메뉴 건너뛰기




Volumn 78, Issue 3, 1998, Pages 763-781

The cytoskeleton and cell signaling: Component localization and mechanical coupling

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR; GUANOSINE TRIPHOSPHATASE; ION CHANNEL; PROTEIN KINASE;

EID: 0031850240     PISSN: 00319333     EISSN: None     Source Type: Journal    
DOI: 10.1152/physrev.1998.78.3.763     Document Type: Review
Times cited : (676)

References (252)
  • 1
    • 0030000980 scopus 로고    scopus 로고
    • Cadherin-catenin complex: Protein interactions and their implications for cadherin function
    • ABERLE, H., H. SCHWARTZ, AND R. KEMLER. Cadherin-catenin complex: protein interactions and their implications for cadherin function. J. Cell Biochem. 61: 514-523, 1996.
    • (1996) J. Cell Biochem. , vol.61 , pp. 514-523
    • Aberle, H.1    Schwartz, H.2    Kemler, R.3
  • 2
    • 0027399438 scopus 로고
    • 2 with the cytoskeleton of stimulated rabbit platelets
    • 2 with the cytoskeleton of stimulated rabbit platelets. J. Biochem. 113: 4-6, 1993.
    • (1993) J. Biochem. , vol.113 , pp. 4-6
    • Akiba, S.1    Sato, T.2    Fujii, T.3
  • 3
  • 4
    • 0014829598 scopus 로고
    • Binding of aldolase and triosephosphate dehydrogenase to F-actin and modification of catalytic properties of aldolase
    • ARNOLD, H., AND D. PETTE. Binding of aldolase and triosephosphate dehydrogenase to F-actin and modification of catalytic properties of aldolase. Eur. J. Biochem. 15: 360-366, 1970.
    • (1970) Eur. J. Biochem. , vol.15 , pp. 360-366
    • Arnold, H.1    Pette, D.2
  • 5
    • 0031050451 scopus 로고    scopus 로고
    • Cell anchorage and the cytoskeleton as partners in growth factor dependent cell cycle progression
    • ASSOIAN, R. K., AND X. Y. ZHU. Cell anchorage and the cytoskeleton as partners in growth factor dependent cell cycle progression. Curr. Opin. Cell Biol. 9: 93-98, 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 93-98
    • Assoian, R.K.1    Zhu, X.Y.2
  • 7
    • 0029884155 scopus 로고    scopus 로고
    • Differential translocation of phospholipase C isozymes to integrin-mediated cytoskeletal complexes in thrombin-stimulated human platelets
    • BANNO, Y., S. NAKASHIMA, M. OHZAWA, AND Y. NOZAWA. Differential translocation of phospholipase C isozymes to integrin-mediated cytoskeletal complexes in thrombin-stimulated human platelets. J. Biol. Chem. 271: 14989-14994, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14989-14994
    • Banno, Y.1    Nakashima, S.2    Ohzawa, M.3    Nozawa, Y.4
  • 8
    • 0026703001 scopus 로고
    • Effects of gelsolin on human platelet cytosolic phosphoinositide-phospholipase C isozymes
    • BANNO, Y., T. NAKASHIMA, T. KUMADA, K. EBISAWA, Y. NONOMURA, AND Y. NOZAWA. Effects of gelsolin on human platelet cytosolic phosphoinositide-phospholipase C isozymes. J. Biol. Chem. 267: 6488-6494, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6488-6494
    • Banno, Y.1    Nakashima, T.2    Kumada, T.3    Ebisawa, K.4    Nonomura, Y.5    Nozawa, Y.6
  • 9
    • 0027170920 scopus 로고
    • SH3 domains direct cellular localization of signaling molecules
    • BAR, S. D., D. ROTIN, A. BATZER, V. MANDIYAN, AND J. SCHLESSINGER. SH3 domains direct cellular localization of signaling molecules. Cell 74: 83-91, 1993.
    • (1993) Cell , vol.74 , pp. 83-91
    • Bar, S.D.1    Rotin, D.2    Batzer, A.3    Mandiyan, V.4    Schlessinger, J.5
  • 12
    • 0028072134 scopus 로고
    • Interactions of eukaryotic elongation factor 2 with actin: A possible link between protein synthetic machinery and cytoskeleton
    • BEKTAS, M., R. NURTEN, Z. GUREL, Z. SAYERS, AND E. BERMEK. Interactions of eukaryotic elongation factor 2 with actin: a possible link between protein synthetic machinery and cytoskeleton. FEBS Lett. 356: 89-93, 1994.
    • (1994) FEBS Lett. , vol.356 , pp. 89-93
    • Bektas, M.1    Nurten, R.2    Gurel, Z.3    Sayers, Z.4    Bermek, E.5
  • 13
    • 0027183089 scopus 로고
    • Cytochalasin modulation of nicotinic cholinergic receptor expression and muscarinic receptor function in human TE671/RD cells: A possible functional role of the cytoskeleton
    • BENCHERIF, M., AND R. J. LUKAS. Cytochalasin modulation of nicotinic cholinergic receptor expression and muscarinic receptor function in human TE671/RD cells: a possible functional role of the cytoskeleton. J. Neurochem. 61: 852-864, 1993.
    • (1993) J. Neurochem. , vol.61 , pp. 852-864
    • Bencherif, M.1    Lukas, R.J.2
  • 14
    • 0030586924 scopus 로고    scopus 로고
    • Force: A new structural control parameter?
    • BENSIMON, D. Force: a new structural control parameter? Structure 4: 885-889, 1996.
    • (1996) Structure , vol.4 , pp. 885-889
    • Bensimon, D.1
  • 15
    • 0031050310 scopus 로고    scopus 로고
    • Cytoskeletal and adhesion proteins as tumor suppressors
    • BENZEEV, A. Cytoskeletal and adhesion proteins as tumor suppressors. Curr. Opin. Cell Biol. 9: 99-108, 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 99-108
    • Benzeev, A.1
  • 17
    • 0029035088 scopus 로고
    • Cell cycle-related changes in F-actin distribution are correlated with glycolytic activity
    • BEREITER, H. J., C. STUBIG, AND V. HEYMANN. Cell cycle-related changes in F-actin distribution are correlated with glycolytic activity. Exp. Cell Res. 218: 551-560, 1995.
    • (1995) Exp. Cell Res. , vol.218 , pp. 551-560
    • Bereiter, H.J.1    Stubig, C.2    Heymann, V.3
  • 18
    • 0029589990 scopus 로고
    • Protein kinases as mediators of fluid shear stress stimulated signal transduction in endothelial cells: A hypothesis for calcium-dependent and calcium-independent events activated by flow
    • BERK, B. C., M. A. CORSON, T. E. PETERSON, AND H. TSENG. Protein kinases as mediators of fluid shear stress stimulated signal transduction in endothelial cells: a hypothesis for calcium-dependent and calcium-independent events activated by flow. J. Biomech. 28: 1439-1450, 1995.
    • (1995) J. Biomech. , vol.28 , pp. 1439-1450
    • Berk, B.C.1    Corson, M.A.2    Peterson, T.E.3    Tseng, H.4
  • 19
    • 0030266491 scopus 로고    scopus 로고
    • Involvement of microtubules in the control of adhesion-dependent signal transduction
    • BERSHADSKY, A., A. CHAUSOVSKY, E. BECKER, A. LYUBIMOVA, AND B. GEIGER. Involvement of microtubules in the control of adhesion-dependent signal transduction. Curr. Biol. 6: 1279-1289, 1996.
    • (1996) Curr. Biol. , vol.6 , pp. 1279-1289
    • Bershadsky, A.1    Chausovsky, A.2    Becker, E.3    Lyubimova, A.4    Geiger, B.5
  • 21
    • 0027049222 scopus 로고
    • Fluid shear stress stimulates membrane phospholipid metabolism in cultured human endothelial cells
    • BHAGYALAKSHMI, A., F. BERTHIAUME, K. M. REICH, AND J. A. FRANGOS. Fluid shear stress stimulates membrane phospholipid metabolism in cultured human endothelial cells. J. Vasc. Res. 29: 443-449, 1992.
    • (1992) J. Vasc. Res. , vol.29 , pp. 443-449
    • Bhagyalakshmi, A.1    Berthiaume, F.2    Reich, K.M.3    Frangos, J.A.4
  • 23
    • 0030001021 scopus 로고    scopus 로고
    • Protein kinase C betaII specifically binds to and is activated by F-actin
    • BLOBE, G. C., D. S. STRIBLING, D. FABBRO, S. STABEL, AND Y. A. HANNUN. Protein kinase C betaII specifically binds to and is activated by F-actin. J. Biol. Chem. 271: 15823-15830, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15823-15830
    • Blobe, G.C.1    Stribling, D.S.2    Fabbro, D.3    Stabel, S.4    Hannun, Y.A.5
  • 24
    • 0030272704 scopus 로고    scopus 로고
    • Intermediate filament-mediated stretch-induced changes in chromatin: A hypothesis for growth initiation in cardiac myocytes
    • BLOOM, S., V. G. LOCKARD, AND M. BLOOM. Intermediate filament-mediated stretch-induced changes in chromatin: a hypothesis for growth initiation in cardiac myocytes. J. Mol. Cell. Cardiol. 28: 2123-2127, 1996.
    • (1996) J. Mol. Cell. Cardiol. , vol.28 , pp. 2123-2127
    • Bloom, S.1    Lockard, V.G.2    Bloom, M.3
  • 26
    • 0028788309 scopus 로고
    • Microfilament reorganization during apoptosis: The role of Gas2, a possible substrate for ICE-like proteases
    • BRANCOLINI, C., M. BENEDETTI, AND C. SCHNEIDER. Microfilament reorganization during apoptosis: the role of Gas2, a possible substrate for ICE-like proteases. EMBO J. 14: 5179-5190, 1995.
    • (1995) EMBO J. , vol.14 , pp. 5179-5190
    • Brancolini, C.1    Benedetti, M.2    Schneider, C.3
  • 27
    • 0029784514 scopus 로고    scopus 로고
    • The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases
    • BRILL, S., S. LI, C. W. LYMAN, D. M. CHURCH, J. J. WASMUTH, L. WEISSBACH, A. BERNARDS, AND A. J. SNIJDERS. The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases. Mol. Cell. Biol. 16: 4869-4878, 1996.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4869-4878
    • Brill, S.1    Li, S.2    Lyman, C.W.3    Church, D.M.4    Wasmuth, J.J.5    Weissbach, L.6    Bernards, A.7    Snijders, A.J.8
  • 28
    • 0030957458 scopus 로고    scopus 로고
    • Actin is cleaved during constitutive apoptosis
    • BROWN, S. B., K. BAILEY, AND J. SAVILL. Actin is cleaved during constitutive apoptosis. Biochem. J. 323: 233-237, 1997.
    • (1997) Biochem. J. , vol.323 , pp. 233-237
    • Brown, S.B.1    Bailey, K.2    Savill, J.3
  • 30
    • 0029646170 scopus 로고
    • Biological levels
    • BUXBAUM, R. Biological levels. Nature 373: 567-568, 1995.
    • (1995) Nature , vol.373 , pp. 567-568
    • Buxbaum, R.1
  • 31
    • 0029102078 scopus 로고
    • + channel regulation
    • + channel regulation. Kidney Int. 48: 970-984, 1995.
    • (1995) Kidney Int. , vol.48 , pp. 970-984
    • Cantiello, H.F.1
  • 32
    • 0029956147 scopus 로고    scopus 로고
    • Role of the actin cytoskeleton in the regulation of the cystic flbrosis transmembrane conductance regulator
    • CANTIELLO, H. F. Role of the actin cytoskeleton in the regulation of the cystic flbrosis transmembrane conductance regulator. Exp. Physiol. 81: 505-514, 1996.
    • (1996) Exp. Physiol. , vol.81 , pp. 505-514
    • Cantiello, H.F.1
  • 33
    • 0027462156 scopus 로고
    • Actin-binding protein contributes to cell volume regulatory ion channel activation in melanoma cells
    • CANTIELLO, H. F., A. G. PRAT, J. V. BONVENTRE, C. C. CUNNINGHAM, J. H. HARTWIG, AND D. A. AUSIELLO. Actin-binding protein contributes to cell volume regulatory ion channel activation in melanoma cells. J. Biol. Chem. 268: 4596-4599, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4596-4599
    • Cantiello, H.F.1    Prat, A.G.2    Bonventre, J.V.3    Cunningham, C.C.4    Hartwig, J.H.5    Ausiello, D.A.6
  • 34
    • 0024588255 scopus 로고
    • Gelsolin modulation in epithelial and stromal cells of mammary carcinoma
    • CHAPONNIER, C., AND G. GABBIANI. Gelsolin modulation in epithelial and stromal cells of mammary carcinoma. Am. J. Pathol. 134: 597-603, 1989.
    • (1989) Am. J. Pathol. , vol.134 , pp. 597-603
    • Chaponnier, C.1    Gabbiani, G.2
  • 36
    • 0029822443 scopus 로고    scopus 로고
    • Activation of actin-cleavable interleukin 1β-converting enzyme (ICE) family protease CPP-32 during chemotherapeutic agent-induced apoptosis in ovarian carcinoma cells
    • CHEN, Z., M. NAITO, T. MASHIMA, AND T. TSURUO. Activation of actin-cleavable interleukin 1β-converting enzyme (ICE) family protease CPP-32 during chemotherapeutic agent-induced apoptosis in ovarian carcinoma cells. Cancer Res. 56: 5224-5229, 1996.
    • (1996) Cancer Res. , vol.56 , pp. 5224-5229
    • Chen, Z.1    Naito, M.2    Mashima, T.3    Tsuruo, T.4
  • 37
    • 0030994017 scopus 로고    scopus 로고
    • Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages
    • CHOQUET, D., D. P. FELSENFELD, AND M. P. SHEETZ. Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages. Cell 88: 39-48, 1997.
    • (1997) Cell , vol.88 , pp. 39-48
    • Choquet, D.1    Felsenfeld, D.P.2    Sheetz, M.P.3
  • 38
    • 0031042994 scopus 로고    scopus 로고
    • Intermediate filaments and cytoplasmic networking: New connections and more functions
    • CHOU, Y. H., O. SKALLI, AND R. D. GOLDMAN. Intermediate filaments and cytoplasmic networking: new connections and more functions. Curr. Opin. Cell Biol. 9: 49-53, 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 49-53
    • Chou, Y.H.1    Skalli, O.2    Goldman, R.D.3
  • 39
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • CHRZANOWSKA, W. M., AND K. BURRIDGE. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133: 1403-1415, 1996.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska, W.M.1    Burridge, K.2
  • 40
    • 0029558724 scopus 로고
    • Immunocytochemical localization of protein kinases Yes and Src in amoeboid microglia in culture: Association of Yes kinase with vimentin intermediate filaments
    • CIESIELSKI-TRESKA, J., G. ULRICH, S. CHASSEROT-GOLAZ, AND D. AUNIS. Immunocytochemical localization of protein kinases Yes and Src in amoeboid microglia in culture: association of Yes kinase with vimentin intermediate filaments. Eur. J. Cell Biol. 68: 369-376, 1995.
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 369-376
    • Ciesielski-Treska, J.1    Ulrich, G.2    Chasserot-Golaz, S.3    Aunis, D.4
  • 41
    • 0021159838 scopus 로고
    • Intracellular water and the cytomatrix: Some methods of study and current views
    • CLEGG, J. S. Intracellular water and the cytomatrix: some methods of study and current views. J. Cell Biol. 99: 167s-171s, 1984.
    • (1984) J. Cell Biol. , vol.99
    • Clegg, J.S.1
  • 42
    • 0027333420 scopus 로고
    • Life at the leading edge: The formation of cell protrusions
    • CONDEELIS, J. Life at the leading edge: the formation of cell protrusions. Annu. Rev. Cell Biol. 9: 411-444, 1993.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 411-444
    • Condeelis, J.1
  • 43
    • 0027276953 scopus 로고
    • Cytoskeleton and ion movements during volume regulation in cultured PC12 cells
    • CORNET, M., J. UBL, AND H. A. KOLB. Cytoskeleton and ion movements during volume regulation in cultured PC12 cells. J. Membr. Biol. 133: 161-170, 1993.
    • (1993) J. Membr. Biol. , vol.133 , pp. 161-170
    • Cornet, M.1    Ubl, J.2    Kolb, H.A.3
  • 46
    • 0031030244 scopus 로고    scopus 로고
    • Transient expression of epidermal filaggrin in cultured cells causes collapse of intermediate filament networks with alteration of cell shape and nuclear integrity
    • DALE, B. A., R. B. PRESLAND, S. P. LEWIS, R. A. UNDERWOOD, AND P. FLECKMAN. Transient expression of epidermal filaggrin in cultured cells causes collapse of intermediate filament networks with alteration of cell shape and nuclear integrity. J. Invest. Dermatol. 108: 179-187, 1997.
    • (1997) J. Invest. Dermatol. , vol.108 , pp. 179-187
    • Dale, B.A.1    Presland, R.B.2    Lewis, S.P.3    Underwood, R.A.4    Fleckman, P.5
  • 47
    • 0027586393 scopus 로고
    • Intercellular and intracellular signals and their transduction via the plasma membrane-cytoskeleton interface
    • DAVIES, E. Intercellular and intracellular signals and their transduction via the plasma membrane-cytoskeleton interface. Semin. Cell Biol. 4: 139-147, 1993.
    • (1993) Semin. Cell Biol. , vol.4 , pp. 139-147
    • Davies, E.1
  • 48
    • 0029072762 scopus 로고
    • Flow-mediated endothelial mechanotransduction
    • DAVIES, P. F. Flow-mediated endothelial mechanotransduction. Physiol. Rev. 75: 519-560, 1995.
    • (1995) Physiol. Rev. , vol.75 , pp. 519-560
    • Davies, P.F.1
  • 50
    • 0030878051 scopus 로고    scopus 로고
    • Gelsolin activates DNase I in vitro and cystic fibrosis sputum
    • DAVOODIAN, K., B. W. RITCHINGS, R. RAMPHAL, AND M. R. BUBB. Gelsolin activates DNase I in vitro and cystic fibrosis sputum. Biochemistry 36: 9637-9641, 1997.
    • (1997) Biochemistry , vol.36 , pp. 9637-9641
    • Davoodian, K.1    Ritchings, B.W.2    Ramphal, R.3    Bubb, M.R.4
  • 51
    • 0028262115 scopus 로고
    • Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit
    • DEVARAJAN, P., D. A. SCARAMUZZINO, AND J. S. MORROW. Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit. Proc. Natl. Acad. Sci. USA 91: 2965-2969, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2965-2969
    • Devarajan, P.1    Scaramuzzino, D.A.2    Morrow, J.S.3
  • 52
    • 0028170633 scopus 로고
    • Mechanically induced calcium mobilization in cultured endothelial cells is dependent on actin and phospholipase
    • DIAMOND, S. L., F. SACHS, AND W. J. SIGURDSON. Mechanically induced calcium mobilization in cultured endothelial cells is dependent on actin and phospholipase. Arterioscler. Thromb. 14: 2000-2006, 1994.
    • (1994) Arterioscler. Thromb. , vol.14 , pp. 2000-2006
    • Diamond, S.L.1    Sachs, F.2    Sigurdson, W.J.3
  • 53
    • 0029853096 scopus 로고    scopus 로고
    • Biochemical isolation of a membrane microdomain from resting platelets highly enriched in the plasma membrane glycoprotein CD36
    • DORAHY, D. J., L. F. LINCZ, C. J. MELDRUM, AND G. F. BURNS. Biochemical isolation of a membrane microdomain from resting platelets highly enriched in the plasma membrane glycoprotein CD36. Biochem. J. 67-72, 1996.
    • (1996) Biochem. J. , pp. 67-72
    • Dorahy, D.J.1    Lincz, L.F.2    Meldrum, C.J.3    Burns, G.F.4
  • 55
    • 0029020353 scopus 로고
    • pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1 alpha
    • EDMONDS, B. T., J. MURRAY, AND J. CONDEELIS. pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1 alpha. J. Biol. Chem. 270: 15222-15230, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15222-15230
    • Edmonds, B.T.1    Murray, J.2    Condeelis, J.3
  • 56
    • 0027409180 scopus 로고
    • Sodium-dependent regulation of epithelial sodium channel densities in frog skin: A role for the cytoskeleton
    • ELS, W. J., AND K. Y. CHOU. Sodium-dependent regulation of epithelial sodium channel densities in frog skin: a role for the cytoskeleton. J. Physiol. (Lond.). 462: 447-464, 1993.
    • (1993) J. Physiol. (Lond.) , vol.462 , pp. 447-464
    • Els, W.J.1    Chou, K.Y.2
  • 57
    • 0021219218 scopus 로고
    • Epithelial structure revealed by chemical dissection and unembedded electron microscopy
    • FEY, E. G., D. G. CAPCO, G. KROCHMALNIC, AND S. PENMAN. Epithelial structure revealed by chemical dissection and unembedded electron microscopy. J. Cell Biol. 99: 203s-208s, 1984.
    • (1984) J. Cell Biol. , vol.99
    • Fey, E.G.1    Capco, D.G.2    Krochmalnic, G.3    Penman, S.4
  • 58
    • 0021244964 scopus 로고
    • Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: Three-dimensional organization and protein composition
    • FEY, E. G., K. M. WAN, AND S. PENMAN. Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: three-dimensional organization and protein composition. J. Cell Biol. 98: 1973-1984, 1984.
    • (1984) J. Cell Biol. , vol.98 , pp. 1973-1984
    • Fey, E.G.1    Wan, K.M.2    Penman, S.3
  • 59
    • 0030482560 scopus 로고    scopus 로고
    • Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins
    • FINCHAM, V. J., M. UNLU, V. G. BRUNTON, J. D. PITTS, J. A. WYKE, AND M. C. FRAME. Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins. J. Cell Biol. 135: 1551-1564, 1996.
    • (1996) J. Cell Biol. , vol.135 , pp. 1551-1564
    • Fincham, V.J.1    Unlu, M.2    Brunton, V.G.3    Pitts, J.D.4    Wyke, J.A.5    Frame, M.C.6
  • 62
    • 0029331876 scopus 로고
    • Biological specificity and measurable physical properties of cell surface receptors and their possible role in signal transduction through the cytoskeleton
    • FORGACS, G. Biological specificity and measurable physical properties of cell surface receptors and their possible role in signal transduction through the cytoskeleton. Biochem. Cell. Biol. 73: 317-326, 1995.
    • (1995) Biochem. Cell. Biol. , vol.73 , pp. 317-326
    • Forgacs, G.1
  • 63
    • 0029011651 scopus 로고
    • On the possible role of cytoskeletal filamentous networks in intracellular signaling: An approach based on percolation
    • FORGACS, G. On the possible role of cytoskeletal filamentous networks in intracellular signaling: an approach based on percolation. J. Cell Sci. 108: 2131-2143, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 2131-2143
    • Forgacs, G.1
  • 64
    • 0027404301 scopus 로고
    • Regulation of ion channel distribution at synapses
    • FROEHNER, S. C. Regulation of ion channel distribution at synapses. Annu. Rev. Neurosci. 16: 347-368, 1993.
    • (1993) Annu. Rev. Neurosci. , vol.16 , pp. 347-368
    • Froehner, S.C.1
  • 66
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-actinin function
    • FUKAMI, K., K. FURUHASHI, M. INAGAKI, T. ENDO, S. HATANO, AND T. TAKENAWA. Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-actinin function. Nature 359: 150-152, 1992.
    • (1992) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5    Takenawa, T.6
  • 67
    • 0028954815 scopus 로고
    • Embryonic axis induction by the armadillo repeat domain of beta-catenin: Evidence for intracellular signaling
    • FUNAYAMA, N., F. FAGOTTO, P. MCCREA, AND B. M. GUMBINER. Embryonic axis induction by the armadillo repeat domain of beta-catenin: evidence for intracellular signaling. J. Cell Biol. 128: 959-968, 1995.
    • (1995) J. Cell Biol. , vol.128 , pp. 959-968
    • Funayama, N.1    Fagotto, F.2    Mccrea, P.3    Gumbiner, B.M.4
  • 71
    • 0031054182 scopus 로고    scopus 로고
    • Reversible translocation of phosphoinositide 3-kinase to the cytoskeleton of ADP-aggregated human phosphatidylinositol (3,4)-bisphosphate
    • GACHET, C., B. PAYRASTRE, C. GUINEBAULT, C TRUMEL, P. OHLMANN, G. MAUCO, J. P. CAZENAVE, M. PLANTAVID, AND H. CHAP. Reversible translocation of phosphoinositide 3-kinase to the cytoskeleton of ADP-aggregated human phosphatidylinositol (3,4)-bisphosphate. J. Biol. Chem. 272: 4850-4854, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4850-4854
    • Gachet, C.1    Payrastre, B.2    Guinebault, C.3    Trumel, C.4    Ohlmann, P.5    Mauco, G.6    Cazenave, J.P.7    Plantavid, M.8    Chap, H.9
  • 72
    • 0025855929 scopus 로고
    • Binding of sugar phosphates, inositol phosphates and phosphorylated amino acids to actin
    • GAERTNER, A., G. W. MAYR, AND A. WEGNER. Binding of sugar phosphates, inositol phosphates and phosphorylated amino acids to actin. Eur. J. Biochem. 198: 67-71, 1991.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 67-71
    • Gaertner, A.1    Mayr, G.W.2    Wegner, A.3
  • 73
    • 0028081489 scopus 로고
    • Inactivation of L-type Ca channels in embryonic chick ventricle cells: Dependence on the cytoskeletal agents colchicine and taxol
    • GALLI, A., AND L. J. DEFELICE. Inactivation of L-type Ca channels in embryonic chick ventricle cells: dependence on the cytoskeletal agents colchicine and taxol. Biophys. J. 67: 2296-2304, 1994.
    • (1994) Biophys. J. , vol.67 , pp. 2296-2304
    • Galli, A.1    Defelice, L.J.2
  • 74
    • 0029115973 scopus 로고
    • Taxol cytotoxicity on human leukemia cell lines is a function of their susceptibility to programmed cell death
    • GANGEMI, R. M., M. TISO, C. MARCHETTI, A. B. SEVERI, AND M. FABBI. Taxol cytotoxicity on human leukemia cell lines is a function of their susceptibility to programmed cell death. Cancer Chemother. Pharmacol. 36: 385-392, 1995.
    • (1995) Cancer Chemother. Pharmacol. , vol.36 , pp. 385-392
    • Gangemi, R.M.1    Tiso, M.2    Marchetti, C.3    Severi, A.B.4    Fabbi, M.5
  • 75
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate
    • GILMORE, A., AND K. BURRIDGE. Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate. Nature 381: 531-535, 1996.
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.1    Burridge, K.2
  • 76
    • 0027194031 scopus 로고
    • Characterization of distinct tethering and intracellular targeting domains in AKAP75, a protein that links cAMP-dependent protein kinase II beta to the cytoskeleton
    • GLANTZ, S. B., Y. LI, AND C. S. RUBIN. Characterization of distinct tethering and intracellular targeting domains in AKAP75, a protein that links cAMP-dependent protein kinase II beta to the cytoskeleton J. Biol. Chem. 268: 12796-12804, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12796-12804
    • Glantz, S.B.1    Li, Y.2    Rubin, C.S.3
  • 78
    • 0031020163 scopus 로고    scopus 로고
    • Calcium ions and tyrosine phosphorylation interact coordinately with actin to regulate cytoprotective responses to stretching
    • GLOGAUER, M., P. ARORA, G. YAO, I. SOKHOLOV, J. FERRIER, AND C. MCCULLOCH. Calcium ions and tyrosine phosphorylation interact coordinately with actin to regulate cytoprotective responses to stretching. J. Cell Sci. 110: 11-21, 1997.
    • (1997) J. Cell Sci. , vol.110 , pp. 11-21
    • Glogauer, M.1    Arora, P.2    Yao, G.3    Sokholov, I.4    Ferrier, J.5    Mcculloch, C.6
  • 80
    • 0029795964 scopus 로고    scopus 로고
    • The function of intermediate filaments in cell shape and cytoskeletal integrity
    • GOLDMAN, R. D., S. KHUON, Y. H. CHOU, P. OPAL, AND P. M. STEINERT. The function of intermediate filaments in cell shape and cytoskeletal integrity. J. Cell Biol. 134: 971-983, 1996.
    • (1996) J. Cell Biol. , vol.134 , pp. 971-983
    • Goldman, R.D.1    Khuon, S.2    Chou, Y.H.3    Opal, P.4    Steinert, P.M.5
  • 81
    • 0025760751 scopus 로고
    • Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation
    • GOLDSCHMIDT, C. P., J. W. KIM, L. M. MACHESKY, S. G. RHEE, AND T. D. POLLARD. Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation. Science 251: 1231-1233, 1991.
    • (1991) Science , vol.251 , pp. 1231-1233
    • Goldschmidt, C.P.1    Kim, J.W.2    Machesky, L.M.3    Rhee, S.G.4    Pollard, T.D.5
  • 84
    • 0025925359 scopus 로고
    • Interaction of pp60c-src, phospholipase C, inositol-lipid, and diacyglycerol kinases with the cytoskeletons of thrombin-stimulated platelets
    • GRONDIN, P., M. PLANTAVID, C. SULTAN, M. BRETON, G. MAUCO, AND H. CHAP. Interaction of pp60c-src, phospholipase C, inositol-lipid, and diacyglycerol kinases with the cytoskeletons of thrombin-stimulated platelets. J. Biol. Chem. 266: 15705-15709, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15705-15709
    • Grondin, P.1    Plantavid, M.2    Sultan, C.3    Breton, M.4    Mauco, G.5    Chap, H.6
  • 85
    • 0029584101 scopus 로고
    • Compression-induced changes in the shape and volume of the chondrocyte nucleus
    • GUILAK, F. Compression-induced changes in the shape and volume of the chondrocyte nucleus. J. Biomech. 28: 1529-1541, 1995.
    • (1995) J. Biomech. , vol.28 , pp. 1529-1541
    • Guilak, F.1
  • 86
    • 0027723788 scopus 로고
    • Catenins as mediators of the cytoplasmic functions of cadherins
    • GUMBINER, B. M., AND P. D. MCCREA. Catenins as mediators of the cytoplasmic functions of cadherins. J. Cell Sci. Suppl. 17: 155-158, 1993.
    • (1993) J. Cell Sci. Suppl. , vol.17 , pp. 155-158
    • Gumbiner, B.M.1    Mccrea, P.D.2
  • 87
    • 0028264160 scopus 로고
    • Luminal communication between intracellular calcium stores modulated by GTP and the cytoskeleton
    • HAJNOCZKY, G., C. LIN, AND A. P. THOMAS. Luminal communication between intracellular calcium stores modulated by GTP and the cytoskeleton. J. Biol. Chem. 269: 10280-10287, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10280-10287
    • Hajnoczky, G.1    Lin, C.2    Thomas, A.P.3
  • 88
    • 0031035693 scopus 로고    scopus 로고
    • Bcl2 is the guardian of microtubule integrity
    • HALDAR, S., A. BASU, AND C. M. CROCE. Bcl2 is the guardian of microtubule integrity. Cancer Res. 57: 229-233, 1997.
    • (1997) Cancer Res. , vol.57 , pp. 229-233
    • Haldar, S.1    Basu, A.2    Croce, C.M.3
  • 89
    • 0028024709 scopus 로고
    • Molecular interactions between G-actin, DNase I and the beta-thymosins in apoptosis: A hypothesis
    • HALL, A. K. Molecular interactions between G-actin, DNase I and the beta-thymosins in apoptosis: a hypothesis. Med Hypoth. 43: 125-131, 1994.
    • (1994) Med Hypoth. , vol.43 , pp. 125-131
    • Hall, A.K.1
  • 90
    • 0028819945 scopus 로고
    • Thymosin beta-10 accelerates apoptosis
    • HALL, A. K. Thymosin beta-10 accelerates apoptosis. Cell. Mol. Biol. Res. 41: 167-180, 1995.
    • (1995) Cell. Mol. Biol. Res. , vol.41 , pp. 167-180
    • Hall, A.K.1
  • 91
    • 0028985227 scopus 로고
    • Requirement of a colchicine-sensitive component of the cytoskeleton for acetylcholine receptor recovery
    • HARDWICK, J. C., AND R. L. PARSONS. Requirement of a colchicine-sensitive component of the cytoskeleton for acetylcholine receptor recovery. Br. J. Pharmacol. 114: 442-446, 1995.
    • (1995) Br. J. Pharmacol. , vol.114 , pp. 442-446
    • Hardwick, J.C.1    Parsons, R.L.2
  • 93
    • 0028241496 scopus 로고
    • Mechanical tension as a regulator of axonal development
    • HEIDEMANN, S. R., AND R. E. BUXBAUM. Mechanical tension as a regulator of axonal development. Neurotoxicology 15: 95-107, 1994.
    • (1994) Neurotoxicology , vol.15 , pp. 95-107
    • Heidemann, S.R.1    Buxbaum, R.E.2
  • 95
    • 0028948121 scopus 로고
    • Growth cone enrichment and cytoskeletal association of non-receptor tyrosine kinases
    • HELMKE, S., AND K. H. PFENNINGER. Growth cone enrichment and cytoskeletal association of non-receptor tyrosine kinases. Cell. Motil. Cytoskeleton 30: 194-207, 1995.
    • (1995) Cell. Motil. Cytoskeleton , vol.30 , pp. 194-207
    • Helmke, S.1    Pfenninger, K.H.2
  • 96
    • 0029827247 scopus 로고    scopus 로고
    • 2 (4,5) levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton
    • 2 (4,5) levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton. EMBO J. 15: 6516-6524, 1996.
    • (1996) EMBO J. , vol.15 , pp. 6516-6524
    • Hinchliffe, K.A.1    Irvine, R.F.2    Divecha, N.3
  • 97
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • HIRAO, M., N. SATO, T. KONDO, S. YONEMURA, M. MONDEN, T. SASAKI, Y. TAKAI, S. TSUKITA, AND S. TSUKITA. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J. Cell Biol. 135: 37-51, 1996.
    • (1996) J. Cell Biol. , vol.135 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6    Takai, Y.7    Tsukita, S.8    Tsukita, S.9
  • 98
    • 0027360142 scopus 로고
    • A neurofilament-associated kinase phosphorylates only a subset of sites in the tail of chicken midsize neurofilament protein
    • HOLLANDER, B. A., C. AYYUB, G. SHAW, AND G. S. BENNETT. A neurofilament-associated kinase phosphorylates only a subset of sites in the tail of chicken midsize neurofilament protein. J. Neurochem. 61: 2115-2123, 1993.
    • (1993) J. Neurochem. , vol.61 , pp. 2115-2123
    • Hollander, B.A.1    Ayyub, C.2    Shaw, G.3    Bennett, G.S.4
  • 99
    • 0030272844 scopus 로고    scopus 로고
    • The compartmentalization of protein synthesis: Importance of cytoskeleon and role in RNA targetting
    • HOVLAND, R., J. HESKETH, AND I. PRYME. The compartmentalization of protein synthesis: importance of cytoskeleon and role in RNA targetting. Int. J. Cell Biol. 28: 1089-1105, 1996.
    • (1996) Int. J. Cell Biol. , vol.28 , pp. 1089-1105
    • Hovland, R.1    Hesketh, J.2    Pryme, I.3
  • 100
    • 0028572556 scopus 로고
    • E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton
    • HULSKEN, J., W. BIRCHMEIER, AND J. BEHRENS. E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton. J. Cell Biol. 2061-2069, 1994.
    • (1994) J. Cell Biol. , pp. 2061-2069
    • Hulsken, J.1    Birchmeier, W.2    Behrens, J.3
  • 101
    • 0001169160 scopus 로고    scopus 로고
    • Activation of phospholipase C-gamma by the concerted action of tau proteins and arachidonic acid
    • HWANG, S., D.-Y. JHON, Y. BAE, J. KIM, AND S. RHEE. Activation of phospholipase C-gamma by the concerted action of tau proteins and arachidonic acid. J. Biol. Chem. 271: 18342-18349, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18342-18349
    • Hwang, S.1    Jhon, D.-Y.2    Bae, Y.3    Kim, J.4    Rhee, S.5
  • 103
    • 0026245524 scopus 로고
    • Integrins as mechanochemical transducers
    • INGBER, D. Integrins as mechanochemical transducers. Curr. Opin. Cell Biol. 3: 841-848, 1991.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 841-848
    • Ingber, D.1
  • 104
    • 0030899760 scopus 로고    scopus 로고
    • Tensegrity: The architectural basis of cellular mechanotransduction
    • INGBER, D. Tensegrity: the architectural basis of cellular mechanotransduction. Annu. Rev. Physiol. 59: 575-599, 1997.
    • (1997) Annu. Rev. Physiol. , vol.59 , pp. 575-599
    • Ingber, D.1
  • 105
    • 0002497456 scopus 로고
    • Cells as tensegrity structures: Architectural regulation of histodifferentiation by physical forces transduced over basement membrane
    • edited by L. C. Andersson, C. G. Gahmberg, and P. Ekblom. Orlando, FL: Academic
    • INGBER, D. E., AND J. D. JAMIESON. Cells as tensegrity structures: architectural regulation of histodifferentiation by physical forces transduced over basement membrane. In: Gene Expression During Normal and Malignant Differentiation, edited by L. C. Andersson, C. G. Gahmberg, and P. Ekblom. Orlando, FL: Academic, 1985, p. 13-32.
    • (1985) Gene Expression during Normal and Malignant Differentiation , pp. 13-32
    • Ingber, D.E.1    Jamieson, J.D.2
  • 106
    • 0031569517 scopus 로고    scopus 로고
    • Fluid shear stress-mediated signal transduction: How do endothelial cells transduce mechanical force into biological responses?
    • ISHIDA, T., M. TAKAHASHI, M. A. CORSON, AND B. C. BERK. Fluid shear stress-mediated signal transduction: how do endothelial cells transduce mechanical force into biological responses? Ann. NY Acad. Sci. 811: 12-24, 1997.
    • (1997) Ann. NY Acad. Sci. , vol.811 , pp. 12-24
    • Ishida, T.1    Takahashi, M.2    Corson, M.A.3    Berk, B.C.4
  • 107
    • 0001969438 scopus 로고
    • Cell membranes and the cytoskeleton
    • Amsterdam: Elsevier
    • JANMEY, P. Cell membranes and the cytoskeleton. In: Structure and Dynamics of Membranes. Amsterdam: Elsevier, 1995, p. 805-850.
    • (1995) Structure and Dynamics of Membranes , pp. 805-850
    • Janmey, P.1
  • 108
    • 0028899770 scopus 로고
    • Medical aspects of the actin cytoskeleton
    • JANMEY, P., AND C. CHAPONNIER. Medical aspects of the actin cytoskeleton. Curr. Opin. Cell Biol. 7: 111-117, 1995.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 111-117
    • Janmey, P.1    Chaponnier, C.2
  • 110
    • 0028541012 scopus 로고
    • 2+-dependent inactivation in a mammalian central neuron involves the cytoskeleton
    • 2+-dependent inactivation in a mammalian central neuron involves the cytoskeleton. Pflügers Arch. 429: 14-21, 1994.
    • (1994) Pflügers Arch. , vol.429 , pp. 14-21
    • Johnson, B.D.1    Byerly, L.2
  • 111
    • 0027442924 scopus 로고
    • Internalization of activated platelet-derived growth factor receptor-phosphatidylinositol-3′ kinase complexes: Potential interactions with the microtubule cytoskeleton
    • KAPELLER, R., R. CHAKRABARTI, L. CANTLEY, F. FAY, AND S. CORVERA. Internalization of activated platelet-derived growth factor receptor-phosphatidylinositol-3′ kinase complexes: potential interactions with the microtubule cytoskeleton. Mol. Cell. Biol. 13: 6052-6063, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6052-6063
    • Kapeller, R.1    Chakrabarti, R.2    Cantley, L.3    Fay, F.4    Corvera, S.5
  • 112
    • 0028843916 scopus 로고
    • Phosphoinositide 3-kinase binds constitutively to alpha/beta-tubulin and binds to gamma-tubulin in response to insulin
    • KAPELLER, R., A. TOKER, L. C. CANTLEY, AND C. L. CARPENTER. Phosphoinositide 3-kinase binds constitutively to alpha/beta-tubulin and binds to gamma-tubulin in response to insulin. J. Biol. Chem. 270: 25985-25991, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25985-25991
    • Kapeller, R.1    Toker, A.2    Cantley, L.C.3    Carpenter, C.L.4
  • 113
    • 0026483847 scopus 로고
    • Talin anchors and nucleates actin filaments at lipid membranes. A direct demonstration
    • KAUFMANN, S., J. KAS, W. H. GOLDMANN, E. SACKMANN, AND G. ISENBERG. Talin anchors and nucleates actin filaments at lipid membranes. A direct demonstration. FEBS Lett. 314: 203-205, 1992.
    • (1992) FEBS Lett. , vol.314 , pp. 203-205
    • Kaufmann, S.1    Kas, J.2    Goldmann, W.H.3    Sackmann, E.4    Isenberg, G.5
  • 114
    • 0029876247 scopus 로고    scopus 로고
    • Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition
    • KAYALAR, C., T. ORD, M. P. TESTA, L. T. ZHONG, AND D. E. BREDESEN. Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition. Proc. Natl. Acad. Sci. USA 93: 2234-2238, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2234-2238
    • Kayalar, C.1    Ord, T.2    Testa, M.P.3    Zhong, L.T.4    Bredesen, D.E.5
  • 115
    • 0028800221 scopus 로고
    • Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain
    • KOLODNEY, M. S., AND E. L. ELSON. Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain. Proc. Natl. Acad. Sci. USA 92: 10252-10256, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10252-10256
    • Kolodney, M.S.1    Elson, E.L.2
  • 117
    • 0029779004 scopus 로고    scopus 로고
    • The GTPase-activating protein n-chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia
    • KOZMA, R., S. AHMED, A. BEST, AND L. LIM. The GTPase-activating protein n-chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia. Mol. Cell. Biol. 16: 5069-5080, 1996.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5069-5080
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 118
    • 0028067857 scopus 로고
    • Signal transduction and calcium: A suggested role for the cytoskeleton in inositol 1,4,5-trisphosphate action
    • KRAUS, F. N. Signal transduction and calcium: a suggested role for the cytoskeleton in inositol 1,4,5-trisphosphate action. Cell. Motil. Cytoskeleton 28: 279-284, 1994.
    • (1994) Cell. Motil. Cytoskeleton , vol.28 , pp. 279-284
    • Kraus, F.N.1
  • 120
    • 0030597056 scopus 로고    scopus 로고
    • Calcium storage and release properties of F-actin: Evidence for the involvement of F-actin in cellular calcium signaling
    • LANGE, K., AND U. BRANDT. Calcium storage and release properties of F-actin: evidence for the involvement of F-actin in cellular calcium signaling. FEBS Lett. 395: 137-142, 1996.
    • (1996) FEBS Lett. , vol.395 , pp. 137-142
    • Lange, K.1    Brandt, U.2
  • 121
    • 0030886975 scopus 로고    scopus 로고
    • p53-independent apoptosis induced by paclitaxel through an indirect mechanism
    • LANNI, J. S., S. W. LOWE, E. J. LICITRA, J. O. LIU, AND T. JACKS. p53-independent apoptosis induced by paclitaxel through an indirect mechanism. Proc. Natl. Acad. Sci. USA 94: 9679-9683, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9679-9683
    • Lanni, J.S.1    Lowe, S.W.2    Licitra, E.J.3    Liu, J.O.4    Jacks, T.5
  • 122
    • 0029891890 scopus 로고    scopus 로고
    • Bleb formation and F-actin distribution during mitosis and tumor necrosis factor-induced apoptosis
    • LASTER, S. M., AND J. J. MACKENZIE. Bleb formation and F-actin distribution during mitosis and tumor necrosis factor-induced apoptosis. Microsc. Res. Techn. 34: 272-280, 1996.
    • (1996) Microsc. Res. Techn. , vol.34 , pp. 272-280
    • Laster, S.M.1    Mackenzie, J.J.2
  • 123
    • 0016361516 scopus 로고
    • Actin is the naturally occurring inhibitor of deoxyribonuclease I
    • LAZARIDES, E., AND U. LINDBERG. Actin is the naturally occurring inhibitor of deoxyribonuclease I. Proc. Natl. Acad. Sci. USA 71: 4742-4746, 1974.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4742-4746
    • Lazarides, E.1    Lindberg, U.2
  • 124
    • 0027161621 scopus 로고
    • Interaction of phosphofructokinase with tubulin and microtubules. Quantitative evaluation of the mutual effects
    • LEHOTZKY, A., M. TELEGDI, K. LILIOM, AND J. OVADI. Interaction of phosphofructokinase with tubulin and microtubules. Quantitative evaluation of the mutual effects. J. Biol. Chem. 268: 10888-10894, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10888-10894
    • Lehotzky, A.1    Telegdi, M.2    Liliom, K.3    Ovadi, J.4
  • 126
    • 0026701552 scopus 로고
    • Age-dependent changes in the ultrastructure and in the molecular composition of rat brain microtubules
    • LETERRIER, J. F., AND J. EYER. Age-dependent changes in the ultrastructure and in the molecular composition of rat brain microtubules. J. Neurochem. 59: 1126-1137, 1992.
    • (1992) J. Neurochem. , vol.59 , pp. 1126-1137
    • Leterrier, J.F.1    Eyer, J.2
  • 127
    • 0030465874 scopus 로고    scopus 로고
    • Actin polymerization and depolymerization during apoptosis in HL-60 cells
    • (Cell Physiol. 40)
    • LEVEE, M. G., M. I. DABROWSKA, J. J. LELLI, AND D. B. HINSHAW. Actin polymerization and depolymerization during apoptosis in HL-60 cells. Am. J. Physiol. 271 (Cell Physiol. 40): C1981-C1992, 1996.
    • (1996) Am. J. Physiol. , vol.271
    • Levee, M.G.1    Dabrowska, M.I.2    Lelli, J.J.3    Hinshaw, D.B.4
  • 128
    • 0027983091 scopus 로고
    • Cytoskeletal regulation of ion channel distribution in the tip-growing organism Saprolegnia ferax
    • LEVINA, N. N., R. R. LEW, AND I. B. HEATH. Cytoskeletal regulation of ion channel distribution in the tip-growing organism Saprolegnia ferax. J. Cell Sci. 107: 127-134, 1994.
    • (1994) J. Cell Sci. , vol.107 , pp. 127-134
    • Levina, N.N.1    Lew, R.R.2    Heath, I.B.3
  • 129
    • 0028972040 scopus 로고
    • Modulation of a volume-regulated chloride current by F-actin
    • LEVITAN, I., C. ALMONTE, P. MOLLARD, AND S. S. GARBER. Modulation of a volume-regulated chloride current by F-actin. J. Membr. Biol. 147: 283-294, 1995.
    • (1995) J. Membr. Biol. , vol.147 , pp. 283-294
    • Levitan, I.1    Almonte, C.2    Mollard, P.3    Garber, S.S.4
  • 130
    • 0029904265 scopus 로고    scopus 로고
    • A kinase anchor protein 75 targets regulatory (RII) subunits of cAMP-dependent protein kinase II to the cortical actin cytoskeleton in non-neuronal cells
    • LI, Y., C. NDUBUKA, AND C. S. RUBIN. A kinase anchor protein 75 targets regulatory (RII) subunits of cAMP-dependent protein kinase II to the cortical actin cytoskeleton in non-neuronal cells. J. Biol. Chem. 271: 16862-16869, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16862-16869
    • Li, Y.1    Ndubuka, C.2    Rubin, C.S.3
  • 131
    • 0028910357 scopus 로고
    • Mutagenesis of the regulatory subunit (RD beta) of cAMP-dependent protein kinase II beta reveals hydrophobic amino acids that are essential for RII beta dimerization and/or anchoring RII beta to the cytoskeleton
    • LI, Y., AND C. S. RUBIN. Mutagenesis of the regulatory subunit (RD beta) of cAMP-dependent protein kinase II beta reveals hydrophobic amino acids that are essential for RII beta dimerization and/or anchoring RII beta to the cytoskeleton. J. Biol. Chem. 270: 1935-1944, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1935-1944
    • Li, Y.1    Rubin, C.S.2
  • 132
    • 0030857803 scopus 로고    scopus 로고
    • Stress, apoptosis, and mitosis induce phosphorylation of human keratin 8 at Ser-73 in tissues and cultured cells
    • LIAO, J., N. O. KU, AND M. B. OMARY. Stress, apoptosis, and mitosis induce phosphorylation of human keratin 8 at Ser-73 in tissues and cultured cells. J. Biol. Chem. 272: 17565-17573, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17565-17573
    • Liao, J.1    Ku, N.O.2    Omary, M.B.3
  • 133
    • 0027430107 scopus 로고
    • A novel method to study the electrodynamic behavior of actin filaments. Evidence for cable-like properties of actin
    • LIN, E. C., AND H. F. CANTIELLO. A novel method to study the electrodynamic behavior of actin filaments. Evidence for cable-like properties of actin. Biophys. J. 65: 1371-1378, 1993.
    • (1993) Biophys. J. , vol.65 , pp. 1371-1378
    • Lin, E.C.1    Cantiello, H.F.2
  • 134
    • 0014036353 scopus 로고
    • Purification from calf spleen of two inhibitors of deoxyribonuclease. I. Physical and chemical characterization of the inhibitor II
    • LINDBERG, U. Purification from calf spleen of two inhibitors of deoxyribonuclease. I. Physical and chemical characterization of the inhibitor II. Biochemistry 6: 323-335, 1967.
    • (1967) Biochemistry , vol.6 , pp. 323-335
    • Lindberg, U.1
  • 135
    • 0028319060 scopus 로고
    • Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: Implications for human disease
    • LISANTI, M. P., P. E. SCHERER, J. VIDUGIRIENE, Z. TANG, V. A. HERMANOWSKI, Y. H. TU, R. F. COOK, AND M. SARGIACOMO. Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: implications for human disease. J. Cell Biol. 126: 111-126, 1994.
    • (1994) J. Cell Biol. , vol.126 , pp. 111-126
    • Lisanti, M.P.1    Scherer, P.E.2    Vidugiriene, J.3    Tang, Z.4    Hermanowski, V.A.5    Tu, Y.H.6    Cook, R.F.7    Sargiacomo, M.8
  • 137
    • 0029828821 scopus 로고    scopus 로고
    • F-actin sequesters elongation factor 1α from interaction with aminoacyl-tRNa in a pH-dependent reaction
    • LIU, G., J. TANG, B. T. EDMONDS, J. MURRAY, S. LEVIN, AND J. CONDEELIS. F-actin sequesters elongation factor 1α from interaction with aminoacyl-tRNA in a pH-dependent reaction. J. Cell Biol. 135: 953-963, 1996.
    • (1996) J. Cell Biol. , vol.135 , pp. 953-963
    • Liu, G.1    Tang, J.2    Edmonds, B.T.3    Murray, J.4    Levin, S.5    Condeelis, J.6
  • 139
    • 0025633236 scopus 로고
    • Identification of the MAP2- and P75-binding domain in the regulatory subunit (RII beta) of type II cAMP-dependent protein kinase. Cloning and expression of the cDNA for bovine brain RII beta
    • LUO, Z., B. SHAFIT-ZAGARDO, AND J. ERLICHMAN. Identification of the MAP2-and P75-binding domain in the regulatory subunit (RII beta) of type II cAMP-dependent protein kinase. Cloning and expression of the cDNA for bovine brain RII beta. J. Biol. Chem. 265: 21804-21810, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21804-21810
    • Luo, Z.1    Shafit-Zagardo, B.2    Erlichman, J.3
  • 140
    • 0028358761 scopus 로고
    • High-affinity binding and localization of the cyclic GMP-dependent protein kinase with the intermediate filament protein vimentin
    • MACMILLAN, C. L., AND T. M. LINCOLN. High-affinity binding and localization of the cyclic GMP-dependent protein kinase with the intermediate filament protein vimentin. Biochemistry 33: 8035-8043, 1994.
    • (1994) Biochemistry , vol.33 , pp. 8035-8043
    • Macmillan, C.L.1    Lincoln, T.M.2
  • 141
    • 0025834866 scopus 로고
    • Transmembrane molecular assemblies regulated by the greater cadherin family
    • MAGEE, A. I., AND R. S. BUXTON. Transmembrane molecular assemblies regulated by the greater cadherin family. Curr. Opin. Cell Biol. 3: 854-861, 1991.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 854-861
    • Magee, A.I.1    Buxton, R.S.2
  • 142
    • 0029115343 scopus 로고
    • Signal transduction by the alpha 6 beta 4 integrin: Distinct beta 4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes
    • MAINIERO, F., A. PEPE, K. K. WARY, L. SPINARDI, M. MOHAMMADI, J. SCHLESSINGER, AND F. G. GIANCOTTI. Signal transduction by the alpha 6 beta 4 integrin: distinct beta 4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes. EMBO J. 14: 4470-4481, 1995.
    • (1995) EMBO J. , vol.14 , pp. 4470-4481
    • Mainiero, F.1    Pepe, A.2    Wary, K.K.3    Spinardi, L.4    Mohammadi, M.5    Schlessinger, J.6    Giancotti, F.G.7
  • 143
    • 0031017220 scopus 로고    scopus 로고
    • Demonstration of mechanical connections between integrins cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure
    • MANIOTIS, A. J., C. S. CHEN, AND D. E. INGBER. Demonstration of mechanical connections between integrins cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure. Proc. Natl. Acad. Sci. USA 94: 849-854, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 849-854
    • Maniotis, A.J.1    Chen, C.S.2    Ingber, D.E.3
  • 146
    • 0021129923 scopus 로고
    • Interactions between glycolytic enzymes and components of the cytomatrix
    • MASTERS, C. Interactions between glycolytic enzymes and components of the cytomatrix. J. Cell Biol. 222s-225s, 1984.
    • (1984) J. Cell Biol.
    • Masters, C.1
  • 148
    • 0027176804 scopus 로고
    • Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown
    • MCNAMEE, H. P., D. E. INGBER, AND M. A. SCHWARTZ. Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown. J. Cell Biol. 121: 673-678, 1993.
    • (1993) J. Cell Biol. , vol.121 , pp. 673-678
    • Mcnamee, H.P.1    Ingber, D.E.2    Schwartz, M.A.3
  • 149
    • 0027536793 scopus 로고
    • An actin-binding function contributes to transformation by the Bcr-Abl oncoprotein of Philadelphia chromosome-positive human leukemias
    • MCWHIRTER, J. R., AND J. Y. WANG. An actin-binding function contributes to transformation by the Bcr-Abl oncoprotein of Philadelphia chromosome-positive human leukemias. EMBO J. 12: 1533-1546, 1993.
    • (1993) EMBO J. , vol.12 , pp. 1533-1546
    • Mcwhirter, J.R.1    Wang, J.Y.2
  • 150
    • 0029907075 scopus 로고    scopus 로고
    • The physics of lamellipodial protrusion
    • MOGILNER, A., AND G. OSTER. The physics of lamellipodial protrusion. Eur. Biophys. J. 25: 47-53, 1996.
    • (1996) Eur. Biophys. J. , vol.25 , pp. 47-53
    • Mogilner, A.1    Oster, G.2
  • 151
    • 0029943566 scopus 로고    scopus 로고
    • The pool of MAP kinase associated with microtubules is small but constitutively active
    • MORISHIMA, K. M., AND K. S. KOSIK. The pool of MAP kinase associated with microtubules is small but constitutively active. Mol. Biol. Cell 7: 893-905, 1996.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 893-905
    • Morishima, K.M.1    Kosik, K.S.2
  • 154
    • 0030471363 scopus 로고    scopus 로고
    • Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends
    • MURRAY, J. W., B. T. EDMONDS, G. LIU, AND J. CONDEELIS. Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends. J. Cell Biol. 135: 1309-1321, 1996.
    • (1996) J. Cell Biol. , vol.135 , pp. 1309-1321
    • Murray, J.W.1    Edmonds, B.T.2    Liu, G.3    Condeelis, J.4
  • 155
    • 0024549991 scopus 로고
    • Association of phosphatidylinositol kinase and phosphatidylinositol 4-phosphate kinase activities with the cytoskeleton in human platelets
    • NAHAS, N., M. PLANTAVID, G. MAUCO, AND H. CHAP. Association of phosphatidylinositol kinase and phosphatidylinositol 4-phosphate kinase activities with the cytoskeleton in human platelets. FEBS Lett. 264: 30-34, 1989.
    • (1989) FEBS Lett. , vol.264 , pp. 30-34
    • Nahas, N.1    Plantavid, M.2    Mauco, G.3    Chap, H.4
  • 156
    • 0029852050 scopus 로고    scopus 로고
    • Disruption of actin filaments increases the activity of sodium-conducting channels in human myeloid leukemia cells
    • NEGULYAEV, Y., E. VEDERNIKOVA, AND A. MAXIMOV. Disruption of actin filaments increases the activity of sodium-conducting channels in human myeloid leukemia cells. Mol. Biol. Cell. 7: 1857-1864, 1996.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 1857-1864
    • Negulyaev, Y.1    Vedernikova, E.2    Maximov, A.3
  • 157
    • 0028800154 scopus 로고
    • Identification of a phosphatidylinositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin
    • NIGGLI, V., C. ANDREOLI, C. ROY, AND P. MANGEAT. Identification of a phosphatidylinositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin. FEBS Lett 376: 172-176, 1995.
    • (1995) FEBS Lett , vol.376 , pp. 172-176
    • Niggli, V.1    Andreoli, C.2    Roy, C.3    Mangeat, P.4
  • 158
    • 0024761741 scopus 로고
    • The RII subunit of cAMP-dependent protein kinase binds to a common amino-terminal domain in microtubule-associated proteins 2A, 2B, and 2C
    • OBAR, R., J. DINGUS, H. BAYLEY, AND R. VALLEE. The RII subunit of cAMP-dependent protein kinase binds to a common amino-terminal domain in microtubule-associated proteins 2A, 2B, and 2C. Neuron 3: 639-645, 1989.
    • (1989) Neuron , vol.3 , pp. 639-645
    • Obar, R.1    Dingus, J.2    Bayley, H.3    Vallee, R.4
  • 160
    • 0028173799 scopus 로고
    • Differential binding of pp60c-src and pp60v-src to cytoskeleton is mediated by SH2 and catalytic domains
    • OKAMURA, H., AND M. D. RESH. Differential binding of pp60c-src and pp60v-src to cytoskeleton is mediated by SH2 and catalytic domains. Oncogene 9: 2293-2303, 1994.
    • (1994) Oncogene , vol.9 , pp. 2293-2303
    • Okamura, H.1    Resh, M.D.2
  • 161
    • 0028157445 scopus 로고
    • Transduction of membrane tension by the ion channel alamethicin
    • OPSAHL, L. R., AND W. W. WEBB. Transduction of membrane tension by the ion channel alamethicin. Biophys. J. 66: 71-74, 1994.
    • (1994) Biophys. J. , vol.66 , pp. 71-74
    • Opsahl, L.R.1    Webb, W.W.2
  • 162
    • 0029942021 scopus 로고    scopus 로고
    • Protein kinase C-delta associates with vimentin intermediate filaments in differentiated HL60 cells
    • OWEN, P. J., G. D. JOHNSON, AND J. M. LORD. Protein kinase C-delta associates with vimentin intermediate filaments in differentiated HL60 cells. Exp. Cell Res. 225: 366-373, 1996.
    • (1996) Exp. Cell Res. , vol.225 , pp. 366-373
    • Owen, P.J.1    Johnson, G.D.2    Lord, J.M.3
  • 163
    • 0030012116 scopus 로고    scopus 로고
    • Phase specific association of heterotrimeric GTP-binding proteins with the actin-based cytoskeleton during thrombin receptor-mediated platelet activation
    • OZAWA, K., M. TAKAHASHI, AND K. SOBUE. Phase specific association of heterotrimeric GTP-binding proteins with the actin-based cytoskeleton during thrombin receptor-mediated platelet activation. FEBS Lett. 382: 159-163, 1996.
    • (1996) FEBS Lett. , vol.382 , pp. 159-163
    • Ozawa, K.1    Takahashi, M.2    Sobue, K.3
  • 164
    • 0002215313 scopus 로고
    • Glycolysis in vivo: Fluorescence microscopy as a tool for studying enzyme organization in living cells
    • PAGLIARO, L. Glycolysis in vivo: fluorescence microscopy as a tool for studying enzyme organization in living cells. Adv. Mol. Cell. Biol. 11: 93-123, 1995.
    • (1995) Adv. Mol. Cell. Biol. , vol.11 , pp. 93-123
    • Pagliaro, L.1
  • 165
    • 0026698574 scopus 로고
    • 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells
    • PAGLIARO, L., AND D. L. TAYLOR. 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells. J. Cell Biol. 118: 859-863, 1992.
    • (1992) J. Cell Biol. , vol.118 , pp. 859-863
    • Pagliaro, L.1    Taylor, D.L.2
  • 167
    • 0025990831 scopus 로고
    • Phosphoinositide kinase, diacylglycerol kinase, and phospholipase C activities associated to the cytoskeleton: Effect of epidermal growth factor
    • PAYRASTRE, B., P. VAN BERGEN EN HENEGOUWEN, M. BRETON, J. DEN HARTIGH, M. PLANTAVID, A. J. VERKLEIJ, AND J. BOONSTRA. Phosphoinositide kinase, diacylglycerol kinase, and phospholipase C activities associated to the cytoskeleton: effect of epidermal growth factor. J. Cell Biol. 115: 121-128, 1991.
    • (1991) J. Cell Biol. , vol.115 , pp. 121-128
    • Payrastre, B.1    Van Bergen En Henegouwen, P.2    Breton, M.3    Den Hartigh, J.4    Plantavid, M.5    Verkleij, A.J.6    Boonstra, J.7
  • 168
    • 0030597277 scopus 로고    scopus 로고
    • Phospholipase C-gamma 1 binds to actin-cytoskeleton via its C-terminal SH2 domain in vitro
    • PEI, Z., L. YANG, AND J. R. WILLIAMSON. Phospholipase C-gamma 1 binds to actin-cytoskeleton via its C-terminal SH2 domain in vitro. Biochem. Biophys. Res. Commun. 228: 802-806, 1996.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 802-806
    • Pei, Z.1    Yang, L.2    Williamson, J.R.3
  • 169
    • 0027458695 scopus 로고
    • Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death)
    • PEITSCH, M. C., B. POLZAR, H. STEPHAN, T. CROMPTON, H. R. MACDONALD, H. G. MANNHERZ, AND J. TSCHOPP. Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death). EMBO J. 12: 371-377, 1993.
    • (1993) EMBO J. , vol.12 , pp. 371-377
    • Peitsch, M.C.1    Polzar, B.2    Stephan, H.3    Crompton, T.4    Macdonald, H.R.5    Mannherz, H.G.6    Tschopp, J.7
  • 170
    • 0029926545 scopus 로고    scopus 로고
    • Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains
    • PIKE, L. J., AND L. CASEY. Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains. J. Biol. Chem. 271: 26453-26456, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26453-26456
    • Pike, L.J.1    Casey, L.2
  • 171
    • 0023857288 scopus 로고
    • Association of deoxyribonuclease I with the pointed ends of actin filaments in human red blood cell membrane skeletons
    • PODOLSKI, J. L., AND T. L. STECK. Association of deoxyribonuclease I with the pointed ends of actin filaments in human red blood cell membrane skeletons. J. Biol. Chem. 263: 638-645, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 638-645
    • Podolski, J.L.1    Steck, T.L.2
  • 172
    • 0030052208 scopus 로고
    • RNA localization and the cytoskeleton in Drosophila oocytes
    • POKRYWKA, N. J. RNA localization and the cytoskeleton in Drosophila oocytes. Curr. Top. Dev. Biol. 31: 139-166, 1995.
    • (1995) Curr. Top. Dev. Biol. , vol.31 , pp. 139-166
    • Pokrywka, N.J.1
  • 174
    • 0028801698 scopus 로고
    • cAMP-independent regulation of CFTR by the actin cytoskeleton
    • (Cell Physiol. 36)
    • PRAT, A. G., Y. F. XIAO, D. A. AUSIELLO, AND H. F. CANTIELLO. cAMP-independent regulation of CFTR by the actin cytoskeleton. Am. J. Physiol. 267 (Cell Physiol. 36): C1552-C1561, 1995.
    • (1995) Am. J. Physiol. , vol.267
    • Prat, A.G.1    Xiao, Y.F.2    Ausiello, D.A.3    Cantiello, H.F.4
  • 175
    • 0030042104 scopus 로고    scopus 로고
    • Identification and localization of an actin-binding motif that is unique
    • PREKERIS, R., M. W. MAYHEW, J. B. COOPER, AND D. M. TERRIAN. Identification and localization of an actin-binding motif that is unique to the epsilon isoform of protein kinase C and participates in the regulation of synaptic function. J. Cell Biol. 132: 77-90, 1996.
    • (1996) J. Cell Biol. , vol.132 , pp. 77-90
    • Prekeris, R.1    Mayhew, M.W.2    Cooper, J.B.3    Terrian, D.M.4
  • 176
    • 0028012110 scopus 로고
    • Effect of cAMP on the association of small GTP-binding proteins with the cytoskeleton of human platelets
    • RAMASCHI, G., C. BALDUINI, M. TORTI, AND F. SINIGAGLIA. Effect of cAMP on the association of small GTP-binding proteins with the cytoskeleton of human platelets. Biochim. Biophys. Acta 1199: 20-26, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1199 , pp. 20-26
    • Ramaschi, G.1    Balduini, C.2    Torti, M.3    Sinigaglia, F.4
  • 177
    • 0029132731 scopus 로고
    • Hemodynamic forces are complex regulators of endothelial gene expression
    • RESNICK, N., AND M. J. GIMBRONE. Hemodynamic forces are complex regulators of endothelial gene expression. FASEB J. 9: 874-882, 1995.
    • (1995) FASEB J. , vol.9 , pp. 874-882
    • Resnick, N.1    Gimbrone, M.J.2
  • 178
    • 0029026860 scopus 로고
    • Association of mitogen-activated protein kinase with the microtubule cytoskeleton
    • RESZKA, A. A., R. SEGER, C. D. DILTZ, E. G. KREBS, AND E. H. FISCHER. Association of mitogen-activated protein kinase with the microtubule cytoskeleton. Proc. Natl. Acad. Sci. USA 92: 8881-8885, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8881-8885
    • Reszka, A.A.1    Seger, R.2    Diltz, C.D.3    Krebs, E.G.4    Fischer, E.H.5
  • 179
    • 0029995352 scopus 로고    scopus 로고
    • Mono-(2-ethylhexyl)-phthalate rapidly alters both Sertoli cell vimentin filaments and germ cell apoptosis in young rat testes
    • RICHBURG, J. H., AND K. BOEKELHEIDE. Mono-(2-ethylhexyl)-phthalate rapidly alters both Sertoli cell vimentin filaments and germ cell apoptosis in young rat testes. Toxicol. Appl. Pharmacol. 137: 42-50, 1996.
    • (1996) Toxicol. Appl. Pharmacol. , vol.137 , pp. 42-50
    • Richburg, J.H.1    Boekelheide, K.2
  • 180
    • 0026662546 scopus 로고
    • Signal transduction by neutrophil immunoglobulin G Fc receptors. Dissociation of intracytoplasmic calcium concentration rise from inositol 1,4,5-trisphosphate
    • ROSALES, C., AND E. J. BROWN. Signal transduction by neutrophil immunoglobulin G Fc receptors. Dissociation of intracytoplasmic calcium concentration rise from inositol 1,4,5-trisphosphate. J. Biol. Chem. 267: 5265-5271, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5265-5271
    • Rosales, C.1    Brown, E.J.2
  • 182
    • 0029902057 scopus 로고    scopus 로고
    • Microtubules can modulate pseudopod activity from a distance inside macrophages
    • ROSANIA, G. R., AND J. A. SWANSON. Microtubules can modulate pseudopod activity from a distance inside macrophages. Cell. Motil. Cytoskeleton 34: 230-245, 1996.
    • (1996) Cell. Motil. Cytoskeleton , vol.34 , pp. 230-245
    • Rosania, G.R.1    Swanson, J.A.2
  • 183
    • 0027258451 scopus 로고
    • Calcium-induced actin depolymerization reduces NMDA channel activity
    • ROSENMUND, C., AND G. L. WESTBROOK. Calcium-induced actin depolymerization reduces NMDA channel activity. Neuron 10: 805-814, 1993.
    • (1993) Neuron , vol.10 , pp. 805-814
    • Rosenmund, C.1    Westbrook, G.L.2
  • 184
    • 0028964437 scopus 로고
    • Cytoskeletal control of gene expression: Depolymerization of microtubules activates NF-kappa B
    • ROSETTE, C., AND M. KARIN. Cytoskeletal control of gene expression: depolymerization of microtubules activates NF-kappa B. J. Cell Biol. 128: 1111-1119, 1995.
    • (1995) J. Cell Biol. , vol.128 , pp. 1111-1119
    • Rosette, C.1    Karin, M.2
  • 185
    • 0027934665 scopus 로고
    • Tubulin-G protein association stabilizes GTP binding and activates GTPase: Cytoskeletal participation in neuronal signal transduction
    • ROYCHOWDHURY, S., AND M. M. RASENICK. Tubulin-G protein association stabilizes GTP binding and activates GTPase: cytoskeletal participation in neuronal signal transduction. Biochemistry 33: 9800-9805, 1994.
    • (1994) Biochemistry , vol.33 , pp. 9800-9805
    • Roychowdhury, S.1    Rasenick, M.M.2
  • 186
    • 0027235428 scopus 로고
    • G protein binding and G protein activation by nucleotide transfer involve distinct domains on tubulin: Regulation of signal transduction by cytoskeletal elements
    • ROYCHOWDHURY, S., N. WANG, AND M. M. RASENICK. G protein binding and G protein activation by nucleotide transfer involve distinct domains on tubulin: regulation of signal transduction by cytoskeletal elements. Biochemistry 32: 4955-4961, 1993.
    • (1993) Biochemistry , vol.32 , pp. 4955-4961
    • Roychowdhury, S.1    Wang, N.2    Rasenick, M.M.3
  • 187
    • 0024763898 scopus 로고
    • Localization and characterization of the binding site for the regulatory subunit of type II cAMP-dependent protein kinase on MAP2
    • RUBINO, H., M. DAMMERMAN, B. SHAFIT-ZAGARDO, AND J. ERLICHMAN. Localization and characterization of the binding site for the regulatory subunit of type II cAMP-dependent protein kinase on MAP2. Neuron 3: 631-638, 1989.
    • (1989) Neuron , vol.3 , pp. 631-638
    • Rubino, H.1    Dammerman, M.2    Shafit-Zagardo, B.3    Erlichman, J.4
  • 188
    • 0027184483 scopus 로고
    • Stimulus-induced dissociation of alpha subunits of heterotrimeric GTP-binding proteins from the cytoskeleton of human neutrophils
    • SARNDAHL, E., G. M. BOKOCH, O. STENDAHL, AND T. ANDERSSON. Stimulus-induced dissociation of alpha subunits of heterotrimeric GTP-binding proteins from the cytoskeleton of human neutrophils. Proc. Natl. Acad. Sci. USA 90: 6552-6556, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6552-6556
    • Sarndahl, E.1    Bokoch, G.M.2    Stendahl, O.3    Andersson, T.4
  • 189
    • 0027432754 scopus 로고
    • Cytochalasin-D treatment triggers premature apoptosis of insect ovarian follicle and nurse cells
    • SAUMAN, I., AND S. J. BERRY. Cytochalasin-D treatment triggers premature apoptosis of insect ovarian follicle and nurse cells. Int. J. Dev. Biol. 37: 441-450, 1993.
    • (1993) Int. J. Dev. Biol. , vol.37 , pp. 441-450
    • Sauman, I.1    Berry, S.J.2
  • 191
    • 0029791502 scopus 로고    scopus 로고
    • Transport of protein kinase C a into the nucleus requires intact cytoskeleton while the transport of a protein containing a canonical nuclear localization signal does not
    • SCHMALZ, D., F. KALKBRENNER, F. HUCHO, AND K. BUCHNER. Transport of protein kinase C a into the nucleus requires intact cytoskeleton while the transport of a protein containing a canonical nuclear localization signal does not. J. Cell Sci. 109: 2401-2406, 1996.
    • (1996) J. Cell Sci. , vol.109 , pp. 2401-2406
    • Schmalz, D.1    Kalkbrenner, F.2    Hucho, F.3    Buchner, K.4
  • 192
    • 0028246241 scopus 로고
    • Actin-based cytoskeleton regulates a chloride channel and cell volume in a renal cortical collecting duct cell line
    • SCHWIEBERT, E. M., J. W. MILLS, AND B. A. STANTON. Actin-based cytoskeleton regulates a chloride channel and cell volume in a renal cortical collecting duct cell line. J. Biol. Chem. 269: 7081-7089, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7081-7089
    • Schwiebert, E.M.1    Mills, J.W.2    Stanton, B.A.3
  • 193
    • 0026460555 scopus 로고
    • Effect of cytochalasin D, diphtheria toxin, and ricin on the localization of eukaryotic elongation factor 2 along actin filament bundles in fibroblasts
    • SHESTAKOVA, E. A., AND L. P. GAVRILOVA. Effect of cytochalasin D, diphtheria toxin, and ricin on the localization of eukaryotic elongation factor 2 along actin filament bundles in fibroblasts. Dokl. Akad. Nauk. 324: 196-199, 1992.
    • (1992) Dokl. Akad. Nauk. , vol.324 , pp. 196-199
    • Shestakova, E.A.1    Gavrilova, L.P.2
  • 195
    • 0027335514 scopus 로고
    • Study of localization of the protein-synthesizing machinery along actin filament bundles
    • SHESTAKOVA, E. A., L. P. MOTUZ, A. A. MININ, AND L. P. GAVRILOVA. Study of localization of the protein-synthesizing machinery along actin filament bundles. Cell Biol. Int. 17: 409-416, 1993.
    • (1993) Cell Biol. Int. , vol.17 , pp. 409-416
    • Shestakova, E.A.1    Motuz, L.P.2    Minin, A.A.3    Gavrilova, L.P.4
  • 196
    • 0029757471 scopus 로고    scopus 로고
    • Dominant negative inhibition of the association between beta-catenin and c-erbB-2 by N-terminally deleted beta-catenin suppresses the invasion and metastasis of cancer cells
    • SHIBATA, T., A. OCHIAI, Y. KANAI, S. AKIMOTO, M. GOTOH, N. YASUI, R. MACHINAMI, AND S. HIROHASHI. Dominant negative inhibition of the association between beta-catenin and c-erbB-2 by N-terminally deleted beta-catenin suppresses the invasion and metastasis of cancer cells. Oncogene 13: 883-889, 1996.
    • (1996) Oncogene , vol.13 , pp. 883-889
    • Shibata, T.1    Ochiai, A.2    Kanai, Y.3    Akimoto, S.4    Gotoh, M.5    Yasui, N.6    Machinami, R.7    Hirohashi, S.8
  • 198
    • 0029032179 scopus 로고
    • Mutational analysis of a putative polyphosphoinositide binding site in phospholipase C-beta 2
    • SIMOES, A. P., M. CAMPS, P. SCHNABEL, AND P. GIERSCHIK. Mutational analysis of a putative polyphosphoinositide binding site in phospholipase C-beta 2. FEBS Lett. 365: 155-158, 1995.
    • (1995) FEBS Lett. , vol.365 , pp. 155-158
    • Simoes, A.P.1    Camps, M.2    Schnabel, P.3    Gierschik, P.4
  • 199
    • 0028920630 scopus 로고
    • Characterization of putative polyphosphoinositide binding motifs from phospholipase C beta 2
    • SIMOES, A. P., J. REED, P. SCHNABEL, M. CAMPS, AND P. GIERSCHIK. Characterization of putative polyphosphoinositide binding motifs from phospholipase C beta 2. Biochemistry 34: 5113-5119, 1995.
    • (1995) Biochemistry , vol.34 , pp. 5113-5119
    • Simoes, A.P.1    Reed, J.2    Schnabel, P.3    Camps, M.4    Gierschik, P.5
  • 200
    • 0027379415 scopus 로고
    • A peptide corresponding to a potential polyphosphoinositide binding site of phospholipase C-beta 2 enhances its catalytic activity
    • SIMOES, A. P., P. SCHNABEL, R. PIPKORN, M. CAMPS, AND P. GIERSCHIK. A peptide corresponding to a potential polyphosphoinositide binding site of phospholipase C-beta 2 enhances its catalytic activity. FEBS Lett. 331: 248-251, 1993.
    • (1993) FEBS Lett. , vol.331 , pp. 248-251
    • Simoes, A.P.1    Schnabel, P.2    Pipkorn, R.3    Camps, M.4    Gierschik, P.5
  • 201
    • 0030475263 scopus 로고    scopus 로고
    • Profilin and gelsolin stimulate phosphatidylinositol 3-kinase activity
    • SINGH, S. S., A. CHAUHAN, N. MURAKAMI, AND V. P. CHAUHAN. Profilin and gelsolin stimulate phosphatidylinositol 3-kinase activity. Biochemistry 35: 16544-16549, 1996.
    • (1996) Biochemistry , vol.35 , pp. 16544-16549
    • Singh, S.S.1    Chauhan, A.2    Murakami, N.3    Chauhan, V.P.4
  • 203
    • 0023747169 scopus 로고
    • Application of percolation theory principles to the analysis of interaction of adenylate cyclase complex proteins in cell membranes
    • SOBOLEV, A. S., A. R. KAZAROV, AND A. A. ROSENKRANZ. Application of percolation theory principles to the analysis of interaction of adenylate cyclase complex proteins in cell membranes. Mol. Cell. Biochem. 81: 19-28, 1988.
    • (1988) Mol. Cell. Biochem. , vol.81 , pp. 19-28
    • Sobolev, A.S.1    Kazarov, A.R.2    Rosenkranz, A.A.3
  • 205
    • 0026776234 scopus 로고
    • Association of the beta isoform of protein kinase C with vimentin filaments
    • SPUDICH, A., T. MEYER, AND L. STRYER. Association of the beta isoform of protein kinase C with vimentin filaments. Cell. Motil. Cytoskeleton 22: 250-256, 1992.
    • (1992) Cell. Motil. Cytoskeleton , vol.22 , pp. 250-256
    • Spudich, A.1    Meyer, T.2    Stryer, L.3
  • 206
    • 0026713281 scopus 로고
    • Mapping the binding site on ankyrin for the voltage-dependent sodium channel from brain
    • SRINIVASAN, Y., M. LEWALLEN, AND K. J. ANGELIDES. Mapping the binding site on ankyrin for the voltage-dependent sodium channel from brain. J. Biol. Chem. 267: 7483-7489, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7483-7489
    • Srinivasan, Y.1    Lewallen, M.2    Angelides, K.J.3
  • 207
    • 0029970290 scopus 로고    scopus 로고
    • Phospholipase D regulation by a physical interaction with the actin-binding protein gelsolin
    • STEED, P. M., S. NAGAR, AND L. P. WENNOGLE. Phospholipase D regulation by a physical interaction with the actin-binding protein gelsolin. Biochemistry 35: 5229-5237, 1996.
    • (1996) Biochemistry , vol.35 , pp. 5229-5237
    • Steed, P.M.1    Nagar, S.2    Wennogle, L.P.3
  • 208
    • 0028503567 scopus 로고
    • The machinery of cell crawling
    • STOSSEL, T. P. The machinery of cell crawling. Sci. Am. 271: 54-55, 58-63, 1994.
    • (1994) Sci. Am. , vol.271 , pp. 54-55
    • Stossel, T.P.1
  • 209
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • SYMONS, M., J. M. DERRY, B. KARLAK, S. JIANG, V. LEMAHIEU, F. MCCORMICK, U. FRANCKE, AND A. ABO. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84: 723-734, 1996.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    Mccormick, F.6    Francke, U.7    Abo, A.8
  • 211
    • 0001115976 scopus 로고    scopus 로고
    • Counterion induced bundle formation of rodlike polyelectrolytes
    • TANG, J., S. WONG, P. TRAN, AND P. JANMEY. Counterion induced bundle formation of rodlike polyelectrolytes. Ber. Bunsen-Ges. Phys. Chem. 100: 796-806, 1996.
    • (1996) Ber. Bunsen-Ges. Phys. Chem. , vol.100 , pp. 796-806
    • Tang, J.1    Wong, S.2    Tran, P.3    Janmey, P.4
  • 212
    • 0030012323 scopus 로고    scopus 로고
    • The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation
    • TANG, J. X., AND P. A. JANMEY. The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation. J. Biol. Chem. 271: 8556-8563, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8556-8563
    • Tang, J.X.1    Janmey, P.A.2
  • 213
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • TAPON, N., AND A. HALL. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 9: 86-92, 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 214
    • 0029062869 scopus 로고
    • Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: A computer analysis
    • TEMPEL, M., W. H. GOLDMANN, G. ISENBERG, AND E. SACKMANN. Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: a computer analysis. Biophys. J. 69: 228-241, 1995.
    • (1995) Biophys. J. , vol.69 , pp. 228-241
    • Tempel, M.1    Goldmann, W.H.2    Isenberg, G.3    Sackmann, E.4
  • 215
    • 0028888558 scopus 로고
    • Persistent enhancement of sustained calcium-dependent glutamate release by phorbol esters: Role of calmodulin-independent serine/threonine phosphorylation and actin disassembly
    • TERRIAN, D. M., AND D. K. WAYS. Persistent enhancement of sustained calcium-dependent glutamate release by phorbol esters: role of calmodulin-independent serine/threonine phosphorylation and actin disassembly. J. Neurochem. 64: 181-190, 1995.
    • (1995) J. Neurochem. , vol.64 , pp. 181-190
    • Terrian, D.M.1    Ways, D.K.2
  • 216
    • 0029887723 scopus 로고    scopus 로고
    • Actin microfilament disrupters enhance K(ATP) channel opening in patches from guinea-pig cardiomyocytes
    • (Lond.)
    • TERZIC, A., AND Y. KURACHI. Actin microfilament disrupters enhance K(ATP) channel opening in patches from guinea-pig cardiomyocytes. J. Physiol. (Lond.) 492: 395-404, 1996.
    • (1996) J. Physiol. , vol.492 , pp. 395-404
    • Terzic, A.1    Kurachi, Y.2
  • 217
    • 0030576991 scopus 로고    scopus 로고
    • Activation of plasma membrane voltage-dependent calcium-permeable channels by disruption of microtubules in carrot cells
    • THION, L., C. MAZARS, P. THULEAU, A. GRAZIANA, M. ROSSIGNOL, M. MOREAU, AND R. RANJEVA. Activation of plasma membrane voltage-dependent calcium-permeable channels by disruption of microtubules in carrot cells. FEBS Lett. 393: 13-18, 1996.
    • (1996) FEBS Lett. , vol.393 , pp. 13-18
    • Thion, L.1    Mazars, C.2    Thuleau, P.3    Graziana, A.4    Rossignol, M.5    Moreau, M.6    Ranjeva, R.7
  • 218
    • 0028876287 scopus 로고
    • Src homologous and collagen (Shc) protein binds to F-actin and translocates to the cytoskeleton upon nerve growth factor stimulation in PC12 cells
    • THOMAS, D., S. D. PATTERSON, AND R. A. BRADSHAW. Src homologous and collagen (Shc) protein binds to F-actin and translocates to the cytoskeleton upon nerve growth factor stimulation in PC12 cells. J. Biol. Chem. 270: 28924-28931, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28924-28931
    • Thomas, D.1    Patterson, S.D.2    Bradshaw, R.A.3
  • 219
    • 0030291756 scopus 로고    scopus 로고
    • Control of cellular morphology by mechanical factors
    • THOUMINE, O. Control of cellular morphology by mechanical factors. J. Physique 6: 1555-1566, 1996.
    • (1996) J. Physique , vol.6 , pp. 1555-1566
    • Thoumine, O.1
  • 220
    • 0022599195 scopus 로고
    • Relation of actin fibrils to energy metabolism of endothelial cells
    • TILLMANN, U., AND H. J. BEREITER. Relation of actin fibrils to energy metabolism of endothelial cells. Cell Tissue Res. 243: 579-585, 1986.
    • (1986) Cell Tissue Res. , vol.243 , pp. 579-585
    • Tillmann, U.1    Bereiter, H.J.2
  • 221
    • 0027268213 scopus 로고
    • Association of the low molecular weight GTP-binding protein rap2B with the cytoskeleton during platelet aggregation
    • TORTI, M., G. RAMASCHI, F. SINIGAGLIA, E. G. LAPETINA, AND C. BALDUINI. Association of the low molecular weight GTP-binding protein rap2B with the cytoskeleton during platelet aggregation. Proc. Natl. Acad. Sci. USA 90: 7553-7557, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7553-7557
    • Torti, M.1    Ramaschi, G.2    Sinigaglia, F.3    Lapetina, E.G.4    Balduini, C.5
  • 222
    • 0029460729 scopus 로고
    • Intermediate filaments and gene regulation
    • TRAUB, P. Intermediate filaments and gene regulation. Physiol. Chem. Phys. Med. NMR 27: 377-400, 1995.
    • (1995) Physiol. Chem. Phys. Med. NMR , vol.27 , pp. 377-400
    • Traub, P.1
  • 223
    • 0028674554 scopus 로고
    • Intermediate filament proteins: Cytoskeletal elements with gene-regulatory function?
    • TRAUB, P., AND R. L. SHOEMAN. Intermediate filament proteins: cytoskeletal elements with gene-regulatory function? Int. Rev. Cytol. 154: 1-103, 1994.
    • (1994) Int. Rev. Cytol. , vol.154 , pp. 1-103
    • Traub, P.1    Shoeman, R.L.2
  • 224
    • 0027717728 scopus 로고
    • Microtubule antagonists activate programmed cell death (apoptosis) in cultured rat hepatocytes
    • TSUKIDATE, K., K. YAMAMOTO, J. W. SNYDER, AND J. L. FARBER. Microtubule antagonists activate programmed cell death (apoptosis) in cultured rat hepatocytes. Am. J. Pathol. 143: 918-925, 1993.
    • (1993) Am. J. Pathol. , vol.143 , pp. 918-925
    • Tsukidate, K.1    Yamamoto, K.2    Snyder, J.W.3    Farber, J.L.4
  • 225
    • 0031043523 scopus 로고    scopus 로고
    • ERM (ezrin/radixin/ moesin) family: From cytoskeleton to signal transduction
    • TSUKITA, S., S. YONEMURA, AND S. TSUKITA. ERM (ezrin/radixin/ moesin) family: from cytoskeleton to signal transduction. Curr. Opin. Cell Biol. 9: 70-75, 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 70-75
    • Tsukita, S.1    Yonemura, S.2    Tsukita, S.3
  • 226
    • 0028891155 scopus 로고
    • Cytoskeleton modulates gating of voltage-dependent sodium channel in heart
    • (Heart Circ. Physiol. 37)
    • UNDROVINAS, A. I., G. S. SHANDER, AND J. C. MAKIELSKI. Cytoskeleton modulates gating of voltage-dependent sodium channel in heart. Am. J. Physiol. 268 (Heart Circ. Physiol. 37): H203-H214, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Undrovinas, A.I.1    Shander, G.S.2    Makielski, J.C.3
  • 227
    • 0025363196 scopus 로고
    • Comparative two-dimensional gel analysis and microsequencing identifies gelsolin as one of the most prominent downregulated markers of transformed human fibroblasts and epithelial cells
    • VANDEKERCKHOVE, J., G. BAUW, K. VANCOMPERNOLLE, B. HONORE, AND J. CELIS. Comparative two-dimensional gel analysis and microsequencing identifies gelsolin as one of the most prominent downregulated markers of transformed human fibroblasts and epithelial cells. J. Cell Biol. 111: 95-102, 1990.
    • (1990) J. Cell Biol. , vol.111 , pp. 95-102
    • Vandekerckhove, J.1    Bauw, G.2    Vancompernolle, K.3    Honore, B.4    Celis, J.5
  • 228
    • 0029974446 scopus 로고    scopus 로고
    • F-actin disorganization in apoptotic cell death of cultured rat renal proximal tubular cells
    • (Renal Fluid Electrolyte Physiol. 39)
    • VAN DE WATER, B., M. KRUIDERING, AND J. F. NAGELKERKE. F-actin disorganization in apoptotic cell death of cultured rat renal proximal tubular cells. Am. J. Physiol. 270 (Renal Fluid Electrolyte Physiol. 39): F593-F603, 1996.
    • (1996) Am. J. Physiol. , vol.270
    • Van De Water, B.1    Kruidering, M.2    Nagelkerke, J.F.3
  • 230
    • 0031037505 scopus 로고    scopus 로고
    • A tension-based theory of morphogenesis and compact wiring in the central nervous system
    • VAN ESSEN, D. A tension-based theory of morphogenesis and compact wiring in the central nervous system. Nature 385: 313-318, 1997.
    • (1997) Nature , vol.385 , pp. 313-318
    • Van Essen, D.1
  • 231
    • 0028084328 scopus 로고
    • The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity
    • VAN ETTEN, R., P. K. JACKSON, D. BALTIMORE, M. C. SANDERS, P. T. MATSUDAIRA, AND P. A. JANMEY. The COOH terminus of the c-Abl tyrosine kinase contains distinct F-and G-actin binding domains with bundling activity. J. Cell Biol. 124: 325-340, 1994.
    • (1994) J. Cell Biol. , vol.124 , pp. 325-340
    • Van Etten, R.1    Jackson, P.K.2    Baltimore, D.3    Sanders, M.C.4    Matsudaira, P.T.5    Janmey, P.A.6
  • 232
    • 0023849518 scopus 로고
    • Cytochalasin stimulates phosphoinositide metabolism in murine B lymphocytes
    • VAN HAELST, C., AND T. L. ROTHSTEIN. Cytochalasin stimulates phosphoinositide metabolism in murine B lymphocytes. J. Immunol. 140: 1256-1258, 1988.
    • (1988) J. Immunol. , vol.140 , pp. 1256-1258
    • Van Haelst, C.1    Rothstein, T.L.2
  • 233
    • 0026482525 scopus 로고
    • Association of a receptor and G-protein-regulated phospholipase C with the cytoskeleton
    • VAZIRI, C., AND C. P. DOWNES. Association of a receptor and G-protein-regulated phospholipase C with the cytoskeleton. J. Biol. Chem. 267: 22973-22981, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22973-22981
    • Vaziri, C.1    Downes, C.P.2
  • 234
    • 0029058849 scopus 로고
    • Cytoskeletal disruption in A6 kidney cells: Impact on endo/exocytosis and NaCl transport regulation by antidiuretic hormone
    • VERREY, F., P. GROSCURTH, AND U. BOLLIGER. Cytoskeletal disruption in A6 kidney cells: impact on endo/exocytosis and NaCl transport regulation by antidiuretic hormone. J. Membr. Biol. 145: 193-204, 1995.
    • (1995) J. Membr. Biol. , vol.145 , pp. 193-204
    • Verrey, F.1    Groscurth, P.2    Bolliger, U.3
  • 235
    • 0023396034 scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate is selectively retained by platelet-fibrin clots formed by thrombin
    • VICKERS, J. D., R. KINLOUGH-RATHBONE, AND J. F. MUSTARD. Phosphatidylinositol 4,5-bisphosphate is selectively retained by platelet-fibrin clots formed by thrombin. Biochem. J. 245: 649-653, 1987.
    • (1987) Biochem. J. , vol.245 , pp. 649-653
    • Vickers, J.D.1    Kinlough-Rathbone, R.2    Mustard, J.F.3
  • 237
    • 0029975931 scopus 로고    scopus 로고
    • The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants
    • WANG, J., A. J. MORRIS, D. R. TOLAN, AND L. PAGLIARO. The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants. J. Biol. Chem. 271: 6861-6865, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6861-6865
    • Wang, J.1    Morris, A.J.2    Tolan, D.R.3    Pagliaro, L.4
  • 238
    • 0027172919 scopus 로고
    • Mechanotransduction across the cell surface and through the cytoskeleton
    • WANG, N., J. P. BUTLER, AND D. E. INGBER. Mechanotransduction across the cell surface and through the cytoskeleton. Science 260: 1124-1127, 1993.
    • (1993) Science , vol.260 , pp. 1124-1127
    • Wang, N.1    Butler, J.P.2    Ingber, D.E.3
  • 239
    • 0027992930 scopus 로고
    • Involvement of actin cytoskeleton in modulation of apical K channel activity in rat collecting duct
    • (Renal Fluid Electrolyte Physiol. 35)
    • WANG, W. H., A. CASSOLA, AND G. GIEBISCH. Involvement of actin cytoskeleton in modulation of apical K channel activity in rat collecting duct. Am. J. Physiol. 266 (Renal Fluid Electrolyte Physiol. 35): F592-F598, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Wang, W.H.1    Cassola, A.2    Giebisch, G.3
  • 240
    • 0026595895 scopus 로고
    • + exchange in Caco-2 cells by a mechanism which is dependent on F-actin
    • (published erratum appears in J. Biol. Chem. 268: 3016, 1993)
    • + exchange in Caco-2 cells by a mechanism which is dependent on F-actin (published erratum appears in J. Biol. Chem. 268: 3016, 1993) J. Biol. Chem. 267: 956-962, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 956-962
    • Watson, A.J.1    Levine, S.2    Donowitz, M.3    Montrose, M.H.4
  • 241
    • 0028900861 scopus 로고
    • Activation and translocation of c-Src to the cytoskeleton by both platelet-derived growth factor and epidermal growth factor
    • WEERNINK, P. A., AND G. RIJKSEN. Activation and translocation of c-Src to the cytoskeleton by both platelet-derived growth factor and epidermal growth factor. J. Biol. Chem. 270: 2264-2267, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2264-2267
    • Weernink, P.A.1    Rijksen, G.2
  • 242
    • 0029979775 scopus 로고    scopus 로고
    • Receptor-induced translocation of activated guanine-nucleotide-binding protein alpha i subunits to the cytoskeleton in myeloid differentiated human leukemia (HL-60) cells
    • WIELAND, T., D. MEYER ZU HERINGDORF, R. A. SCHULZE, S. KALDENBERG-STASCH, AND K. H. JAKOBS. Receptor-induced translocation of activated guanine-nucleotide-binding protein alpha i subunits to the cytoskeleton in myeloid differentiated human leukemia (HL-60) cells. Eur. J. Biochem. 239: 752-758, 1996.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 752-758
    • Wieland, T.1    Meyer Zu Heringdorf, D.2    Schulze, R.A.3    Kaldenberg-Stasch, S.4    Jakobs, K.H.5
  • 243
    • 0028048364 scopus 로고
    • Protein kinase C association with the retinal cytoskeleton and phosphorylation of vimentin
    • WILLIAMS, D. S., S. PARK, C. L. SCHLAMP, AND A. C. NEWTON. Protein kinase C association with the retinal cytoskeleton and phosphorylation of vimentin. Exp. Eye Res. 58: 747-759, 1994.
    • (1994) Exp. Eye Res. , vol.58 , pp. 747-759
    • Williams, D.S.1    Park, S.2    Schlamp, C.L.3    Newton, A.C.4
  • 244
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • YAMADA, K. M., AND B. GEIGER. Molecular interactions in cell adhesion complexes. Curr. Opin. Cell Biol. 9: 76-85, 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2
  • 245
    • 0030026237 scopus 로고    scopus 로고
    • Activation of SRC family kinases in human neutrophils. Evidence that p58C-FGR and p53/56LYN redistributed to a Triton X-100-insoluble cytoskeletal fraction also enriched in the caveolar protein caveolin, display an enhanced kinase activity
    • YAN, S. R., L. FUMAGALLI, AND G. BERTON. Activation of SRC family kinases in human neutrophils. Evidence that p58C-FGR and p53/56LYN redistributed to a Triton X-100-insoluble cytoskeletal fraction also enriched in the caveolar protein caveolin, display an enhanced kinase activity. FEBS Lett. 380: 198-203, 1996.
    • (1996) FEBS Lett. , vol.380 , pp. 198-203
    • Yan, S.R.1    Fumagalli, L.2    Berton, G.3
  • 246
    • 0025000290 scopus 로고
    • Identification of an actin-binding protein from Dictyostelium as elongation factor 1α
    • YANG, F., M. DEMMA, V. WARREN, S. DHARMAWARDHANE, AND J. CONDEELIS. Identification of an actin-binding protein from Dictyostelium as elongation factor 1α. Nature 347: 494-496, 1990.
    • (1990) Nature , vol.347 , pp. 494-496
    • Yang, F.1    Demma, M.2    Warren, V.3    Dharmawardhane, S.4    Condeelis, J.5
  • 247
    • 0028111491 scopus 로고
    • Regulation of phosphatidylinositol 4-kinase by the protein activator PIK-A49. Activation requires phosphorylation of PIK-A49
    • YANG, W., AND W. F. BOSS. Regulation of phosphatidylinositol 4-kinase by the protein activator PIK-A49. Activation requires phosphorylation of PIK-A49. J. Biol. Chem. 269: 3852-3857, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3852-3857
    • Yang, W.1    Boss, W.F.2
  • 248
    • 0026752622 scopus 로고
    • Identification of a polyphosphoinositide-binding sequence in an actin monomerbinding domain of gelsolin
    • YU, F. X., H. Q. SUN, P. A. JANMEY, AND H. L. YIN. Identification of a polyphosphoinositide-binding sequence in an actin monomerbinding domain of gelsolin. J. Biol. Chem. 267: 14616-14621, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14616-14621
    • Yu, F.X.1    Sun, H.Q.2    Janmey, P.A.3    Yin, H.L.4
  • 250
    • 0025000617 scopus 로고
    • Synergy between zinc and phorbol ester in translocation of protein kinase C to cytoskeleton
    • ZALEWSKI, P. D., I. J. FORBES, C. GIANNAKIS, P. A. COWLED, AND W. H. BETTS. Synergy between zinc and phorbol ester in translocation of protein kinase C to cytoskeleton. FEBS Lett. 273: 131-134, 1990.
    • (1990) FEBS Lett. , vol.273 , pp. 131-134
    • Zalewski, P.D.1    Forbes, I.J.2    Giannakis, C.3    Cowled, P.A.4    Betts, W.H.5
  • 251
    • 0030777109 scopus 로고    scopus 로고
    • Microfilament depletion and circumvention of multiple drug resistance by sphinxolides
    • ZHANG, X., L. MINALE, A. ZAMPELLA, AND C. D. SMITH. Microfilament depletion and circumvention of multiple drug resistance by sphinxolides. Cancer Res. 57: 3751-3758, 1997.
    • (1997) Cancer Res. , vol.57 , pp. 3751-3758
    • Zhang, X.1    Minale, L.2    Zampella, A.3    Smith, C.D.4
  • 252
    • 0030021649 scopus 로고    scopus 로고
    • Signal transduction and actin filament organization
    • ZIGMOND, S. H. Signal transduction and actin filament organization. Curr. Opin. Cell Biol. 8: 66-73, 1996.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 66-73
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.