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Volumn 18, Issue 15, 2004, Pages 1879-1890

Novel role of microtubules in thrombin-induced endothelial barrier dysfunction

Author keywords

G proteins; Pulmonary endothelium; Rho kinase; Tau; Thrombin

Indexed keywords

GUANOSINE TRIPHOSPHATASE; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; PACLITAXEL; RHO FACTOR; RHO KINASE; THROMBIN;

EID: 10044270843     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.04-2328com     Document Type: Article
Times cited : (179)

References (55)
  • 1
    • 0042343904 scopus 로고    scopus 로고
    • Vascular pharmacology of acute lung injury and acute respiratory distress syndrome
    • Groeneveld, A. B. (2002) Vascular pharmacology of acute lung injury and acute respiratory distress syndrome. Vascul. Pharmacol. 39, 247-256
    • (2002) Vascul. Pharmacol. , vol.39 , pp. 247-256
    • Groeneveld, A.B.1
  • 2
    • 0030477840 scopus 로고    scopus 로고
    • Of increased endothelial permeability
    • Lum, H., and Malik, A. B. (1996) of increased endothelial permeability. Can. J. Physiol. Pharmacol. 74, 787-800
    • (1996) Can. J. Physiol. Pharmacol. , vol.74 , pp. 787-800
    • Lum, H.1    Malik, A.B.2
  • 3
    • 0029803695 scopus 로고    scopus 로고
    • Regulation of thrombin-mediated endothelial cell contraction and permeability
    • Garcia, J. G., Verin, A. D., and Schaphorst, K. L. (1996) Regulation of thrombin-mediated endothelial cell contraction and permeability. Semin. Thromb. Hemost. 22, 309-315
    • (1996) Semin. Thromb. Hemost. , vol.22 , pp. 309-315
    • Garcia, J.G.1    Verin, A.D.2    Schaphorst, K.L.3
  • 4
    • 0034682993 scopus 로고    scopus 로고
    • Activation of RhoA by thrombin in endothelial hyperpermeability: Role of Rho kinase and protein tyrosine kinases
    • van Nieuw Amerongen, G. P., van Delft, S., Vermeer, M. A., Collard, J. G., and van Hinsbergh, V. W. (2000) Activation of RhoA by thrombin in endothelial hyperpermeability: role of Rho kinase and protein tyrosine kinases. Circ. Res. 87, 335-340
    • (2000) Circ. Res. , vol.87 , pp. 335-340
    • Nieuw Amerongen, G.P.1    Van Delft, S.2    Vermeer, M.A.3    Collard, J.G.4    Van Hinsbergh, V.W.5
  • 5
    • 0029012398 scopus 로고
    • Regulation of endothelial cell gap formation and barrier dysfunction: Role of myosin light chain phosphorylation
    • Garcia, J. G., Davis, H. W., and Patterson, C. E. (1995) Regulation of endothelial cell gap formation and barrier dysfunction: role of myosin light chain phosphorylation. J. Cell. Physiol. 163, 510-522
    • (1995) J. Cell. Physiol. , vol.163 , pp. 510-522
    • Garcia, J.G.1    Davis, H.W.2    Patterson, C.E.3
  • 6
    • 0033953888 scopus 로고    scopus 로고
    • Functional cooperation between the microtubule and actin cytoskeletons
    • Goode, B. L., Drubin, D. G., and Barnes, G. (2000) Functional cooperation between the microtubule and actin cytoskeletons. Curr. Opin. Cell Biol. 12, 63-71
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 63-71
    • Goode, B.L.1    Drubin, D.G.2    Barnes, G.3
  • 7
    • 0032966238 scopus 로고    scopus 로고
    • Positive feedback interactions between microtubule and actin dynamics during cell motility
    • Waterman-Storer, C. M., and Salmon, E. (1999) Positive feedback interactions between microtubule and actin dynamics during cell motility. Curr. Opin. Cell Biol. 11, 61-67
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 61-67
    • Waterman-Storer, C.M.1    Salmon, E.2
  • 8
    • 0034828134 scopus 로고    scopus 로고
    • Microtubule disassembly increases endothelial cell barrier dysfunction: Role of MLC phosphorylation
    • Verin, A. D., Birukova, A., Wang, P., Liu, F., Becker, P., Birukov, K., and Garcia, J. G. (2001) Microtubule disassembly increases endothelial cell barrier dysfunction: role of MLC phosphorylation. Am. J. Physiol. 281, L565-L574
    • (2001) Am. J. Physiol. , vol.281
    • Verin, A.D.1    Birukova, A.2    Wang, P.3    Liu, F.4    Becker, P.5    Birukov, K.6    Garcia, J.G.7
  • 10
    • 0037223457 scopus 로고    scopus 로고
    • Microfilaments and microtubules maintain endothelial integrity
    • Lee, T. Y., and Gotlieb, A. I. (2003) Microfilaments and microtubules maintain endothelial integrity. Microsc. Res. Tech. 60, 115-127
    • (2003) Microsc. Res. Tech. , vol.60 , pp. 115-127
    • Lee, T.Y.1    Gotlieb, A.I.2
  • 11
    • 0030266491 scopus 로고    scopus 로고
    • Involvement of microtubules in the control of adhesion-dependent signal transduction
    • Bershadsky, A., Chausovsky, A., Becker. E., Lyubimova, A., and Geiger, B. (1996) Involvement of microtubules in the control of adhesion-dependent signal transduction. Curr. Biol. 6, 1279-1289
    • (1996) Curr. Biol. , vol.6 , pp. 1279-1289
    • Bershadsky, A.1    Chausovsky, A.2    Becker, E.3    Lyubimova, A.4    Geiger, B.5
  • 12
    • 0030462929 scopus 로고    scopus 로고
    • Microtubule disruption induces the formation of actin stress fibers and focal adhesions in cultured cells: Possible involvement of the rho signal cascade
    • Enomoto, T. (1996) Microtubule disruption induces the formation of actin stress fibers and focal adhesions in cultured cells: possible involvement of the rho signal cascade. Cell Struct. Funct. 21, 317-326
    • (1996) Cell Struct. Funct. , vol.21 , pp. 317-326
    • Enomoto, T.1
  • 13
    • 0030928057 scopus 로고    scopus 로고
    • Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction
    • Zhang, Q., Magnusson, M. K., and Mosher, D. F. (1997) Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction. Mol. Biol. Cell 8, 1415-1425
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1415-1425
    • Zhang, Q.1    Magnusson, M.K.2    Mosher, D.F.3
  • 14
    • 0032583083 scopus 로고    scopus 로고
    • Transient and prolonged increase in endothelial permeability induced by histamine and thrombin: Role of protein kinases, calcium, and RhoA
    • van Nieuw Amerongen, G. P., Draijer, R., Vermeer, M. A., and van Hinsbergh, V. W. (1998) Transient and prolonged increase in endothelial permeability induced by histamine and thrombin: role of protein kinases, calcium, and RhoA. Circ. Res. 83, 1115-1123
    • (1998) Circ. Res. , vol.83 , pp. 1115-1123
    • Van Nieuw Amerongen, G.P.1    Draijer, R.2    Vermeer, M.A.3    Van Hinsbergh, V.W.4
  • 15
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu, T. K., Hung, D. T., Wheaton, V. I., and Coughlin, S. R. (1991) Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64, 1057-1068
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 16
    • 0031029553 scopus 로고    scopus 로고
    • Reconstitution of receptors and GTP-binding regulatory proteins (G proteins) in Sf9 cells. A direct evaluation of selectivity in receptor G protein coupling
    • Barr, A. J., Brass, L. F., and Manning, D. R. (1997) Reconstitution of receptors and GTP-binding regulatory proteins (G proteins) in Sf9 cells. A direct evaluation of selectivity in receptor G protein coupling. J. Biol. Chem. 272, 2223-2229
    • (1997) J. Biol. Chem. , vol.272 , pp. 2223-2229
    • Barr, A.J.1    Brass, L.F.2    Manning, D.R.3
  • 17
    • 0035854829 scopus 로고    scopus 로고
    • G alpha minigenes expressing C-terminal peptides serve as specific inhibitors of thrombin-mediated endothelial activation
    • Gilchrist, A., Vanhauwe, J. F., Li, A., Thomas, T. O., Voyno-Yasenetskaya, T., and Hamm, H. E. (2001) G alpha minigenes expressing C-terminal peptides serve as specific inhibitors of thrombin-mediated endothelial activation. J. Biol. Chem. 276, 25672-25679
    • (2001) J. Biol. Chem. , vol.276 , pp. 25672-25679
    • Gilchrist, A.1    Vanhauwe, J.F.2    Li, A.3    Thomas, T.O.4    Voyno-Yasenetskaya, T.5    Hamm, H.E.6
  • 18
    • 0030068979 scopus 로고    scopus 로고
    • Regulation of the thrombin receptor response in human endothelial cells
    • Storck, J., and Zimmermann, E. R. (1996) Regulation of the thrombin receptor response in human endothelial cells. Thromb. Res. 81, 121-131
    • (1996) Thromb. Res. , vol.81 , pp. 121-131
    • Storck, J.1    Zimmermann, E.R.2
  • 19
    • 0027934665 scopus 로고
    • Tubulin-G protein association stabilizes GTP binding and activates GTPase: Cytoskeletal participation in neuronal signal transduction
    • Roychowdhury, S., and Rasenick, M. M. (1994) Tubulin-G protein association stabilizes GTP binding and activates GTPase: cytoskeletal participation in neuronal signal transduction. Biochemistry 33, 9800-9805
    • (1994) Biochemistry , vol.33 , pp. 9800-9805
    • Roychowdhury, S.1    Rasenick, M.M.2
  • 20
    • 0028168836 scopus 로고
    • Chimeric G alpha s/G alpha i2 proteins define domains on G alpha s that interact with tubulin for beta-adrenergic activation of adenylyl cyclase
    • Popova, J. S., Johnson, G. L., and Rasenick, M. M. (1994) Chimeric G alpha s/G alpha i2 proteins define domains on G alpha s that interact with tubulin for beta-adrenergic activation of adenylyl cyclase. J. Biol. Chem. 269, 21748-21754
    • (1994) J. Biol. Chem. , vol.269 , pp. 21748-21754
    • Popova, J.S.1    Johnson, G.L.2    Rasenick, M.M.3
  • 22
  • 23
    • 0036460051 scopus 로고    scopus 로고
    • Rho/Rho-kinase mediated signaling in physiology and pathophysiology
    • Wettschureck, N., and Offermanns, S. (2002) Rho/Rho-kinase mediated signaling in physiology and pathophysiology. J. Mol. Med. 80, 629-638
    • (2002) J. Mol. Med. , vol.80 , pp. 629-638
    • Wettschureck, N.1    Offermanns, S.2
  • 24
    • 0034536529 scopus 로고    scopus 로고
    • Overexpression of wild-type RhoA produces growth arrest by disrupting actin cytoskeleton and microtubules
    • Song, Y., Wong, C., and Chang, D. D. (2000) Overexpression of wild-type RhoA produces growth arrest by disrupting actin cytoskeleton and microtubules. J. Cell. Biochem. 80, 229-240
    • (2000) J. Cell. Biochem. , vol.80 , pp. 229-240
    • Song, Y.1    Wong, C.2    Chang, D.D.3
  • 25
    • 0033601337 scopus 로고    scopus 로고
    • The neurite retraction induced by lysophosphatidic acid increases Alzheimer's disease-like Tau phosphorylation
    • Sayas, C. L., Moreno-Floves, M. T., Avila, J., and Wandosell, F. (1999) The neurite retraction induced by lysophosphatidic acid increases Alzheimer's disease-like Tau phosphorylation. J. Biol. Chem. 274, 37046-37052
    • (1999) J. Biol. Chem. , vol.274 , pp. 37046-37052
    • Sayas, C.L.1    Moreno-Floves, M.T.2    Avila, J.3    Wandosell, F.4
  • 28
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung, T., Chen, X. Q., Manser, E., and Lim, L. (1996) The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16, 5313-5327
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 29
    • 0028100892 scopus 로고
    • Mutant alpha subunits of G12 and G13 proteins induce neoplastic transformation of Rat-1 fibroblasts
    • Voyno-Yasenetskaya, T. A., Pace, A. M., and Bourne, H. R. (1994) Mutant alpha subunits of G12 and G13 proteins induce neoplastic transformation of Rat-1 fibroblasts. Oncogene 9, 2559-2565
    • (1994) Oncogene , vol.9 , pp. 2559-2565
    • Voyno-Yasenetskaya, T.A.1    Pace, A.M.2    Bourne, H.R.3
  • 30
    • 0034647493 scopus 로고    scopus 로고
    • Regulator of G protein signaling RGS3T is localized to the nucleus and induces apoptosis
    • Dulin, N. O., Pratt, P., Tiruppathi, C., Niu, J., Voyno-Yasenetskaya, T., and Dunn, M. J. (2000) Regulator of G protein signaling RGS3T is localized to the nucleus and induces apoptosis. J. Biol. Chem. 275, 21317-21323
    • (2000) J. Biol. Chem. , vol.275 , pp. 21317-21323
    • Dulin, N.O.1    Pratt, P.2    Tiruppathi, C.3    Niu, J.4    Voyno-Yasenetskaya, T.5    Dunn, M.J.6
  • 31
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., and Tuschl, T. (2001) Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature (London) 411, 494-498
    • (2001) Nature (London) , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 32
    • 0034667960 scopus 로고    scopus 로고
    • Introduction of C3 exoenzyme into cultured endothelium by lipofectamine
    • Borbiev, T., Nurmukhambetova, S., Liu, F., Verin, A. D., and Garcia, J. G. (2000) Introduction of C3 exoenzyme into cultured endothelium by lipofectamine. Anal. Biochem. 285, 260-264
    • (2000) Anal. Biochem. , vol.285 , pp. 260-264
    • Borbiev, T.1    Nurmukhambetova, S.2    Liu, F.3    Verin, A.D.4    Garcia, J.G.5
  • 33
    • 0033661641 scopus 로고    scopus 로고
    • Changes in cytoskeletal organization in polyoma middle T antigen-transformed fibroblasts: Involvement of protein phosphatase 2A and src tyrosine kinases
    • da Costa, S. R., Wang, Y., Vilalta, P. M., Schonthal, A. H., and Hamm-Alvarez, S. F. (2000) Changes in cytoskeletal organization in polyoma middle T antigen-transformed fibroblasts: involvement of protein phosphatase 2A and src tyrosine kinases. Cell Motil. Cytoskeleton 47, 253-268
    • (2000) Cell Motil. Cytoskeleton , vol.47 , pp. 253-268
    • Costa, S.R.1    Wang, Y.2    Vilalta, P.M.3    Schonthal, A.H.4    Hamm-Alvarez, S.F.5
  • 34
    • 2942718916 scopus 로고    scopus 로고
    • Protein kinase a attenuates endothelial cell barrier dysfunction induced by microtubule disassembly
    • Birukova, A. A., Liu, F., Garcia, J. G., and Verin, A. D. (2004) Protein kinase A attenuates endothelial cell barrier dysfunction induced by microtubule disassembly. Am. J. Physiol. 287, L86-L93
    • (2004) Am. J. Physiol. , vol.287
    • Birukova, A.A.1    Liu, F.2    Garcia, J.G.3    Verin, A.D.4
  • 35
    • 0033791649 scopus 로고    scopus 로고
    • Structural insights into microtubule function
    • Nogales, E. (2000) Structural insights into microtubule function. Annu. Rev. Biochem. 69, 277-302
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 277-302
    • Nogales, E.1
  • 36
    • 0023293040 scopus 로고
    • Microtubules containing acetylated alpha-tubulin in mammalian cells in culture
    • Piperno, G., LeDizet, M., and Chang, X.J. (1987) Microtubules containing acetylated alpha-tubulin in mammalian cells in culture. J. Cell Biol. 104, 289-302
    • (1987) J. Cell Biol. , vol.104 , pp. 289-302
    • Piperno, G.1    Ledizet, M.2    Chang, X.J.3
  • 37
    • 0842331443 scopus 로고    scopus 로고
    • Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling
    • Palazzo, A. F., Eng, C. H., Schlaepfer, D. D., Marcantonio, E. E., and Gundersen, G. G. (2004) Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling. Science 303, 836-839
    • (2004) Science , vol.303 , pp. 836-839
    • Palazzo, A.F.1    Eng, C.H.2    Schlaepfer, D.D.3    Marcantonio, E.E.4    Gundersen, G.G.5
  • 38
    • 0034907213 scopus 로고    scopus 로고
    • Dia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo, A. F., Cook, T. A., Alberts, A. S., and Gundersen, G. G. (2001) mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat. Cell Biol. 3, 723-729
    • (2001) Nat. Cell Biol. , vol.3 , pp. 723-729
    • Palazzo, A.F.1    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 39
    • 0035800854 scopus 로고    scopus 로고
    • Identification of potential mechanisms for regulation of p115 RhoGEF through analysis of endogenous and mutant forms of the exchange factor
    • Wells, C. D., Gutowski, S., Bollag, G., and Sternweis, P. C. (2001) Identification of potential mechanisms for regulation of p115 RhoGEF through analysis of endogenous and mutant forms of the exchange factor. J. Biol. Chem. 276, 28897-28905
    • (2001) J. Biol. Chem. , vol.276 , pp. 28897-28905
    • Wells, C.D.1    Gutowski, S.2    Bollag, G.3    Sternweis, P.C.4
  • 40
    • 0038746767 scopus 로고    scopus 로고
    • The role of the microtubules in tumor necrosis factor-alpha-induced endothelial cell permeability
    • Petrache, I., Birukova, A., Ramirez, S. I., Garcia, J. G., and Verin, A. D. (2003) The role of the microtubules in tumor necrosis factor-alpha-induced endothelial cell permeability. Am. J. Respir. Cell Mol.. Biol. 28, 574-581
    • (2003) Am. J. Respir. Cell Mol.. Biol. , vol.28 , pp. 574-581
    • Petrache, I.1    Birukova, A.2    Ramirez, S.I.3    Garcia, J.G.4    Verin, A.D.5
  • 41
    • 0032723693 scopus 로고    scopus 로고
    • Differential cytoskeletal changes during growth cone collapse in response to hSema III and thrombin
    • Fritsche, J., Reber, B. F., Schindelholz, B., and Bandtlow, C. E. (1999) Differential cytoskeletal changes during growth cone collapse in response to hSema III and thrombin. Mol. Cell. Neurosci. 14, 398-418
    • (1999) Mol. Cell. Neurosci. , vol.14 , pp. 398-418
    • Fritsche, J.1    Reber, B.F.2    Schindelholz, B.3    Bandtlow, C.E.4
  • 42
    • 0035901615 scopus 로고    scopus 로고
    • A lineage-restricted and divergent beta-tubulin isoform is essential for the biogenesis, structure and function of blood platelets
    • Schwer, H. D., Lecine, P., Tiwari, S., Italiano, J. E., Jr., Hartwig, J. H., and Shivdasani, R. A. (2001) A lineage-restricted and divergent beta-tubulin isoform is essential for the biogenesis, structure and function of blood platelets. Curr. Biol. 11, 579-586
    • (2001) Curr. Biol. , vol.11 , pp. 579-586
    • Schwer, H.D.1    Lecine, P.2    Tiwari, S.3    Italiano Jr., J.E.4    Hartwig, J.H.5    Shivdasani, R.A.6
  • 43
    • 0242412383 scopus 로고    scopus 로고
    • The immunopharmacology of paclitaxel (Taxol), docetaxel (Taxotere), and related agents
    • Fitzpatrick, F. A., and Wheeler, R. (2003) The immunopharmacology of paclitaxel (Taxol), docetaxel (Taxotere), and related agents. Int. Immunopharmacol. 3, 1699-1714
    • (2003) Int. Immunopharmacol. , vol.3 , pp. 1699-1714
    • Fitzpatrick, F.A.1    Wheeler, R.2
  • 45
    • 0030926125 scopus 로고    scopus 로고
    • The thrombin receptor in adrenal medullary microvascular endothelial cells is negatively coupled to adenylyl cyclase through a Gi protein
    • Manolopoulos, V. G., Fenton, J. W., II, and Lelkes, P. I. (1997) The thrombin receptor in adrenal medullary microvascular endothelial cells is negatively coupled to adenylyl cyclase through a Gi protein. Biochim. Biophys. Acta 1356, 321-332
    • (1997) Biochim. Biophys. Acta , vol.1356 , pp. 321-332
    • Manolopoulos, V.G.1    Fenton II, J.W.2    Lelkes, P.I.3
  • 46
    • 0038414642 scopus 로고    scopus 로고
    • Heterotrimeric G-proteins associate with microtubules during differentiation in PC12 pheochromocytoma cells
    • Sarma, T., Voyno-Yasenetskaya, T., Hope, T. J., and Rasenick, M. M. (2003) Heterotrimeric G-proteins associate with microtubules during differentiation in PC12 pheochromocytoma cells. FASEB J. 17, 848-859
    • (2003) FASEB J. , vol.17 , pp. 848-859
    • Sarma, T.1    Voyno-Yasenetskaya, T.2    Hope, T.J.3    Rasenick, M.M.4
  • 47
    • 0030589578 scopus 로고    scopus 로고
    • Tau-like proteins associated with centrosomes in cultured cells
    • Cross, D., Tapia, L., Garrido, J., and Maccioni, R. B. (1996) Tau-like proteins associated with centrosomes in cultured cells. Exp. Cell Res. 229, 378-387
    • (1996) Exp. Cell Res. , vol.229 , pp. 378-387
    • Cross, D.1    Tapia, L.2    Garrido, J.3    Maccioni, R.B.4
  • 48
    • 18144445001 scopus 로고    scopus 로고
    • Microtubule-associated protein tau in human fibroblasts with the Swedish Alzheimer mutation
    • Ingelson, M., Vanmechelen, E., and Lannfelt, L. (1996) Microtubule-associated protein tau in human fibroblasts with the Swedish Alzheimer mutation. Neurosci. Lett. 220, 9-12
    • (1996) Neurosci. Lett. , vol.220 , pp. 9-12
    • Ingelson, M.1    Vanmechelen, E.2    Lannfelt, L.3
  • 49
    • 0028220180 scopus 로고
    • Comparison of the phosphorylation of microtubuleassociated protein tau by nonproline dependent protein kinases
    • Singh, T. J., Grundke-Iqbal, I., McDonald, B., and Iqbal, K. (1994) Comparison of the phosphorylation of microtubuleassociated protein tau by nonproline dependent protein kinases. Mol. Cell. Biochem. 131, 181-189
    • (1994) Mol. Cell. Biochem. , vol.131 , pp. 181-189
    • Singh, T.J.1    Grundke-Iqbal, I.2    McDonald, B.3    Iqbal, K.4
  • 50
    • 0033562166 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II in tau phosphorylation
    • 2+/calmodulin-dependent protein kinase II in tau phosphorylation. Arch. Biochem. Biophys. 365, 268-278
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 268-278
    • Gupta, R.P.1    Abou-Donia, M.B.2
  • 51
    • 0141733132 scopus 로고    scopus 로고
    • Rapid tau aggregation and delayed hippocampal neuronal death induced by persistent thrombin signaling
    • Suo, Z., Wu, M., Citron, B. A., Palazzo, R. E., and Festoff, B. W. (2003) Rapid tau aggregation and delayed hippocampal neuronal death induced by persistent thrombin signaling. J. Biol. Chem. 278, 37681-37689
    • (2003) J. Biol. Chem. , vol.278 , pp. 37681-37689
    • Suo, Z.1    Wu, M.2    Citron, B.A.3    Palazzo, R.E.4    Festoff, B.W.5
  • 52
    • 0028237079 scopus 로고
    • Proteolydc degradation of microtubule associated protein tau by thrombin
    • Olesen, O. F. (1994) Proteolydc degradation of microtubule associated protein tau by thrombin. Biochem. Biophys. Res. Commun. 201, 716-721
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 716-721
    • Olesen, O.F.1
  • 53
    • 0035895915 scopus 로고    scopus 로고
    • Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules
    • van Horck, F. P., Ahmadian, M. R., Haeusler, L. C., Moolenaar, W. H., and Kranenburg, O. (2001) Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules. J. Biol. Chem. 276, 4948-4956
    • (2001) J. Biol. Chem. , vol.276 , pp. 4948-4956
    • Van Horck, F.P.1    Ahmadian, M.R.2    Haeusler, L.C.3    Moolenaar, W.H.4    Kranenburg, O.5
  • 54
    • 0033593337 scopus 로고    scopus 로고
    • The Dbl-related protein, Lfc, localizes to microtubules and mediates the activation of Rac signaling pathways in cells
    • Glaven, J. A., Whitehead, I., Bagrodia, S., Kay, R., and Cerione, R. A. (1999) The Dbl-related protein, Lfc, localizes to microtubules and mediates the activation of Rac signaling pathways in cells. J. Biol. Chem. 274, 2279-2285
    • (1999) J. Biol. Chem. , vol.274 , pp. 2279-2285
    • Glaven, J.A.1    Whitehead, I.2    Bagrodia, S.3    Kay, R.4    Cerione, R.A.5
  • 55
    • 0036228955 scopus 로고    scopus 로고
    • Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton
    • Krendel, M., Zenke, F. T., and Bokoch, G. M. (2002) Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton. Nat. Cell Biol. 4, 294-301
    • (2002) Nat. Cell Biol. , vol.4 , pp. 294-301
    • Krendel, M.1    Zenke, F.T.2    Bokoch, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.