L.Y.3    Jan, Y.N.4
  • 31
  • 32
    • 9544225039 scopus 로고    scopus 로고
    • Identification of a putative effector for Cdc42Hs with high sequence similarity to the RasGAP-related protein IQGAp1 and a Cdc42Hs binding partner with similarity to IQGAP2
    • McCallum, S.J., W.J. Wu, and R.A. Cerione. 1996. Identification of a putative effector for Cdc42Hs with high sequence similarity to the RasGAP-related protein IQGAp1 and a Cdc42Hs binding partner with similarity to IQGAP2. J. Biol. Chem. 271:21732-21737.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21732-21737
    • McCallum, S.J.1    Wu, W.J.2    Cerione, R.A.3
  • 33
    • 0020551238 scopus 로고
    • Changes in actin associated with the cytoskeleton following chemotactic stimulation of Dictyostelium discoideum. Biochem
    • McRobbie, S.J., and P.C. Newell. 1983. Changes in actin associated with the cytoskeleton following chemotactic stimulation of Dictyostelium discoideum. Biochem. Biophys. Res. Commun. 115:351-359.
    • (1983) Biophys. Res. Commun. , vol.115 , pp. 351-359
    • McRobbie, S.J.1    Newell, P.C.2
  • 34
    • 0026568360 scopus 로고
    • Phosphatidylinositol 4-kinase and phosphatidylinositol-4-phosphate 5-kinase from bovine brain membranes
    • Moritz, A., J. Westerman, P.N.E.D. Graan, and K.W.A. Wirtz, 1992. Phosphatidylinositol 4-kinase and phosphatidylinositol-4-phosphate 5-kinase from bovine brain membranes. Methods Enzymol. 209:202-210.
    • (1992) Methods Enzymol. , vol.209 , pp. 202-210
    • Moritz, A.1    Westerman, J.2    Graan, P.N.E.D.3    Wirtz, K.W.A.4
  • 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., 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
  • 37
    • 0028837170 scopus 로고
    • Activation of the small GTP-binding proteins rho and rac by growth factor receptors
    • Nobes, C.D., P. Hawkins, L. Stevens, and A. Hall. 1995. Activation of the small GTP-binding proteins rho and rac by growth factor receptors. J. Cell Science, 108:225-233.
    • (1995) J. Cell Science , vol.108 , pp. 225-233
    • Nobes, C.D.1    Hawkins, P.2    Stevens, L.3    Hall, A.4
  • 38
    • 0028990158 scopus 로고
    • Translocation of p21rac2 from cytosol to plasma membrane is neither necessary nor sufficient for neutrophil NADPH oxidase activity
    • Phillips, M.R., A. Feoktistov, M.H. Pillinger, and S.B. Abramson. 1995. Translocation of p21rac2 from cytosol to plasma membrane is neither necessary nor sufficient for neutrophil NADPH oxidase activity. J. Biol. Chem. 270:11514-11521.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11514-11521
    • Phillips, M.R.1    Feoktistov, A.2    Pillinger, M.H.3    Abramson, S.B.4
  • 39
    • 0028144990 scopus 로고
    • Induction of actin polymerization in permeabilized neutrophils: Role of ATP
    • Redmond, T., M. Tardif, and S.H. Zigmond. 1994. Induction of actin polymerization in permeabilized neutrophils: role of ATP. J. Biol. Chem. 269:21657-21663.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21657-21663
    • Redmond, T.1    Tardif, M.2    Zigmond, S.H.3
  • 40
    • 0030293886 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways
    • Reif, K., C.D. Nobes, G. Thomas, A. Hall, and D.A. Cantrell. 1996. Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways. Curr. Biol. 6:1445-1455.
    • (1996) Curr. Biol. , vol.6 , pp. 1445-1455
    • Reif, K.1    Nobes, C.D.2    Thomas, G.3    Hall, A.4    Cantrell, D.A.5
  • 41
  • 42
    • 0029795850 scopus 로고    scopus 로고
    • Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by polyphospho-inositides
    • Schafer, D.A., P.B. Jennings, and J.A. Cooper. 1996. Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphospho-inositides. J. Cell Biol. 135:169-179.
    • (1996) J. Cell Biol. , vol.135 , pp. 169-179
    • Schafer, D.A.1    Jennings, P.B.2    Cooper, J.A.3
  • 44
    • 0028846966 scopus 로고
    • Actin polymerization induced by GTPγS in permeabilized neutrophils is induced and maintained by free barbed ends
    • Tardif, M., S. Huang, T. Redmond, D. Safer, M. Pring, and S.H. Zigmond. 1995. Actin polymerization induced by GTPγS in permeabilized neutrophils is induced and maintained by free barbed ends. J. Biol. Chem. 270:28075-28083.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28075-28083
    • Tardif, M.1    Huang, S.2    Redmond, T.3    Safer, D.4    Pring, M.5    Zigmond, S.H.6
  • 45
    • 0028030072 scopus 로고
    • Effects of acid phospholipids on nucleotide exchange properties of ADP-ribosylation factor 1
    • Terui, T., R.A. Kahn, and P.A. Randazzo. 1994. Effects of acid phospholipids on nucleotide exchange properties of ADP-ribosylation factor 1. J. Biol. Chem. 269:28130-28135.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28130-28135
    • Terui, T.1    Kahn, R.A.2    Randazzo, P.A.3
  • 46
    • 0024451176 scopus 로고
    • Guanine nucleotide-induced polymerization of actin in electropermeabilized human neutrophils
    • Therrien, S., and P.M. Naccache. 1989. Guanine nucleotide-induced polymerization of actin in electropermeabilized human neutrophils. J. Cell Biol. 109:1125-1132.
    • (1989) J. Cell Biol. , vol.109 , pp. 1125-1132
    • Therrien, S.1    Naccache, P.M.2
  • 47
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias, K.F., L.C. Cantley, and C.L. Carpenter. 1995. Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270:17656-17659.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 48
    • 0029757748 scopus 로고    scopus 로고
    • Identification of a novel Racl-interacting protein involved in membrane ruffling
    • VanAeist, L., T. Joneson, and D. Bar-Sagi. 1996. Identification of a novel Racl-interacting protein involved in membrane ruffling. EMBO (Eur. Mol. Biol. Organ.) J. 15:3778-3786.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 3778-3786
    • Vanaeist, L.1    Joneson, T.2    Bar-Sagi, D.3
  • 49
    • 0028948329 scopus 로고
    • Retroviral transduclion and oncogenic selection of cDNA encoding Dbs, A homolog of the Dhl guanine nucleotide exchange factor
    • Whitehead, I., J. Kirk, and R. Kay. 1995a. Retroviral transduclion and oncogenic selection of cDNA encoding Dbs, a homolog of the Dhl guanine nucleotide exchange factor. Oncogene. 10:713-721.
    • (1995) Oncogene , vol.10 , pp. 713-721
    • Whitehead, I.1    Kirk, J.2    Kay, R.3
  • 50
    • 0029155976 scopus 로고
    • Expression cloning of lfc, A novel oncogene with structual similarities to guanine nucleotide exchange factors and to regulatory region of protein kinase C
    • Whitehead, I., H. Kirk, C. Tognon, G. Trigo-Gonzales, and R. Kay. 1995b. Expression cloning of lfc, a novel oncogene with structual similarities to guanine nucleotide exchange factors and to regulatory region of protein kinase C. J. Biol. Chem. 270:18388-18395.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18388-18395
    • Whitehead, I.1    Kirk, H.2    Tognon, C.3    Trigo-Gonzales, G.4    Kay, R.5
  • 51
    • 0029020634 scopus 로고
    • The G protein β subunit is essential for multiple responses to chemoattractants in Dictyostelium
    • Wu, L., R. Valkema, P.J.M.V. Haastert, and P.N. Devreotes. 1995. The G protein β subunit is essential for multiple responses to chemoattractants in Dictyostelium. J. Cell Biol. 129:1667-1675.
    • (1995) J. Cell Biol. , vol.129 , pp. 1667-1675
    • Wu, L.1    Valkema, R.2    Haastert, P.J.M.V.3    Devreotes, P.N.4
  • 52
    • 0028142464 scopus 로고
    • Differing structural requirements for GTPase-activating protein responsiveness and NADPH oxidase activation by Rac
    • Xu, X., D.C. Barry, J. Settleman, M.A. Schwartz, and G.M. Bokoch. 1994. Differing structural requirements for GTPase-activating protein responsiveness and NADPH oxidase activation by Rac. J. Biol. Chem. 269:23569-23574.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23569-23574
    • Xu, X.1    Barry, D.C.2    Settleman, J.3    Schwartz, M.A.4    Bokoch, G.M.5
  • 53
    • 0028338545 scopus 로고
    • Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85
    • Zheng, Y., S. Bagrodia, and R.A. Cerione. 1994. Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85. J. Biol. Chem. 269:18727-18730.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18727-18730
    • Zheng, Y.1    Bagrodia, S.2    Cerione, R.A.3
  • 54
    • 0029835783 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate provides an alternative to guanine nucleotide exchange factors by stimulating the dissociation of GDP from Cdc42Hs
    • Zheng, Y., J.A. Glaven, W.J. Wu, and R.A. Cerione. 1996. Phosphatidylinositol 4,5-bisphosphate provides an alternative to guanine nucleotide exchange factors by stimulating the dissociation of GDP from Cdc42Hs. J. Biol. Chem. 271:23815-23819.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23815-23819
    • Zheng, Y.1    Glaven, J.A.2    Wu, W.J.3    Cerione, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.