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Volumn 14, Issue 6, 2009, Pages 2307-2334

Integrins and proximal signaling mechanisms in cardiovascular disease

Author keywords

Cardiac hypertrophy cardiomyocytes; Caveolin; Fibroblasts; Focal adhesion kinase; Integrin linked kinase; Integrins; Mitogen activated protein kinase; Review

Indexed keywords

INTEGRIN;

EID: 63849307598     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3381     Document Type: Article
Times cited : (75)

References (284)
  • 1
    • 36749083381 scopus 로고    scopus 로고
    • Integrin-dependent anchoring of a stem-cell niche
    • DOI 10.1038/ncb1660, PII NCB1660
    • Tanentzapf, G., D. Devenport, D. Godt & N. H. Brown: Integrin-dependent anchoring of a stem-cell niche. Nat Cell Biol, 9, 1413-1418 (2007). (Pubitemid 350201754)
    • (2007) Nature Cell Biology , vol.9 , Issue.12 , pp. 1413-1418
    • Tanentzapf, G.1    Devenport, D.2    Godt, D.3    Brown, N.H.4
  • 2
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • DOI 10.1016/S0092-8674(02)00971-6
    • Hynes, R. O.: Integrins: bidirectional, allosteric signaling machines. Cell, 110, 673-87 (2002. (Pubitemid 35283958)
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 3
    • 0031745571 scopus 로고    scopus 로고
    • Signal transduction and signal modulation by cell adhesion receptors: The role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins
    • Aplin, A. E., A. Howe, S. K. Alahari & R. L. Juliano: Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins. Pharmacol Rev, 50, 197-263 (1998). (Pubitemid 28304026)
    • (1998) Pharmacological Reviews , vol.50 , Issue.2 , pp. 197-263
    • Aplin, A.E.1    Howe, A.2    Alahari, S.K.3    Juliano, R.L.4
  • 4
    • 0035964805 scopus 로고    scopus 로고
    • Integrins in vascular development
    • Rupp, P. A. & C. D. Little: Integrins in vascular development. Circ Res, 89, 566-72 (2001). (Pubitemid 32924210)
    • (2001) Circulation Research , vol.89 , Issue.7 , pp. 566-572
    • Rupp, P.A.1    Little, C.D.2
  • 5
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F. G. & E. Ruoslahti: Integrin signaling. Science, 285, 1028-32 (1999).
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 7
    • 3242753503 scopus 로고    scopus 로고
    • Molecular and mechanical synergy: Cross-talk between integrins and growth factor receptors
    • DOI 10.1016/j.cardiores.2004.04.027, PII S0008636304001993
    • Ross, R. S.: Molecular and mechanical synergy: crosstalk between integrins and growth factor receptors. Cardiovasc Res, 63, 381-90 (2004). (Pubitemid 38970182)
    • (2004) Cardiovascular Research , vol.63 , Issue.3 , pp. 381-390
    • Ross, R.S.1
  • 8
    • 0038724539 scopus 로고    scopus 로고
    • Vascular integrins: Pleiotropic adhesion and signaling molecules in vascular homeostasis and angiogenesis
    • Ruegg, C. & A. Mariotti: Vascular integrins: pleiotropic adhesion and signaling molecules in vascular homeostasis and angiogenesis. Cell Mol Life Sci, 60, 1135-57 (2003). (Pubitemid 36791917)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.6 , pp. 1135-1157
    • Ruegg, C.1    Mariotti, A.2
  • 9
    • 0032911020 scopus 로고    scopus 로고
    • Bidirectional signaling between the cytoskeleton and integrins
    • DOI 10.1016/S0955-0674(99)80037-4
    • Schoenwaelder, S. M. & K. Burridge: Bidirectional signaling between the cytoskeleton and integrins. Curr Opin Cell Biol, 11, 274-86 (1999). (Pubitemid 29164045)
    • (1999) Current Opinion in Cell Biology , vol.11 , Issue.2 , pp. 274-286
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 11
    • 0030760119 scopus 로고    scopus 로고
    • Role of integrins in cellular responses to mechanical stress and adhesion
    • DOI 10.1016/S0955-0674(97)80125-1
    • Shyy, J. Y. & S. Chien: Role of integrins in cellular responses to mechanical stress and adhesion. Curr Opin Cell Biol, 9, 707-13 (1997). (Pubitemid 27424928)
    • (1997) Current Opinion in Cell Biology , vol.9 , Issue.5 , pp. 707-713
    • Shyy, J.Y.-J.1    Chien, S.2
  • 13
    • 0033603352 scopus 로고    scopus 로고
    • Mechanotransduction in response to shear stress. Roles of receptor tyrosine kinases, integrins, and Shc
    • Chen, K. D., Y. S. Li, M. Kim, S. Li, S. Yuan, S. Chien & J. Y. Shyy: Mechanotransduction in response to shear stress. Roles of receptor tyrosine kinases, integrins, and Shc. J Biol Chem, 274, 18393-400 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 18393-18400
    • Chen, K.D.1    Li, Y.S.2    Kim, M.3    Li, S.4    Yuan, S.5    Chien, S.6    Shyy, J.Y.7
  • 14
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith, C. G., K. M. Yamada & M. P. Sheetz: The relationship between force and focal complex development. J Cell Biol, 159, 695-705 (2002).
    • (2002) J Cell Biol , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 16
    • 0034123657 scopus 로고    scopus 로고
    • Mechanical stress-induced cardiac hypertrophy: Mechanisms and signal transduction pathways
    • DOI 10.1016/S0008-6363(00)00076-6, PII S0008636300000766
    • Ruwhof, C. & A. van der Laarse: Mechanical stress-induced cardiac hypertrophy: mechanisms and signal transduction pathways. Cardiovasc Res, 47, 23-37 (2000). (Pubitemid 30408547)
    • (2000) Cardiovascular Research , vol.47 , Issue.1 , pp. 23-37
    • Ruwhof, C.1    Van Der Laarse, A.2
  • 17
    • 0031044132 scopus 로고    scopus 로고
    • Integrin signaling transduces shear stress-dependent vasodilation of coronary arterioles
    • Muller, J. M., W. M. Chilian & M. J. Davis: Integrin signaling transduces shear stress-dependent vasodilation of coronary arterioles. Circ Res, 80, 320-6 (1997). (Pubitemid 27093345)
    • (1997) Circulation Research , vol.80 , Issue.3 , pp. 320-326
    • Muller, J.M.1    Chilian, W.M.2    Davis, M.J.3
  • 18
    • 0034038922 scopus 로고    scopus 로고
    • Role of mechanical factors in modulating cardiac fibroblast function and extracellular matrix synthesis
    • DOI 10.1016/S0008-6363(00)00030-4, PII S0008636300000304
    • MacKenna, D., S. R. Summerour & F. J. Villarreal: Role of mechanical factors in modulating cardiac fibroblast function and extracellular matrix synthesis. Cardiovasc Res, 46, 257-63 (2000). (Pubitemid 30204597)
    • (2000) Cardiovascular Research , vol.46 , Issue.2 , pp. 257-263
    • MacKenna, D.1    Summerour, S.R.2    Villarreal, F.J.3
  • 20
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O.: Integrins: versatility, modulation, and signaling in cell adhesion. Cell, 69, 11-25 (1992).
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 21
    • 0036734093 scopus 로고    scopus 로고
    • A reevaluation of integrins as regulators of angiogenesis
    • DOI 10.1038/nm0902-918
    • Hynes, R. O.: A reevaluation of integrins as regulators of angiogenesis. Nat Med, 8, 918-21 (2002). (Pubitemid 35033683)
    • (2002) Nature Medicine , vol.8 , Issue.9 , pp. 918-921
    • Hynes, R.O.1
  • 23
    • 33845657693 scopus 로고    scopus 로고
    • Integrin activation in the heart: A link between electrical and contractile dysfunction?
    • DOI 10.1161/01.RES.0000252291.88540.ac, PII 0000301220061222000016
    • Valencik, M. L., D. Zhang, B. Punske, P. Hu, J. A. McDonald & S. E. Litwin: Integrin activation in the heart: a link between electrical and contractile dysfunction? Circ Res, 99, 1403-10 (2006). (Pubitemid 44949676)
    • (2006) Circulation Research , vol.99 , Issue.12 , pp. 1403-1410
    • Valencik, M.L.1    Zhang, D.2    Punske, B.3    Hu, P.4    McDonald, J.A.5    Litwin, S.E.6
  • 24
    • 0035018246 scopus 로고    scopus 로고
    • Cardiac expression of a gain-of-function alpha (5)-integrin results in perinatal lethality
    • Valencik, M. L. & J. A. McDonald: Cardiac expression of a gain-of-function alpha (5)-integrin results in perinatal lethality. Am J Physiol Heart Circ Physiol, 280, H361-7 (2001).
    • (2001) Am J Physiol Heart Circ Physiol , vol.280
    • Valencik, M.L.1    McDonald, J.A.2
  • 26
    • 0036695847 scopus 로고    scopus 로고
    • A lethal perinatal cardiac phenotype resulting from altered integrin function in cardiomyocytes
    • Valencik, M. L., R. S. Keller, J. C. Loftus & J. A. McDonald: A lethal perinatal cardiac phenotype resulting from altered integrin function in cardiomyocytes. J Card Fail, 8, 262-72 (2002).
    • (2002) J Card Fail , vol.8 , pp. 262-272
    • Valencik, M.L.1    Keller, R.S.2    Loftus, J.C.3    McDonald, J.A.4
  • 27
    • 0035083118 scopus 로고    scopus 로고
    • β1 integrin and organized actin filaments facilitate cardiomyocytes-specific RhoA-dependent activation of the skeletal α-actin promoter
    • DOI 10.1096/fj.00-026com
    • Wei, L., L. Wang, J. A. Carson, J. E. Agan, K. Imanaka-Yoshida & R. J. Schwartz: beta1 integrin and organized actin filaments facilitate cardiomyocyte-specific RhoA-dependent activation of the skeletal alpha-actin promoter. Faseb J, 15, 785-96 (2001). (Pubitemid 32245997)
    • (2001) FASEB Journal , vol.15 , Issue.3 , pp. 785-796
    • Wei, L.1    Wang, L.2    Carson, J.A.3    Agan, J.E.4    Imanaka-Yoshida, K.5    Schwartz, R.J.6
  • 28
    • 0037188927 scopus 로고    scopus 로고
    • GFP-FRNK disrupts focal adhesions and induces anoikis in neonatal rat ventricular myocytes
    • DOI 10.1161/01.RES.0000023201.41774.EA
    • Heidkamp, M. C., A. L. Bayer, J. A. Kalina, D. M. Eble & A. M. Samarel: GFP-FRNK disrupts focal adhesions and induces anoikis in neonatal rat ventricular myocytes. Circ Res, 90, 1282-9 (2002). (Pubitemid 34787410)
    • (2002) Circulation Research , vol.90 , Issue.12 , pp. 1282-1289
    • Heidkamp, M.C.1    Bayer, A.L.2    Kalina, J.A.3    Eble, D.M.4    Samarel, A.M.5
  • 29
    • 0036947050 scopus 로고    scopus 로고
    • The extracellular connections: The role of integrins in myocardial remodeling
    • DOI 10.1054/jcaf.2002.129263
    • Ross, R. S.: The extracellular connections: the role of integrins in myocardial remodeling. J Card Fail, 8, S326-31 (2002). (Pubitemid 36083079)
    • (2002) Journal of Cardiac Failure , vol.8 , Issue.6 SUPPL.
    • Ross, R.S.1
  • 30
    • 0035827723 scopus 로고    scopus 로고
    • Integrins and the myocardium
    • Ross, R. S. & T. K. Borg: Integrins and the myocardium. Circ Res, 88, 1112-9 (2001). (Pubitemid 34132510)
    • (2001) Circulation Research , vol.88 , Issue.11 , pp. 1112-1119
    • Ross, R.S.1    Borg, T.K.2
  • 31
    • 0033843791 scopus 로고    scopus 로고
    • Expression of alpha and beta integrins during terminal differentiation of cardiomyocytes
    • Maitra, N., I. L. Flink, J. J. Bahl & E. Morkin: Expression of alpha and beta integrins during terminal differentiation of cardiomyocytes. Cardiovasc Res, 47, 715-25 (2000).
    • (2000) Cardiovasc Res , vol.47 , pp. 715-725
    • Maitra, N.1    Flink, I.L.2    Bahl, J.J.3    Morkin, E.4
  • 36
    • 0032852665 scopus 로고    scopus 로고
    • Angiotensin II promotes integrin-mediated collagen gel contraction by adult rat cardiac fibroblasts
    • DOI 10.1536/jhj.40.461
    • Nunohiro, T., N. Ashizawa, K. Graf, W. A. Hsueh & K. Yano: Angiotensin II promotes integrin-mediated collagen gel contraction by adult rat cardiac fibroblasts. Jpn Heart J, 40, 461-9 (1999). (Pubitemid 29473838)
    • (1999) Japanese Heart Journal , vol.40 , Issue.4 , pp. 461-469
    • Nunohiro, T.1    Ashizawa, N.2    Graf, K.3    Hsueh, W.A.4    Yano, K.5
  • 38
    • 0029089080 scopus 로고
    • Collagen remodeling after myocardial infarction in the rat heart
    • Cleutjens, J. P., M. J. Verluyten, J. F. Smiths & M. J. Daemen: Collagen remodeling after myocardial infarction in the rat heart. Am J Pathol, 147, 325-38 (1995).
    • (1995) Am J Pathol , vol.147 , pp. 325-338
    • Cleutjens, J.P.1    Verluyten, M.J.2    Smiths, J.F.3    Daemen, M.J.4
  • 39
    • 0030657676 scopus 로고    scopus 로고
    • Extracellular matrix remodeling in heart failure: A role for de novo angiotensin II generation
    • Weber, K. T.: Extracellular matrix remodeling in heart failure: a role for de novo angiotensin II generation. Circulation, 96, 4065-82 (1997).
    • (1997) Circulation , vol.96 , pp. 4065-4082
    • Weber, K.T.1
  • 42
    • 0036211774 scopus 로고    scopus 로고
    • Differential integrin expression by cardiac fibroblasts from hypertensive and exercise-trained rat hearts
    • DOI 10.1016/S1054-8807(01)00104-1, PII S1054880701001041
    • Burgess, M. L., L. Terracio, T. Hirozane & T. K. Borg: Differential integrin expression by cardiac fibroblasts from hypertensive and exercise-trained rat hearts. Cardiovasc Pathol, 11, 78-87 (2002). (Pubitemid 34273662)
    • (2002) Cardiovascular Pathology , vol.11 , Issue.2 , pp. 78-87
    • Burgess, M.L.1    Terracio, L.2    Hirozane, T.3    Borg, T.K.4
  • 43
    • 0028011071 scopus 로고
    • Integrin-mediated collagen gel contraction by cardiac fibroblasts: Effects of angiotensin II
    • Burgess, M. L., W. E. Carver, L. Terracio, S. P. Wilson, M. A. Wilson & T. K. Borg: Integrin-mediated collagen gel contraction by cardiac fibroblasts. Effects of angiotensin II. Circ Res, 74, 291-8 (1994). (Pubitemid 24029161)
    • (1994) Circulation Research , vol.74 , Issue.2 , pp. 291-298
    • Burgess, M.L.1    Carver, W.E.2    Terracio, L.3    Wilson, S.P.4    Wilson, M.A.5    Borg, T.K.6
  • 45
    • 0033954573 scopus 로고    scopus 로고
    • Angiotensin II enhances integrin and α-actinin expression in adult rat cardiac fibroblasts
    • Kawano, H., R. J. Cody, K. Graf, S. Goetze, Y. Kawano, J. Schnee, R. E. Law & W. A. Hsueh: Angiotensin II enhances integrin and alpha-actinin expression in adult rat cardiac fibroblasts. Hypertension, 35, 273-9 (2000). (Pubitemid 30054185)
    • (2000) Hypertension , vol.35 , Issue.1 , pp. 273-279
    • Kawano, H.1    Cody, R.J.2    Graf, K.3    Goetze, S.4    Kawano, Y.5    Schnee, J.6    Law, R.E.7    Hsueh, W.A.8
  • 46
    • 4444281827 scopus 로고    scopus 로고
    • Regulation of integrin function through conformational complexity: Not simply a knee-jerk reaction?
    • DOI 10.1016/j.ceb.2004.07.003, PII S0955067404000985
    • Mould, A. P. & M. J. Humphries: Regulation of integrin function through conformational complexity: not simply a knee-jerk reaction? Curr Opin Cell Biol, 16, 544-51 (2004). (Pubitemid 39201239)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.5 , pp. 544-551
    • Mould, A.P.1    Humphries, M.J.2
  • 48
    • 16644368209 scopus 로고    scopus 로고
    • Integrin bidirectional signaling: A molecular view
    • Qin, J., O. Vinogradova & E. F. Plow: Integrin bidirectional signaling: a molecular view. PLoS Biol, 2, e169 (2004).
    • (2004) PLoS Biol , vol.2
    • Qin, J.1    Vinogradova, O.2    Plow, E.F.3
  • 49
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • DOI 10.1242/jcs.01014
    • Calderwood, D. A.: Integrin activation. J Cell Sci, 117, 657-66 (2004). (Pubitemid 38268081)
    • (2004) Journal of Cell Science , vol.117 , Issue.5 , pp. 657-666
    • Calderwood, D.A.1
  • 50
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-binding proteins
    • Liu, S., D. A. Calderwood & M. H. Ginsberg: Integrin cytoplasmic domain-binding proteins. J Cell Sci, 113 (Pt 20) 3563-71 (2000).
    • (2000) J Cell Sci , vol.113 , Issue.PART 20 , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2    Ginsberg, M.H.3
  • 51
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir, E. & B. Geiger: Molecular complexity and dynamics of cell-matrix adhesions. J Cell Sci, 114, 3583-90 (2001). (Pubitemid 33041040)
    • (2001) Journal of Cell Science , vol.114 , Issue.20 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 53
    • 0029072762 scopus 로고
    • Flow-mediated endothelial mechanotransduction
    • Davies, P. F.: Flow-mediated endothelial mechanotransduction. Physiol Rev, 75, 519-60 (1995).
    • (1995) Physiol Rev , vol.75 , pp. 519-560
    • Davies, P.F.1
  • 54
    • 0031601849 scopus 로고    scopus 로고
    • Effects of mechanical forces on signal transduction and gene expression in endothelial cells
    • Chien, S., S. Li & Y. J. Shyy: Effects of mechanical forces on signal transduction and gene expression in endothelial cells. Hypertension, 31, 162-9 (1998).
    • (1998) Hypertension , vol.31 , pp. 162-169
    • Chien, S.1    Li, S.2    Shyy, Y.J.3
  • 55
    • 0032589393 scopus 로고    scopus 로고
    • α5β1 Integrin controls cyclin D1 expression by sustaining mitogen- activated protein kinase activity in growth factor-treated cells
    • Roovers, K., G. Davey, X. Zhu, M. E. Bottazzi & R. K. Assoian: Alpha5beta1 integrin controls cyclin D1 expression by sustaining mitogen-activated protein kinase activity in growth factor-treated cells. Mol Biol Cell, 10, 3197-204 (1999). (Pubitemid 29489555)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.10 , pp. 3197-3204
    • Roovers, K.1    Davey, G.2    Zhu, X.3    Bottazzi, M.E.4    Assoian, R.K.5
  • 56
    • 0035897407 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1
    • Aplin, A. E., S. A. Stewart, R. K. Assoian & R. L. Juliano: Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1. J Cell Biol, 153, 273-82 (2001).
    • (2001) J Cell Biol , vol.153 , pp. 273-282
    • Aplin, A.E.1    Stewart, S.A.2    Assoian, R.K.3    Juliano, R.L.4
  • 58
    • 0035479910 scopus 로고    scopus 로고
    • Assembly and mechanosensory function of focal contacts
    • DOI 10.1016/S0955-0674(00)00255-6
    • Geiger, B. & A. Bershadsky: Assembly and mechanosensory function of focal contacts. Curr Opin Cell Biol, 13, 584-92 (2001). (Pubitemid 32817017)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.5 , pp. 584-592
    • Geiger, B.1    Bershadsky, A.2
  • 60
    • 24344442455 scopus 로고    scopus 로고
    • Focal adhesion kinase mediates MEF2 and c-Jun activation by stretch: Role in the activation of the cardiac hypertrophic genetic program
    • DOI 10.1016/j.cardiores.2005.05.011, PII S0008636305002531
    • Nadruz, W. Jr., M. A. Corat, T. M. Marin, G. A. Guimaraes Pereira & K. G. Franchini: Focal adhesion kinase mediates MEF2 and c-Jun activation by stretch: role in the activation of the cardiac hypertrophic genetic program. Cardiovasc Res, 68, 87-97 (2005). (Pubitemid 41253559)
    • (2005) Cardiovascular Research , vol.68 , Issue.1 , pp. 87-97
    • Nadruz Jr., W.1    Corat, M.A.F.2    Marin, T.M.3    Guimaraes Pereira, G.A.4    Franchini, K.G.5
  • 61
    • 0033378656 scopus 로고    scopus 로고
    • Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats
    • Li, F., Y. Zhang & C. Wu: Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats. J Cell Sci, 112 (Pt 24), 4589-99 (1999). (Pubitemid 30034808)
    • (1999) Journal of Cell Science , vol.112 , Issue.24 , pp. 4589-4599
    • Li, F.1    Zhang, Y.2    Wu, C.3
  • 62
    • 0141533033 scopus 로고    scopus 로고
    • ADAMs: Modulators of cell-cell and cell-matrix interactions
    • DOI 10.1016/j.ceb.2003.08.001
    • White, J. M.: ADAMs: modulators of cell-cell and cellmatrix interactions. Curr Opin Cell Biol, 15, 598-606 (2003). (Pubitemid 37176969)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.5 , pp. 598-606
    • White, J.M.1
  • 64
    • 0027722248 scopus 로고
    • Autocrine release of angiotensin II mediates stretch-induced hypertrophy of cardiac myocytes in vitro
    • DOI 10.1016/0092-8674(93)90541-W
    • Sadoshima, J., Y. Xu, H. S. Slayter & S. Izumo: Autocrine release of angiotensin II mediates stretch-induced hypertrophy of cardiac myocytes in vitro. Cell, 75, 977-84 (1993). (Pubitemid 24014554)
    • (1993) Cell , vol.75 , Issue.5 , pp. 977-984
    • Sadoshima, J.-I.1    Xu, Y.2    Slayter, H.S.3    Izumo, S.4
  • 66
    • 0141927452 scopus 로고    scopus 로고
    • A newly developed angiotensin II type 1 receptor antagonist, CS866, promotes regression of cardiac hypertrophy by reducing integrin β1 expression
    • DOI 10.1291/hypres.26.737
    • Jia, N., H. Okamoto, T. Shimizu, S. Chiba, Y. Matsui, T. Sugawara, M. Akino & A. Kitabatake: A newly developed angiotensin II type 1 receptor antagonist, CS866, promotes regression of cardiac hypertrophy by reducing integrin beta1 expression. Hypertens Res, 26, 737-42 (2003). (Pubitemid 37258662)
    • (2003) Hypertension Research , vol.26 , Issue.9 , pp. 737-742
    • Jia, N.1    Okamoto, H.2    Shimizu, T.3    Chiba, S.4    Matsui, Y.5    Sugawara, T.6    Akino, M.7    Kitabatake, A.8
  • 68
    • 2942685631 scopus 로고    scopus 로고
    • Caveolae and caveolins in the cardiovascular system
    • DOI 10.1161/01.RES.0000129178.56294.17
    • Gratton, J. P., P. Bernatchez & W. C. Sessa: Caveolae and caveolins in the cardiovascular system. Circ Res, 94, 1408-17 (2004). (Pubitemid 38780313)
    • (2004) Circulation Research , vol.94 , Issue.11 , pp. 1408-1417
    • Gratton, J.-P.1    Bernatchez, P.2    Sessa, W.C.3
  • 69
    • 29244452619 scopus 로고    scopus 로고
    • Growth factor receptors, lipid rafts and caveolae: An evolving story
    • DOI 10.1016/j.bbamcr.2005.05.005, PII S0167488905000881, Lipid Refts: From Model Membranes to Cells
    • Pike, L. J.: Growth factor receptors, lipid rafts and caveolae: an evolving story. Biochim Biophys Acta, 1746, 260-73 (2005). (Pubitemid 41818991)
    • (2005) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1746 , Issue.3 , pp. 260-273
    • Pike, L.J.1
  • 70
    • 24344485458 scopus 로고    scopus 로고
    • Na/K-ATPase tethers phospholipase C and IP3 receptor into a calcium-regulatory complex
    • DOI 10.1091/mbc.E05-04-0295
    • Yuan, Z., T. Cai, J. Tian, A. V. Ivanov, D. R. Giovannucci & Z. Xie: Na/K-ATPase tethers phospholipase C and IP3 receptor into a calcium-regulatory complex. Mol Biol Cell, 16, 4034-45 (2005). (Pubitemid 41262876)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.9 , pp. 4034-4045
    • Yuan, Z.1    Cai, T.2    Tian, J.3    Ivanov, A.V.4    Giovannucci, D.R.5    Xie, Z.6
  • 72
    • 33645241165 scopus 로고    scopus 로고
    • Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane
    • Nicolau, D. V. Jr., K. Burrage, R. G. Parton & J. F. Hancock: Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane. Mol Cell Biol, 26, 313-23 (2006).
    • (2006) Mol Cell Biol , vol.26 , pp. 313-323
    • Nicolau Jr., D.V.1    Burrage, K.2    Parton, R.G.3    Hancock, J.F.4
  • 73
    • 33646014808 scopus 로고    scopus 로고
    • Characterization of the liquid-ordered state by proton MAS NMR
    • Polozov, I. V. & K. Gawrisch: Characterization of the liquid-ordered state by proton MAS NMR. Biophys J, 90, 2051-61 (2006).
    • (2006) Biophys J , vol.90 , pp. 2051-2061
    • Polozov, I.V.1    Gawrisch, K.2
  • 74
    • 0035881755 scopus 로고    scopus 로고
    • 2 rafts
    • DOI 10.1093/emboj/20.16.4332
    • Caroni, P.: New EMBO members' review: actin cytoskeleton regulation through modulation of PI (4, 5) P (2)rafts. Embo J, 20, 4332-6 (2001). (Pubitemid 32772026)
    • (2001) EMBO Journal , vol.20 , Issue.16 , pp. 4332-4336
    • Caroni, P.1
  • 75
    • 0842331441 scopus 로고    scopus 로고
    • Integrins Regulate Rac Targeting by Internalization of Membrane Domains
    • DOI 10.1126/science.1092571
    • Del Pozo, M. A., N. B. Alderson, W. B. Kiosses, H. H. Chiang, R. G. Anderson & M. A. Schwartz: Integrins regulate Rac targeting by internalization of membrane domains. Science, 303, 839-42 (2004). (Pubitemid 38174662)
    • (2004) Science , vol.303 , Issue.5659 , pp. 839-842
    • Del Pozo, M.A.1    Alderson, N.B.2    Kiosses, W.B.3    Chiang, H.-H.4    Anderson, R.G.W.5    Schwartz, M.A.6
  • 76
    • 0347764491 scopus 로고    scopus 로고
    • Polarization of plasma membrane microviscosity during endothelial cell migration
    • DOI 10.1016/S1534-5807(03)00397-6, PII S1534580703003976
    • Vasanji, A., P. K. Ghosh, L. M. Graham, S. J. Eppell & P. L. Fox: Polarization of plasma membrane microviscosity during endothelial cell migration. Dev Cell, 6, 29-41 (2004). (Pubitemid 38089203)
    • (2004) Developmental Cell , vol.6 , Issue.1 , pp. 29-41
    • Vasanji, A.1    Ghosh, P.K.2    Graham, L.M.3    Eppell, S.J.4    Fox, P.L.5
  • 78
    • 0000855817 scopus 로고
    • Fine structure of blood capillaries
    • Palade, G.: Fine structure of blood capillaries. J Appl Phys, 24, 1424-1436 (1953).
    • (1953) J Appl Phys , vol.24 , pp. 1424-1436
    • Palade, G.1
  • 79
    • 0033945943 scopus 로고    scopus 로고
    • Caveolin proteins in signaling, oncogenic transformation and muscular dystrophy
    • Razani, B., A. Schlegel & M. P. Lisanti: Caveolin proteins in signaling, oncogenic transformation and muscular dystrophy. J Cell Sci, 113 (Pt 12), 2103-9 (2000). (Pubitemid 30426825)
    • (2000) Journal of Cell Science , vol.113 , Issue.12 , pp. 2103-2109
    • Razani, B.1    Schlegel, A.2    Lisanti, M.P.3
  • 81
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • DOI 10.1126/science.1069784
    • Pelkmans, L., D. Puntener & A. Helenius: Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science, 296, 535-9 (2002). (Pubitemid 34408673)
    • (2002) Science , vol.296 , Issue.5567 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 82
    • 0035963902 scopus 로고    scopus 로고
    • Caveolae and intracellular trafficking of cholesterol
    • DOI 10.1016/S0169-409X(01)00140-5, PII S0169409X01001405
    • Fielding, C. J. & P. E. Fielding: Caveolae and intracellular trafficking of cholesterol. Adv Drug Deliv Rev, 49, 251-64 (2001). (Pubitemid 32718687)
    • (2001) Advanced Drug Delivery Reviews , vol.49 , Issue.3 , pp. 251-264
    • Fielding, C.J.1    Fielding, P.E.2
  • 83
    • 0042191629 scopus 로고    scopus 로고
    • Caveolin-1 and caveolae act as regulators of mitogenic signaling in vascular smooth muscle cells
    • DOI 10.1161/01.ATV.0000089081.43743.F6
    • Thyberg, J.: Caveolin-1 and caveolae act as regulators of mitogenic signaling in vascular smooth muscle cells. Arterioscler Thromb Vasc Biol, 23, 1481-3 (2003). (Pubitemid 37108185)
    • (2003) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.23 , Issue.9 , pp. 1481-1483
    • Thyberg, J.1
  • 84
    • 0037088672 scopus 로고    scopus 로고
    • A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14. Recruitment of C-terminal Src kinase
    • DOI 10.1074/jbc.C100661200
    • Cao, H., W. E. Courchesne & C. C. Mastick: A phosphotyrosine- dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase. J Biol Chem, 277, 8771-4 (2002). (Pubitemid 34952941)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.11 , pp. 8771-8774
    • Cao, H.1    Courchesne, W.E.2    Mastick, C.C.3
  • 89
    • 0032483575 scopus 로고    scopus 로고
    • A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth
    • DOI 10.1016/S0092-8674(00)81604-9
    • Wary, K. K., A. Mariotti, C. Zurzolo & F. G. Giancotti: A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth. Cell, 94, 625-34 (1998). (Pubitemid 28427581)
    • (1998) Cell , vol.94 , Issue.5 , pp. 625-634
    • Wary, K.K.1    Mariotti, A.2    Zurzolo, C.3    Giancotti, F.G.4
  • 91
    • 0344507516 scopus 로고    scopus 로고
    • A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling
    • DOI 10.1083/jcb.144.6.1285
    • Wei, Y., X. Yang, Q. Liu, J. A. Wilkins & H. A. Chapman: A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling. J Cell Biol, 144, 1285-94 (1999). (Pubitemid 29157305)
    • (1999) Journal of Cell Biology , vol.144 , Issue.6 , pp. 1285-1294
    • Ying, W.1    Yang, X.2    Qiumei, L.3    Wilkins, J.A.4    Chapman, H.A.5
  • 93
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases, G(α) subunits, and H-Ras share a common membrane- anchored scaffolding protein, caveolin: Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases
    • DOI 10.1074/jbc.271.46.29182
    • Li, S., J. Couet & M. P. Lisanti: Src tyrosine kinases, Galpha subunits, and H-Ras share a common membraneanchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. J Biol Chem, 271, 29182-90 (1996). (Pubitemid 26382628)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.46 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 94
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin- scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins
    • DOI 10.1074/jbc.272.10.6525
    • Couet, J., S. Li, T. Okamoto, T. Ikezu & M. P. Lisanti: Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins. J Biol Chem, 272, 6525-33 (1997). (Pubitemid 27118133)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.10 , pp. 6525-6533
    • Couet, J.1    Li, S.2    Okamoto, T.3    Ikezu, T.4    Lisanti, M.P.5
  • 95
    • 0037178784 scopus 로고    scopus 로고
    • Exploring the neighborhood: Adhesion-coupled cell mechanosensors
    • DOI 10.1016/S0092-8674(02)00831-0
    • Geiger, B. & A. Bershadsky: Exploring the neighborhood: adhesion-coupled cell mechanosensors. Cell, 110, 139-42 (2002). (Pubitemid 34876542)
    • (2002) Cell , vol.110 , Issue.2 , pp. 139-142
    • Geiger, B.1    Bershadsky, A.2
  • 96
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism
    • Riveline, D., E. Zamir, N. Q. Balaban, U. S. Schwarz, T. Ishizaki, S. Narumiya, Z. Kam, B. Geiger & A. D. Bershadsky: Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism. J Cell Biol, 153, 1175-86 (2001).
    • (2001) J Cell Biol , vol.153 , pp. 1175-1186
    • Riveline, D.1    Zamir, E.2    Balaban, N.Q.3    Schwarz, U.S.4    Ishizaki, T.5    Narumiya, S.6    Kam, Z.7    Geiger, B.8    Bershadsky, A.D.9
  • 98
    • 0027196279 scopus 로고
    • Cytoskeletal role in the contractile dysfunction of hypertrophied myocardium
    • Tsutsui, H., K. Ishihara & G. t. Cooper: Cytoskeletal role in the contractile dysfunction of hypertrophied myocardium. Science, 260, 682-7 (1993). (Pubitemid 23167592)
    • (1993) Science , vol.260 , Issue.5108 , pp. 682-687
    • Tsutsui, H.1    Ishihara, K.2    Cooper IV, G.3
  • 99
    • 0036222784 scopus 로고    scopus 로고
    • Adhesion assembly, disassembly and turnover in migrating cells - Over and over and over again
    • DOI 10.1038/ncb0402-e97
    • Webb, D. J., J. T. Parsons & A. F. Horwitz: Adhesion assembly, disassembly and turnover in migrating cells - over and over and over again. Nat Cell Biol, 4, E97-100 (2002). (Pubitemid 34308850)
    • (2002) Nature Cell Biology , vol.4 , Issue.4
    • Webb, D.J.1    Parsons, J.T.2    Horwitz, A.F.3
  • 100
    • 0034611008 scopus 로고    scopus 로고
    • Integrin dynamics and matrix assembly: Tensin-dependent translocation of alpha (5)beta (1) integrins promotes early fibronectin fibrillogenesis
    • Pankov, R., E. Cukierman, B. Z. Katz, K. Matsumoto, D. C. Lin, S. Lin, C. Hahn & K. M. Yamada: Integrin dynamics and matrix assembly: tensin-dependent translocation of alpha (5)beta (1) integrins promotes early fibronectin fibrillogenesis. J Cell Biol, 148, 1075-90 (2000).
    • (2000) J Cell Biol , vol.148 , pp. 1075-1090
    • Pankov, R.1    Cukierman, E.2    Katz, B.Z.3    Matsumoto, K.4    Lin, D.C.5    Lin, S.6    Hahn, C.7    Yamada, K.M.8
  • 104
    • 34447134113 scopus 로고    scopus 로고
    • Cardiac valve interstitial cells secrete fibronectin and form fibrillar adhesions in response to injury
    • DOI 10.1016/j.carpath.2007.02.008, PII S1054880707000476
    • Fayet, C., M. P. Bendeck & A. I. Gotlieb: Cardiac valve interstitial cells secrete fibronectin and form fibrillar adhesions in response to injury. Cardiovasc Pathol, 16, 203-11 (2007). (Pubitemid 47048753)
    • (2007) Cardiovascular Pathology , vol.16 , Issue.4 , pp. 203-211
    • Fayet, C.1    Bendeck, M.P.2    Gotlieb, A.I.3
  • 106
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks, S. K., M. B. Calalb, M. C. Harper & S. K. Patel: Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc Natl Acad Sci U S A, 89, 8487-91 (1992).
    • (1992) Proc Natl Acad Sci U S a , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 109
    • 0031044781 scopus 로고    scopus 로고
    • Focal adhesion kinase: At the crossroads of signal transduction
    • Ilic, D., C. H. Damsky & T. Yamamoto: Focal adhesion kinase: at the crossroads of signal transduction. J Cell Sci, 110 (Pt 4), 401-7 (1997). (Pubitemid 27116721)
    • (1997) Journal of Cell Science , vol.110 , Issue.4 , pp. 401-407
    • Ilic, D.1    Damsky, C.H.2    Yamamoto, T.3
  • 110
    • 0033002997 scopus 로고    scopus 로고
    • Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2
    • Owen, J. D., P. J. Ruest, D. W. Fry & S. K. Hanks: Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2. Mol Cell Biol, 19, 4806-18 (1999). (Pubitemid 29289519)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.7 , pp. 4806-4818
    • Owen, J.D.1    Ruest, P.J.2    Fry, D.W.3    Hanks, S.K.4
  • 111
    • 0029741102 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation
    • Gilmore, A. P. & L. H. Romer: Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation. Mol Biol Cell, 7, 1209-24 (1996). (Pubitemid 26260738)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.8 , pp. 1209-1224
    • Gilmore, A.P.1    Romer, L.H.2
  • 112
    • 0029948080 scopus 로고    scopus 로고
    • Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn
    • Cary, L. A., J. F. Chang & J. L. Guan: Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn. J Cell Sci, 109 (Pt 7)1787-94 (1996). (Pubitemid 26248624)
    • (1996) Journal of Cell Science , vol.109 , Issue.7 , pp. 1787-1794
    • Cary, L.A.1    Chang, J.F.2    Guan, J.-L.3
  • 113
    • 0038433306 scopus 로고    scopus 로고
    • Identification of transcription factor KLF8 as a downstream target of focal adhesion kinase in its regulation of cyclin D1 and cell cycle progression
    • DOI 10.1016/S1097-2765(03)00179-5
    • Zhao, J., Z. C. Bian, K. Yee, B. P. Chen, S. Chien & J. L. Guan: Identification of transcription factor KLF8 as a downstream target of focal adhesion kinase in its regulation of cyclin D1 and cell cycle progression. Mol Cell, 11, 1503-15 (2003). (Pubitemid 36776537)
    • (2003) Molecular Cell , vol.11 , Issue.6 , pp. 1503-1515
    • Zhao, J.1    Bian, Z.C.2    Yee, K.3    Chen, B.P.C.4    Chien, S.5    Guan, J.-L.6
  • 115
    • 0029240425 scopus 로고
    • Mapping of the focal adhesion kinase (Fadk)gene to mouse chromosome 15 and human chromosome 8
    • Fiedorek, F. T., Jr. & E. S. Kay: Mapping of the focal adhesion kinase (Fadk)gene to mouse chromosome 15 and human chromosome 8. Mamm Genome, 6, 123-6 (1995).
    • (1995) Mamm Genome , vol.6 , pp. 123-126
    • Fiedorek Jr., F.T.1    Kay, E.S.2
  • 116
    • 0033533746 scopus 로고    scopus 로고
    • Increased dosage and amplification of the focal adhesion kinase gene in human cancer cells
    • DOI 10.1038/sj.onc.1202957
    • Agochiya, M., V. G. Brunton, D. W. Owens, E. K. Parkinson, C. Paraskeva, W. N. Keith & M. C. Frame: Increased dosage and amplification of the focal adhesion kinase gene in human cancer cells. Oncogene, 18, 5646-53 (1999). (Pubitemid 29497599)
    • (1999) Oncogene , vol.18 , Issue.41 , pp. 5646-5653
    • Agochiya, M.1    Brunton, V.G.2    Owens, D.W.3    Parkinson, E.K.4    Paraskeva, C.5    Keith, W.N.6    Frame, M.C.7
  • 117
    • 0035948579 scopus 로고    scopus 로고
    • Biochemical signals and biological responses elicited by the focal adhesion kinase
    • DOI 10.1016/S0167-4889(01)00123-9, PII S0167488901001239
    • Schaller, M. D.: Biochemical signals and biological responses elicited by the focal adhesion kinase. Biochim Biophys Acta, 1540, 1-21 (2001). (Pubitemid 32710044)
    • (2001) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1540 , Issue.1 , pp. 1-21
    • Schaller, M.D.1
  • 118
    • 0032479435 scopus 로고    scopus 로고
    • Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide
    • DOI 10.1074/jbc.273.27.17102
    • Gervais, F. G., N. A. Thornberry, S. C. Ruffolo, D. W. Nicholson & S. Roy: Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide. J Biol Chem, 273, 17102-8 (1998). (Pubitemid 28311745)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.27 , pp. 17102-17108
    • Gervais, F.G.1    Thornberry, N.A.2    Ruffolo, S.C.3    Nicholson, D.W.4    Roy, S.5
  • 119
    • 0042266791 scopus 로고    scopus 로고
    • Focal adhesion kinase is activated and mediates the early hypertrophic response to stretch in cardiac myocytes
    • DOI 10.1161/01.RES.0000081595.25297.1B
    • Torsoni, A. S., S. S. Constancio, W. Nadruz, Jr., S. K. Hanks & K. G. Franchini: Focal adhesion kinase is activated and mediates the early hypertrophic response to stretch in cardiac myocytes. Circ Res, 93, 140-7 (2003). (Pubitemid 36919701)
    • (2003) Circulation Research , vol.93 , Issue.2 , pp. 140-147
    • Torsoni, A.S.1    Constancio, S.S.2    Nadruz Jr., W.3    Hanks, S.K.4    Franchini, K.G.5
  • 121
    • 0035947577 scopus 로고    scopus 로고
    • Src family kinases are required for integrin-mediated but not for G protein-coupled receptor stimulation of focal adhesion kinase autophosphorylation at Tyr-397
    • Salazar, E. P. & E. Rozengurt: Src family kinases are required for integrin-mediated but not for G protein-coupled receptor stimulation of focal adhesion kinase autophosphorylation at Tyr-397. J Biol Chem, 276, 17788-95 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 17788-17795
    • Salazar, E.P.1    Rozengurt, E.2
  • 123
    • 0034705523 scopus 로고    scopus 로고
    • A role for focal adhesion kinase in phenylephrine-induced hypertrophy of rat ventricular cardiomyocytes
    • DOI 10.1074/jbc.M909099199
    • Taylor, J. M., J. D. Rovin & J. T. Parsons: A role for focal adhesion kinase in phenylephrine-induced hypertrophy of rat ventricular cardiomyocytes. J Biol Chem, 275, 19250-7 (2000). (Pubitemid 30422897)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 19250-19257
    • Taylor, J.M.1    Rovin, J.D.2    Parsons, J.T.3
  • 125
    • 33751335857 scopus 로고    scopus 로고
    • Force Sensing by Mechanical Extension of the Src Family Kinase Substrate p130Cas
    • DOI 10.1016/j.cell.2006.09.044, PII S009286740601405X
    • Sawada, Y., M. Tamada, B. J. Dubin-Thaler, O. Cherniavskaya, R. Sakai, S. Tanaka & M. P. Sheetz: Force sensing by mechanical extension of the Src family kinase substrate p130Cas. Cell, 127, 1015-26 (2006). (Pubitemid 44803062)
    • (2006) Cell , vol.127 , Issue.5 , pp. 1015-1026
    • Sawada, Y.1    Tamada, M.2    Dubin-Thaler, B.J.3    Cherniavskaya, O.4    Sakai, R.5    Tanaka, S.6    Sheetz, M.P.7
  • 127
    • 8644263977 scopus 로고    scopus 로고
    • Overexpression of focal adhesion kinase in vascular endothelial cells promotes angiogenesis in transgenic mice
    • DOI 10.1016/j.cardiores.2004.07.012, PII S0008636304003281
    • Peng, X., H. Ueda, H. Zhou, T. Stokol, T. L. Shen, A. Alcaraz, T. Nagy, J. D. Vassalli & J. L. Guan: Overexpression of focal adhesion kinase in vascular endothelial cells promotes angiogenesis in transgenic mice. Cardiovasc Res, 64, 421-30 (2004). (Pubitemid 39505421)
    • (2004) Cardiovascular Research , vol.64 , Issue.3 , pp. 421-430
    • Peng, X.1    Ueda, H.2    Zhou, H.3    Stokol, T.4    Shen, T.-L.5    Alcaraz, A.6    Nagy, T.7    Vassalli, J.-D.8    Guan, J.-L.9
  • 128
    • 29944436856 scopus 로고    scopus 로고
    • Endothelial FAK is essential for vascular network stability, cell survival, and lamellipodial formation
    • DOI 10.1083/jcb.200506184
    • Braren, R., H. Hu, Y. H. Kim, H. E. Beggs, L. F. Reichardt & R. Wang: Endothelial FAK is essential for vascular network stability, cell survival, and lamellipodial formation. J Cell Biol, 172, 151-62 (2006). (Pubitemid 43042637)
    • (2006) Journal of Cell Biology , vol.172 , Issue.1 , pp. 151-162
    • Braren, R.1    Hu, H.2    Kim, Y.H.3    Beggs, H.E.4    Reichardt, L.F.5    Wang, R.6
  • 129
    • 22344434300 scopus 로고    scopus 로고
    • Conditional knockout of focal adhesion kinase in endothelial cells reveals its role in angiogenesis and vascular development in late embryogenesis
    • DOI 10.1083/jcb.200411155
    • Shen, T. L., A. Y. Park, A. Alcaraz, X. Peng, I. Jang, P. Koni, R. A. Flavell, H. Gu & J. L. Guan: Conditional knockout of focal adhesion kinase in endothelial cells reveals its role in angiogenesis and vascular development in late embryogenesis. J Cell Biol, 169, 941-52 (2005). (Pubitemid 41002870)
    • (2005) Journal of Cell Biology , vol.169 , Issue.6 , pp. 941-952
    • Shen, T.-L.1    Park, A.Y.-J.2    Alcaraz, A.3    Peng, X.4    Jang, I.5    Koni, P.6    Flavell, R.A.7    Gu, H.8    Guan, J.-L.9
  • 130
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK
    • Furuta, Y., D. Ilic, S. Kanazawa, N. Takeda, T. Yamamoto & S. Aizawa: Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. Oncogene, 11, 1989-95 (1995).
    • (1995) Oncogene , vol.11 , pp. 1989-1995
    • Furuta, Y.1    Ilic, D.2    Kanazawa, S.3    Takeda, N.4    Yamamoto, T.5    Aizawa, S.6
  • 132
    • 33748741079 scopus 로고    scopus 로고
    • Myocyte-restricted focal adhesion kinase deletion attenuates pressure overload-induced hypertrophy
    • DOI 10.1161/01.RES.0000240498.44752.d6, PII 0000301220060915000011
    • DiMichele, L. A., J. T. Doherty, M. Rojas, H. E. Beggs, L. F. Reichardt, C. P. Mack & J. M. Taylor: Myocyte-restricted focal adhesion kinase deletion attenuates pressure overload-induced hypertrophy. Circ Res, 99, 636-45 (2006). (Pubitemid 44401455)
    • (2006) Circulation Research , vol.99 , Issue.6 , pp. 636-645
    • DiMichele, L.A.1    Doherty, J.T.2    Rojas, M.3    Beggs, H.E.4    Reichardt, L.F.5    Mack, C.P.6    Taylor, J.M.7
  • 134
    • 0036306621 scopus 로고    scopus 로고
    • Evidence that the platelet integrin αIIbβ3 is regulated by the integrin-linked kinase, ILK, in a PI3-kinase dependent pathway
    • Pasquet, J. M., M. Noury & A. T. Nurden: Evidence that the platelet integrin alphaIIb beta3 is regulated by the integrin-linked kinase, ILK, in a PI3-kinase dependent pathway. Thromb Haemost, 88, 115-22 (2002). (Pubitemid 34752276)
    • (2002) Thrombosis and Haemostasis , vol.88 , Issue.1 , pp. 115-122
    • Pasquet, J.-M.1    Noury, M.2    Nurden, A.T.3
  • 135
    • 0008584962 scopus 로고    scopus 로고
    • Mapping of the gene encoding the integrin-linked kinase, ILK, to human chromosome 11p15.5-p15.4
    • DOI 10.1006/geno.1997.4719
    • Hannigan, G. E., J. Bayani, R. Weksberg, B. Beatty, A. Pandita, S. Dedhar & J. Squire: Mapping of the gene encoding the integrin-linked kinase, ILK, to human chromosome 11p15.5-p15.4. Genomics, 42, 177-9 (1997). (Pubitemid 27215142)
    • (1997) Genomics , vol.42 , Issue.1 , pp. 177-179
    • Hannigan, G.E.1    Bayani, J.2    Weksberg, R.3    Beatty, B.4    Pandita, A.5    Dedhar, S.6    Squire, J.7
  • 136
    • 0037012729 scopus 로고    scopus 로고
    • Promoter characterization and genomic organization of the gene encoding integrin-linked kinase 1
    • DOI 10.1016/S0167-4781(02)00247-6, PII S0167478102002476
    • Melchior, C., S. Kreis, B. Janji & N. Kieffer: Promoter characterization and genomic organization of the gene encoding integrin-linked kinase 1. Biochim Biophys Acta, 1575, 117-22 (2002). (Pubitemid 34521784)
    • (2002) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1575 , Issue.1-3 , pp. 117-122
    • Melchior, C.1    Kreis, S.2    Janji, B.3    Kieffer, N.4
  • 137
    • 0034698755 scopus 로고    scopus 로고
    • The roles of integrin-linked kinase in the regulation of myogenic differentiation
    • Huang, Y., J. Li, Y. Zhang & C. Wu: The roles of integrin-linked kinase in the regulation of myogenic differentiation. J Cell Biol, 150, 861-72 (2000).
    • (2000) J Cell Biol , vol.150 , pp. 861-872
    • Huang, Y.1    Li, J.2    Zhang, Y.3    Wu, C.4
  • 141
    • 0033020670 scopus 로고    scopus 로고
    • The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells
    • Tu, Y., F. Li, S. Goicoechea & C. Wu: The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells. Mol Cell Biol, 19, 2425-34 (1999). (Pubitemid 29098300)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.3 , pp. 2425-2434
    • Tu, Y.1    Li, F.2    Goicoechea, S.3    Wu, C.4
  • 142
    • 0035341207 scopus 로고    scopus 로고
    • Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1
    • DOI 10.1093/emboj/20.9.2160
    • Leung-Hagesteijn, C., A. Mahendra, I. Naruszewicz & G. E. Hannigan: Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1. Embo J, 20, 2160-70 (2001). (Pubitemid 32410586)
    • (2001) EMBO Journal , vol.20 , Issue.9 , pp. 2160-2170
    • Leung-Hagesteijn, C.1    Mahendra, A.2    Naruszewicz, I.3    Hannigan, G.E.4
  • 143
    • 0027933818 scopus 로고
    • A new LIM protein containing an autoepitope homologous to "senescent cell antigen"
    • Rearden, A.: A new LIM protein containing an autoepitope homologous to "senescent cell antigen". Biochem Biophys Res Commun, 201, 1124-31 (1994).
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 1124-1131
    • Rearden, A.1
  • 144
    • 0037064063 scopus 로고    scopus 로고
    • Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration
    • DOI 10.1074/jbc.M205576200
    • Zhang, Y., K. Chen, L. Guo & C. Wu: Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration. J Biol Chem, 277, 38328-38 (2002). (Pubitemid 35154687)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38328-38338
    • Zhang, Y.1    Chen, K.2    Guo, L.3    Wu, C.4
  • 145
    • 0032787837 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK): A regulator of integrin and growth-factor signalling
    • DOI 10.1016/S0962-8924(99)01612-8, PII S0962892499016128
    • Dedhar, S., B. Williams & G. Hannigan: Integrin-linked kinase (ILK): a regulator of integrin and growth-factor signalling. Trends Cell Biol, 9, 319-23 (1999). (Pubitemid 29339148)
    • (1999) Trends in Cell Biology , vol.9 , Issue.8 , pp. 319-323
    • Dedhar, S.1    Williams, B.2    Hannigan, G.3
  • 146
    • 25144434380 scopus 로고    scopus 로고
    • Assembly and Signaling of Adhesion Complexes
    • DOI 10.1016/S0070-2153(05)68007-6, PII S0070215305680076
    • Sepulveda, J. L., V. Gkretsi & C. Wu: Assembly and signaling of adhesion complexes. Curr Top Dev Biol, 68, 183-225 (2005). (Pubitemid 43588864)
    • (2005) Current Topics in Developmental Biology , vol.68 , pp. 183-225
    • Sepulveda, J.L.1    Gkretsi, V.2    Wu, C.3
  • 147
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • DOI 10.1016/S0960-9822(02)00810-2, PII S0960982202008102
    • Mackinnon, A. C., H. Qadota, K. R. Norman, D. G. Moerman & B. D. Williams: C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr Biol, 12, 787-97 (2002). (Pubitemid 34514364)
    • (2002) Current Biology , vol.12 , Issue.10 , pp. 787-797
    • Mackinnon A.Craig1    Qadota, H.2    Norman, K.R.3    Moerman, D.G.4    Williams, B.D.5
  • 148
    • 0345803932 scopus 로고    scopus 로고
    • PINCH-1 Is an Obligate Partner of Integrin-linked Kinase (ILK) Functioning in Cell Shape Modulation, Motility, and Survival
    • DOI 10.1074/jbc.M309122200
    • Fukuda, T., K. Chen, X. Shi & C. Wu: PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival. J Biol Chem, 278, 51324-33 (2003). (Pubitemid 38020371)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.51 , pp. 51324-51333
    • Fukuda, T.1    Chen, K.2    Shi, X.3    Wu, C.4
  • 149
    • 0037115611 scopus 로고    scopus 로고
    • Assembly fo the PINCH-IL-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
    • DOI 10.1242/jcs.00166
    • Zhang, Y., K. Chen, Y. Tu, A. Velyvis, Y. Yang, J. Qin & C. Wu: Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites. J Cell Sci, 115, 4777-86 (2002). (Pubitemid 36054631)
    • (2002) Journal of Cell Science , vol.115 , Issue.24 , pp. 4777-4786
    • Zhang, Y.1    Chen, K.2    Tu, Y.3    Velyvis, A.4    Yang, Y.5    Qin, J.6    Wu, C.7
  • 151
    • 0035969233 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) and its interactors: A new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes
    • Wu, C. & S. Dedhar: Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes. J Cell Biol, 155, 505-10 (2001). (Pubitemid 34289309)
    • (2001) Journal of Cell Biology , vol.155 , Issue.3 , pp. 505-510
    • Wu, C.1    Dedhar, S.2
  • 152
    • 2442702768 scopus 로고    scopus 로고
    • ILKAP regulates ILK signaling and inhibits anchorage-independent growth
    • DOI 10.1038/sj.onc.1207473
    • Kumar, A. S., I. Naruszewicz, P. Wang, C. Leung-Hagesteijn & G. E. Hannigan: ILKAP regulates ILK signaling and inhibits anchorage-independent growth. Oncogene, 23, 3454-61 (2004). (Pubitemid 38669835)
    • (2004) Oncogene , vol.23 , Issue.19 , pp. 3454-3461
    • Kumar, A.S.1    Naruszewicz, I.2    Wang, P.3    Leung-Hagesteijn, C.4    Hannigan, G.E.5
  • 153
    • 0035844886 scopus 로고    scopus 로고
    • Tumor suppressor PTEN inhibits nuclear accumulation of beta-catenin and T cell/lymphoid enhancer factor 1-mediated transcriptional activation
    • Persad, S., A. A. Troussard, T. R. McPhee, D. J. Mulholland & S. Dedhar: Tumor suppressor PTEN inhibits nuclear accumulation of beta-catenin and T cell/lymphoid enhancer factor 1-mediated transcriptional activation. J Cell Biol, 153, 1161-74 (2001).
    • (2001) J Cell Biol , vol.153 , pp. 1161-1174
    • Persad, S.1    Troussard, A.A.2    McPhee, T.R.3    Mulholland, D.J.4    Dedhar, S.5
  • 154
    • 0037666792 scopus 로고    scopus 로고
    • Conditional knock-out of integrin-linked kinase demonstrates an essential role in protein kinase B/Akt activation
    • DOI 10.1074/jbc.M303083200
    • Troussard, A. A., N. M. Mawji, C. Ong, A. Mui, R. St-Arnaud & S. Dedhar: Conditional knock-out of integrin-linked kinase demonstrates an essential role in protein kinase B/Akt activation. J Biol Chem, 278, 22374-8 (2003). (Pubitemid 36830287)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.25 , pp. 22374-22378
    • Troussard, A.A.1    Mawji, N.M.2    Ong, C.3    Mui, A.4    St.-Arnaud, R.5    Dedhar, S.6
  • 155
    • 0033599029 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates phosphorylation of serine 473 of protein kinase B by an indirect mechanism
    • Lynch, D. K., C. A. Ellis, P. A. Edwards & I. D. Hiles: Integrin-linked kinase regulates phosphorylation of serine 473 of protein kinase B by an indirect mechanism. Oncogene, 18, 8024-32 (1999). (Pubitemid 30050563)
    • (1999) Oncogene , vol.18 , Issue.56 , pp. 8024-8032
    • Lynch, D.K.1    Ellis, C.A.2    Edwards, P.A.3    Hiles, I.D.4
  • 156
    • 0037162291 scopus 로고    scopus 로고
    • Identification of a plasma membrane raft-associated PKB Ser473 kinase activity that is distinct from ILK and PDK1
    • DOI 10.1016/S0960-9822(02)00973-9, PII S0960982202009739
    • Hill, M. M., J. Feng & B. A. Hemmings: Identification of a plasma membrane Raft-associated PKB Ser473 kinase activity that is distinct from ILK and PDK1. Curr Biol, 12, 1251-5 (2002). (Pubitemid 34801175)
    • (2002) Current Biology , vol.12 , Issue.14 , pp. 1251-1255
    • Hill, M.M.1    Feng, J.2    Hemmings, B.A.3
  • 157
    • 0038323946 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates chondrocyte shape and proliferation
    • DOI 10.1038/sj.embor.embor801
    • Grashoff, C., A. Aszodi, T. Sakai, E. B. Hunziker & R. Fassler: Integrin-linked kinase regulates chondrocyte shape and proliferation. EMBO Rep, 4, 432-8 (2003). (Pubitemid 36622011)
    • (2003) EMBO Reports , vol.4 , Issue.4 , pp. 432-438
    • Grashoff, C.1    Aszodi, A.2    Sakai, T.3    Hunziker, E.B.4    Fassler, R.5
  • 158
    • 33748278519 scopus 로고    scopus 로고
    • Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure
    • DOI 10.1101/gad.1458906
    • White, D. E., P. Coutu, Y. F. Shi, J. C. Tardif, S. Nattel, R. St Arnaud, S. Dedhar & W. J. Muller: Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure. Genes Dev, 20, 2355-60 (2006). (Pubitemid 44320384)
    • (2006) Genes and Development , vol.20 , Issue.17 , pp. 2355-2360
    • White, D.E.1    Coutu, P.2    Shi, Y.-F.3    Tardif, J.-C.4    Nattel, S.5    St. Arnaud, R.6    Dedhar, S.7    Muller, W.J.8
  • 159
    • 34249660635 scopus 로고    scopus 로고
    • Integrin-linked kinase at the heart of cardiac contractility, repair, and disease
    • DOI 10.1161/01.RES.0000265233.40455.62, PII 0000301220070525000007
    • Hannigan, G. E., J. G. Coles & S. Dedhar: Integrin-linked kinase at the heart of cardiac contractility, repair, and disease. Circ Res, 100, 1408-14 (2007). (Pubitemid 46834753)
    • (2007) Circulation Research , vol.100 , Issue.10 , pp. 1408-1414
    • Hannigan, G.E.1    Coles, J.G.2    Dedhar, S.3
  • 161
    • 9644281738 scopus 로고    scopus 로고
    • Thymosin β4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair
    • DOI 10.1038/nature03000
    • Bock-Marquette, I., A. Saxena, M. D. White, J. M. Dimaio & D. Srivastava: Thymosin beta4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair. Nature, 432, 466-72 (2004). (Pubitemid 39576522)
    • (2004) Nature , vol.432 , Issue.7016 , pp. 466-472
    • Bock-Marquette, I.1    Saxena, A.2    White, M.D.3    DiMaio, J.M.4    Srivastava, D.5
  • 162
    • 0842288224 scopus 로고    scopus 로고
    • A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5
    • DOI 10.1083/jcb.200309159
    • Akazawa, H., S. Kudoh, N. Mochizuki, N. Takekoshi, H. Takano, T. Nagai & I. Komuro: A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5. J Cell Biol, 164, 395-405 (2004). (Pubitemid 38174767)
    • (2004) Journal of Cell Biology , vol.164 , Issue.3 , pp. 395-405
    • Akazawa, H.1    Kudoh, S.2    Mochizuki, N.3    Takekoshi, N.4    Takano, H.5    Nagai, T.6    Komuro, I.7
  • 164
    • 0026095665 scopus 로고
    • A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region
    • Bellacosa, A., J. R. Testa, S. P. Staal & P. N. Tsichlis: A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region. Science, 254, 274-7 (1991). (Pubitemid 21917339)
    • (1991) Science , vol.254 , Issue.5029 , pp. 274-277
    • Bellacosa, A.1    Testa, J.R.2    Staal, S.P.3    Tsichlis, P.N.4
  • 165
    • 0026006501 scopus 로고
    • Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families
    • Coffer, P. J. & J. R. Woodgett: Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families. Eur J Biochem, 201, 475-81 (1991).
    • (1991) Eur J Biochem , vol.201 , pp. 475-481
    • Coffer, P.J.1    Woodgett, J.R.2
  • 174
    • 58149110431 scopus 로고    scopus 로고
    • Shear stress and vascular smooth muscle cells promote endothelial differentiation of endothelial progenitor cells via activation of Akt
    • Bristol, Avon
    • Ye, C., L. Bai, Z. Q. Yan, Y. H. Wang & Z. L. Jiang: Shear stress and vascular smooth muscle cells promote endothelial differentiation of endothelial progenitor cells via activation of Akt. Clin Biomech (Bristol, Avon) (2007).
    • (2007) Clin Biomech
    • Ye, C.1    Bai, L.2    Yan, Z.Q.3    Wang, Y.H.4    Jiang, Z.L.5
  • 176
    • 0037064005 scopus 로고    scopus 로고
    • Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase
    • DOI 10.1074/jbc.M203387200
    • Conus, N. M., K. M. Hannan, B. E. Cristiano, B. A. Hemmings & R. B. Pearson: Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase. J Biol Chem, 277, 38021-8 (2002). (Pubitemid 35154653)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38021-38028
    • Conus, N.M.1    Hannan, K.M.2    Cristiano, B.E.3    Hemmings, B.A.4    Pearson, R.B.5
  • 177
    • 28844434558 scopus 로고    scopus 로고
    • 473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes
    • DOI 10.1074/jbc.M508361200
    • Hresko, R. C. & M. Mueckler: mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes. J Biol Chem, 280, 40406-16 (2005). (Pubitemid 41780527)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40406-40416
    • Hresko, R.C.1    Mueckler, M.2
  • 179
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • DOI 10.1038/35077225
    • Blume-Jensen, P. & T. Hunter: Oncogenic kinase signalling. Nature, 411, 355-65 (2001). (Pubitemid 32467045)
    • (2001) Nature , vol.411 , Issue.6835 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 180
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • DOI 10.1126/science.1106148
    • Sarbassov, D. D., D. A. Guertin, S. M. Ali & D. M. Sabatini: Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science, 307, 1098-101 (2005). (Pubitemid 40262113)
    • (2005) Science , vol.307 , Issue.5712 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 182
    • 0029979722 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase
    • DOI 10.1074/jbc.271.42.26329
    • Chen, H. C., P. A. Appeddu, H. Isoda & J. L. Guan: Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase. J Biol Chem, 271, 26329-34 (1996). (Pubitemid 26347485)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.42 , pp. 26329-26334
    • Chen, H.-C.1    Appeddu, P.A.2    Isoda, H.3    Guan, J.-L.4
  • 183
    • 11344254134 scopus 로고    scopus 로고
    • β1-Integrins induce phosphorylation of Akt on serine 473 independently of focal adhesion kinase and Src family kinases
    • DOI 10.1038/sj.embor.7400234, PII 7400234
    • Velling, T., S. Nilsson, A. Stefansson & S. Johansson: beta1-Integrins induce phosphorylation of Akt on serine 473 independently of focal adhesion kinase and Src family kinases. EMBO Rep, 5, 901-5 (2004). (Pubitemid 350011236)
    • (2004) EMBO Reports , vol.5 , Issue.9 , pp. 901-905
    • Velling, T.1    Nilsson, S.2    Stefansson, A.3    Johansson, S.4
  • 184
    • 0034983715 scopus 로고    scopus 로고
    • WASP and WAVE family proteins: Key molecules for rapid rearrangement of cortical actin filaments and cell movement
    • Takenawa, T. & H. Miki: WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement. J Cell Sci, 114, 1801-9 (2001). (Pubitemid 32530035)
    • (2001) Journal of Cell Science , vol.114 , Issue.10 , pp. 1801-1809
    • Takenawa, T.1    Miki, H.2
  • 185
    • 0034865456 scopus 로고    scopus 로고
    • Rho GTPases and cell migration
    • Ridley, A. J.: Rho GTPases and cell migration. J Cell Sci, 114, 2713-22 (2001). (Pubitemid 32785451)
    • (2001) Journal of Cell Science , vol.114 , Issue.15 , pp. 2713-2722
    • Ridley, A.J.1
  • 186
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac Take Center Stage
    • DOI 10.1016/S0092-8674(04)00003-0
    • Burridge, K. & K. Wennerberg: Rho and Rac take center stage. Cell, 116, 167-79 (2004). (Pubitemid 38167310)
    • (2004) Cell , vol.116 , Issue.2 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 187
    • 34247175312 scopus 로고    scopus 로고
    • GTP-binding proteins of the Rho/Rac family: Regulation, effectors and functions in vivo
    • DOI 10.1002/bies.20558
    • Bustelo, X. R., V. Sauzeau & I. M. Berenjeno: GTPbinding proteins of the Rho/Rac family: regulation, effectors and functions in vivo. Bioessays, 29, 356-70 (2007). (Pubitemid 46597867)
    • (2007) BioEssays , vol.29 , Issue.4 , pp. 356-370
    • Bustelo, X.R.1    Sauzeau, V.2    Berenjeno, I.M.3
  • 189
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • DOI 10.1042/0264-6021:3480241
    • Bishop, A. L. & A. Hall: Rho GTPases and their effector proteins. Biochem J, 348 Pt 2, 241-55 (2000). (Pubitemid 30345195)
    • (2000) Biochemical Journal , vol.348 , Issue.2 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 190
    • 0035150402 scopus 로고    scopus 로고
    • Rho-Rho-kinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells
    • DOI 10.1016/S0165-6147(00)01596-0, PII S0165614700015960
    • Fukata, Y., M. Amano & K. Kaibuchi: Rho-Rhokinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells. Trends Pharmacol Sci, 22, 32-9 (2001). (Pubitemid 32126284)
    • (2001) Trends in Pharmacological Sciences , vol.22 , Issue.1 , pp. 32-39
    • Fukata, Y.1    Kaibuchi, K.2    Amano, M.3    Kaibuchi, K.4
  • 192
    • 0028980248 scopus 로고
    • Involvement of rho in GTP gamma S-induced enhancement of phosphorylation of 20 kDa myosin light chain in vascular smooth muscle cells: Inhibition of phosphatase activity
    • Noda, M., C. Yasuda-Fukazawa, K. Moriishi, T. Kato, T. Okuda, K. Kurokawa & Y. Takuwa: Involvement of rho in GTP gamma S-induced enhancement of phosphorylation of 20 kDa myosin light chain in vascular smooth muscle cells: inhibition of phosphatase activity. FEBS Lett, 367, 246-50 (1995).
    • (1995) FEBS Lett , vol.367 , pp. 246-250
    • Noda, M.1    Yasuda-Fukazawa, C.2    Moriishi, K.3    Kato, T.4    Okuda, T.5    Kurokawa, K.6    Takuwa, Y.7
  • 193
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso, O. A., M. Chiariello, J. C. Yu, H. Teramoto, P. Crespo, N. Xu, T. Miki & J. S. Gutkind: The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell, 81, 1137-46 (1995).
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, J.S.8
  • 194
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • Minden, A., A. Lin, F. X. Claret, A. Abo & M. Karin: Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell, 81, 1147-57 (1995).
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.X.3    Abo, A.4    Karin, M.5
  • 195
    • 0032841725 scopus 로고    scopus 로고
    • Activation of the small GTPase Cdc42 by the inflammatory cytokines TNFα and IL-1, and by the Epstein-Barr virus transforming protein LMP1
    • Puls, A., A. G. Eliopoulos, C. D. Nobes, T. Bridges, L. S. Young & A. Hall: Activation of the small GTPase Cdc42 by the inflammatory cytokines TNF (alpha) and IL-1, and by the Epstein-Barr virus transforming protein LMP1. J Cell Sci, 112 (Pt 17), 2983-92 (1999). (Pubitemid 29430043)
    • (1999) Journal of Cell Science , vol.112 , Issue.17 , pp. 2983-2992
    • Puls, A.1    Eliopoulos, A.G.2    Nobes, C.D.3    Bridges, T.4    Young, L.S.5    Hall, A.6
  • 196
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo, P. D., D. Drechsel & A. Hall: A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J Biol Chem, 270, 29071-4 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 197
    • 0345826110 scopus 로고    scopus 로고
    • RhoA Binds to the Amino Terminus of MEKK1 and Regulates Its Kinase Activity
    • DOI 10.1074/jbc.M309525200
    • Gallagher, E. D., S. Gutowski, P. C. Sternweis & M. H. Cobb: RhoA binds to the amino terminus of MEKK1 and regulates its kinase activity. J Biol Chem, 279, 1872-7 (2004). (Pubitemid 38084456)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.3 , pp. 1872-1877
    • Gallagher, E.D.1    Gutowski, S.2    Sternweis, P.C.3    Cobb, M.H.4
  • 198
    • 0029913510 scopus 로고    scopus 로고
    • Signaling from the small GTP-binding proteins Rac1 and Cdc42 to the c- Jun N-terminal kinase/stress-activated protein kinase pathway: A role for mixed lineage kinase 3/protein-tyrosine kinase 1, a novel member of the mixed lineage kinase family
    • DOI 10.1074/jbc.271.44.27225
    • Teramoto, H., O. A. Coso, H. Miyata, T. Igishi, T. Miki & J. S. Gutkind: Signaling from the small GTP-binding proteins Rac1 and Cdc42 to the c-Jun N-terminal kinase/stress-activated protein kinase pathway. A role for mixed lineage kinase 3/protein-tyrosine kinase 1, a novel member of the mixed lineage kinase family. J Biol Chem, 271, 27225-8 (1996). (Pubitemid 26367270)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.44 , pp. 27225-27228
    • Teramoto, H.1    Coso, O.A.2    Miyata, H.3    Igishi, T.4    Miki, T.5    Silvio Gutkind, J.6
  • 199
    • 0029911520 scopus 로고    scopus 로고
    • The small GTP-binding protein Rho activates c-Jun N-terminal kinases/stress-activated protein kinases in human kidney 293T cells. Evidence for a Pak-independent signaling pathway
    • DOI 10.1074/jbc.271.42.25731
    • Teramoto, H., P. Crespo, O. A. Coso, T. Igishi, N. Xu & J. S. Gutkind: The small GTP-binding protein rho activates c-Jun N-terminal kinases/stress-activated protein kinases in human kidney 293T cells. Evidence for a Pakindependent signaling pathway. J Biol Chem, 271, 25731-4 (1996). (Pubitemid 26347396)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.42 , pp. 25731-25734
    • Teramoto, H.1    Crespo, P.2    Coso, O.A.3    Igishi, T.4    Xu, N.5    Gutkind, J.S.6
  • 200
    • 0027279176 scopus 로고
    • How receptor tyrosine kinases activate Ras
    • DOI 10.1016/0968-0004(93)90031-H
    • Schlessinger, J.: How receptor tyrosine kinases activate Ras. Trends Biochem Sci, 18, 273-5 (1993). (Pubitemid 23233561)
    • (1993) Trends in Biochemical Sciences , vol.18 , Issue.8 , pp. 273-275
    • Schlessinger, J.1
  • 201
    • 10944244704 scopus 로고    scopus 로고
    • Rho signalling at a glance
    • DOI 10.1242/jcs.01582
    • Schwartz, M.: Rho signalling at a glance. J Cell Sci, 117, 5457-8 (2004). (Pubitemid 40012192)
    • (2004) Journal of Cell Science , vol.117 , Issue.23 , pp. 5457-5458
    • Schwartz, M.1
  • 204
    • 0036315845 scopus 로고    scopus 로고
    • α5β1 integrin activates an NF-κB-dependent program of gene expression important for angiogenesis and inflammation
    • DOI 10.1128/MCB.22.16.5912-5922.2002
    • Klein, S., A. R. de Fougerolles, P. Blaikie, L. Khan, A. Pepe, C. D. Green, V. Koteliansky & F. G. Giancotti: Alpha 5 beta 1 integrin activates an NF-kappa B-dependent program of gene expression important for angiogenesis and inflammation. Mol Cell Biol, 22, 5912-22 (2002). (Pubitemid 34815839)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.16 , pp. 5912-5922
    • Klein, S.1    De Fougerolles, A.R.2    Blaikie, P.3    Khan, L.4    Pepe, A.5    Green, C.D.6    Koteliansky, V.7    Giancotti, F.G.8
  • 205
    • 0030790752 scopus 로고    scopus 로고
    • Studies on the function of rho A protein in cardiac myofibrillogenesis
    • Wang, S. M., Y. J. Tsai, M. J. Jiang & Y. Z. Tseng: Studies on the function of rho A protein in cardiac myofibrillogenesis. J Cell Biochem, 66, 43-53 (1997).
    • (1997) J Cell Biochem , vol.66 , pp. 43-53
    • Wang, S.M.1    Tsai, Y.J.2    Jiang, M.J.3    Tseng, Y.Z.4
  • 206
    • 0030893060 scopus 로고    scopus 로고
    • MAP kinase- and Rho-dependent signals interact to regulate gene expression but not actin morphology in cardiac muscle cells
    • DOI 10.1093/emboj/16.8.1888
    • Thorburn, J., S. Xu & A. Thorburn: MAP kinase- and Rho-dependent signals interact to regulate gene expression but not actin morphology in cardiac muscle cells. Embo J, 16, 1888-900 (1997). (Pubitemid 27170950)
    • (1997) EMBO Journal , vol.16 , Issue.8 , pp. 1888-1900
    • Thorburn, J.1    Xu, S.2    Thorburn, A.3
  • 209
    • 27744466333 scopus 로고    scopus 로고
    • +/- haploinsufficient mice
    • DOI 10.1161/CIRCULATIONAHA.105.584623
    • Rikitake, Y., N. Oyama, C. Y. Wang, K. Noma, M. Satoh, H. H. Kim & J. K. Liao: Decreased perivascular fibrosis but not cardiac hypertrophy in ROCK1+/-haploinsufficient mice. Circulation, 112, 2959-65 (2005). (Pubitemid 41612298)
    • (2005) Circulation , vol.112 , Issue.19 , pp. 2959-2965
    • Rikitake, Y.1    Oyama, N.2    Wang, C.-Y.C.3    Noma, K.4    Satoh, M.5    Kim, H.-H.6    Liao, J.K.7
  • 210
    • 2442509844 scopus 로고    scopus 로고
    • Long-Term Inhibition of Rho-Kinase Suppresses Left Ventricular Remodeling after Myocardial Infarction in Mice
    • DOI 10.1161/01.CIR.0000127939.16111.58
    • Hattori, T., H. Shimokawa, M. Higashi, J. Hiroki, Y. Mukai, H. Tsutsui, K. Kaibuchi & A. Takeshita: Long-term inhibition of Rho-kinase suppresses left ventricular remodeling after myocardial infarction in mice. Circulation, 109, 2234-9 (2004). (Pubitemid 38625402)
    • (2004) Circulation , vol.109 , Issue.18 , pp. 2234-2239
    • Hattori, T.1    Shimokawa, H.2    Higashi, M.3    Hiroki, J.4    Mukai, Y.5    Tsutsui, H.6    Kaibuchi, K.7    Takeshita, A.8
  • 213
  • 215
    • 0032563677 scopus 로고    scopus 로고
    • 'Stress-responsive' mitogen-activated protein kinases (c-Jun N-terminal kinases and p38 mitogen-activated protein kinases) in the myocardium
    • Sugden, P. H. & A. Clerk: "Stress-responsive" mitogen-activated protein kinases (c-Jun N-terminal kinases and p38 mitogen-activated protein kinases) in the myocardium. Circ Res, 83, 345-52 (1998). (Pubitemid 28389964)
    • (1998) Circulation Research , vol.83 , Issue.4 , pp. 345-352
    • Sugden, P.H.1    Clerk, A.2
  • 218
    • 0031817208 scopus 로고    scopus 로고
    • The p38 MAP kinase pathway and its biological function
    • DOI 10.1016/S1050-1738(98)00012-7, PII S1050173898000127
    • New, L. & J. Han: The p38 MAP kinase pathway and its biological function. Trends Cardiovasc Med, 8, 220-8 (1998). (Pubitemid 28345826)
    • (1998) Trends in Cardiovascular Medicine , vol.8 , Issue.5 , pp. 220-228
    • New, L.1    Han, J.2
  • 219
    • 0344924887 scopus 로고    scopus 로고
    • Redefining the roles of p38 and JNK signaling in cardiac hypertrophy: Dichotomy between cultured myocytes and animal models
    • DOI 10.1016/j.yjmcc.2003.10.001
    • Liang, Q. & J. D. Molkentin: Redefining the roles of p38 and JNK signaling in cardiac hypertrophy: dichotomy between cultured myocytes and animal models. J Mol Cell Cardiol, 35, 1385-94 (2003). (Pubitemid 37491181)
    • (2003) Journal of Molecular and Cellular Cardiology , vol.35 , Issue.12 , pp. 1385-1394
    • Liang, Q.1    Molkentin, J.D.2
  • 220
    • 0027521065 scopus 로고
    • Mechanical stretch rapidly activates multiple signal transduction pathways in cardiac myocytes: Potential involvement of an autocrine/paracrine mechanism
    • Sadoshima, J. & S. Izumo: Mechanical stretch rapidly activates multiple signal transduction pathways in cardiac myocytes: potential involvement of an autocrine/paracrine mechanism. Embo J, 12, 1681-92 (1993). (Pubitemid 23112823)
    • (1993) EMBO Journal , vol.12 , Issue.4 , pp. 1681-1692
    • Sadoshima, J.-I.1    Izumo, S.2
  • 221
    • 23244463333 scopus 로고    scopus 로고
    • 2-terminal kinase) are differentially regulated during cardiac volume and pressure overload hypertrophy
    • Sopontammarak, S., A. Aliharoob, C. Ocampo, R. A. Arcilla, M. P. Gupta & M. Gupta: Mitogen-activated protein kinases (p38 and c-Jun NH2-terminal kinase) are differentially regulated during cardiac volume and pressure overload hypertrophy. Cell Biochem Biophys, 43, 61-76 (2005). (Pubitemid 41095274)
    • (2005) Cell Biochemistry and Biophysics , vol.43 , Issue.1 , pp. 61-76
    • Sopontammarak, S.1    Aliharoob, A.2    Ocampo, C.3    Arcilla, R.A.4    Gupta, M.P.5    Gupta, M.6
  • 223
    • 0028805807 scopus 로고
    • The mitogen-activated protein kinase kinase MEK1 stimulates a pattern of gene expression typical of the hypertrophic phenotype in rat ventricular cardiomyocytes
    • Gillespie-Brown, J., S. J. Fuller, M. A. Bogoyevitch, S. Cowley & P. H. Sugden: The mitogen-activated protein kinase kinase MEK1 stimulates a pattern of gene expression typical of the hypertrophic phenotype in rat ventricular cardiomyocytes. J Biol Chem, 270, 28092-6 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 28092-28096
    • Gillespie-Brown, J.1    Fuller, S.J.2    Bogoyevitch, M.A.3    Cowley, S.4    Sugden, P.H.5
  • 224
    • 0030921287 scopus 로고    scopus 로고
    • 1-adrenergic receptor and Ras activation and is associated with in vitro and in vivo cardiac hypertrophy
    • DOI 10.1074/jbc.272.22.14057
    • Ramirez, M. T., V. P. Sah, X. L. Zhao, J. J. Hunter, K. R. Chien & J. H. Brown: The MEKK-JNK pathway is stimulated by alpha1-adrenergic receptor and ras activation and is associated with in vitro and in vivo cardiac hypertrophy. J Biol Chem, 272, 14057-61 (1997). (Pubitemid 27232807)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.22 , pp. 14057-14061
    • Ramirez, M.T.1    Sah, V.P.2    Zhao, X.-L.3    Hunter, J.J.4    Chien, K.R.5    Brown, J.H.6
  • 225
    • 0031844392 scopus 로고    scopus 로고
    • Opposing effects of Jun kinase and p38 mitogen-activated protein kinases on cardiomyocyte hypertrophy
    • Nemoto, S., Z. Sheng & A. Lin: Opposing effects of Jun kinase and p38 mitogen-activated protein kinases on cardiomyocyte hypertrophy. Mol Cell Biol, 18, 3518-26 (1998). (Pubitemid 28240524)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.6 , pp. 3518-3526
    • Nemoto, S.1    Sheng, Z.2    Lin, A.3
  • 227
    • 3442879850 scopus 로고    scopus 로고
    • Mitogenic signal transduction by integrin- and growth factor receptor-mediated pathways
    • Lee, J. W. & R. Juliano: Mitogenic signal transduction by integrin- and growth factor receptor-mediated pathways. Mol Cells, 17, 188-202 (2004). (Pubitemid 39137065)
    • (2004) Molecules and Cells , vol.17 , Issue.2 , pp. 188-202
    • Lee, J.W.1    Juliano, R.2
  • 228
    • 0030874021 scopus 로고    scopus 로고
    • Integrin-mediated activation of MAP kinase is independent of FAK: Evidence for dual integrin signaling pathways in fibroblasts
    • DOI 10.1083/jcb.136.6.1385
    • Lin, T. H., A. E. Aplin, Y. Shen, Q. Chen, M. Schaller, L. Romer, I. Aukhil & R. L. Juliano: Integrin-mediated activation of MAP kinase is independent of FAK: evidence for dual integrin signaling pathways in fibroblasts. J Cell Biol, 136, 1385-95 (1997). (Pubitemid 27421923)
    • (1997) Journal of Cell Biology , vol.136 , Issue.6 , pp. 1385-1395
    • Lin, T.H.1    Aplin, A.E.2    Shen, Y.3    Chen, Q.4    Schaller, M.5    Romer, L.6    Aukhil, I.7    Juliano, R.L.8
  • 229
    • 34047232485 scopus 로고    scopus 로고
    • β1 integrins modulate β-adrenergic receptor-stimulated cardiac myocyte apoptosis and myocardial remodeling
    • DOI 10.1161/01.HYP.0000258703.36986.13
    • Krishnamurthy, P., V. Subramanian, M. Singh & K. Singh: Beta1 integrins modulate beta-adrenergic receptor-stimulated cardiac myocyte apoptosis and myocardial remodeling. Hypertension, 49, 865-72 (2007). (Pubitemid 351664231)
    • (2007) Hypertension , vol.49 , Issue.4 , pp. 865-872
    • Krishnamurthy, P.1    Subramanian, V.2    Singh, M.3    Singh, K.4
  • 230
    • 0035824920 scopus 로고    scopus 로고
    • Integrin and growth factor receptor crosstalk
    • Eliceiri, B. P.: Integrin and growth factor receptor crosstalk. Circ Res, 89, 1104-10 (2001). (Pubitemid 34627867)
    • (2001) Circulation Research , vol.89 , Issue.12 , pp. 1104-1110
    • Eliceiri, B.P.1
  • 233
    • 0035253672 scopus 로고    scopus 로고
    • 1 phase cell-cycle progression
    • DOI 10.1016/S0959-437X(00)00155-6
    • Assoian, R. K. & M. A. Schwartz: Coordinate signaling by integrins and receptor tyrosine kinases in the regulation of G1 phase cell-cycle progression. Curr Opin Genet Dev, 11, 48-53 (2001). (Pubitemid 32119277)
    • (2001) Current Opinion in Genetics and Development , vol.11 , Issue.1 , pp. 48-53
    • Assoian, R.K.1    Schwartz, M.A.2
  • 234
    • 0034990603 scopus 로고    scopus 로고
    • Integrin regulation of receptor tyrosine kinase and G protein-coupled receptor signaling to mitogen-activated protein kinases
    • DOI 10.1016/S0076-6879(01)33053-7
    • Juliano, R. L., A. E. Aplin, A. K. Howe, S. Short, J. W. Lee & S. Alahari: Integrin regulation of receptor tyrosine kinase and G protein-coupled receptor signaling to mitogen-activated protein kinases. Methods Enzymol, 333, 151-63 (2001). (Pubitemid 32507306)
    • (2001) Methods in Enzymology , vol.333 , pp. 151-163
    • Juliano, R.L.1    Aplin, A.E.2    Howe, A.K.3    Short, S.4    Lee, J.W.5    Alahari, S.6
  • 235
    • 34748863572 scopus 로고    scopus 로고
    • Mechanisms of integrin-vascular endothelial growth factor receptor cross-activation in angiogenesis
    • DOI 10.1161/CIRCRESAHA.107.155655
    • Mahabeleshwar, G. H., W. Feng, K. Reddy, E. F. Plow & T. V. Byzova: Mechanisms of integrin-vascular endothelial growth factor receptor cross-activation in angiogenesis. Circ Res, 101, 570-80 (2007). (Pubitemid 351325874)
    • (2007) Circulation Research , vol.101 , Issue.6 , pp. 570-580
    • Mahabeleshwar, G.H.1    Feng, W.2    Reddy, K.3    Plow, E.F.4    Byzova, T.V.5
  • 236
    • 33645359717 scopus 로고    scopus 로고
    • Crosstalk between hepatocyte growth factor and integrin signaling pathways
    • Chan, P. C., S. Y. Chen, C. H. Chen & H. C. Chen: Crosstalk between hepatocyte growth factor and integrin signaling pathways. J Biomed Sci, 13, 215-23 (2006).
    • (2006) J Biomed Sci , vol.13 , pp. 215-223
    • Chan, P.C.1    Chen, S.Y.2    Chen, C.H.3    Chen, H.C.4
  • 237
    • 0141756154 scopus 로고    scopus 로고
    • Interactions between growth factor receptors and adhesion molecules: Breaking the rules
    • DOI 10.1016/S0955-0674(03)00096-6
    • Comoglio, P. M., C. Boccaccio & L. Trusolino: Interactions between growth factor receptors and adhesion molecules: breaking the rules. Curr Opin Cell Biol, 15, 565-71 (2003). (Pubitemid 37176965)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.5 , pp. 565-571
    • Comoglio, P.M.1    Boccaccio, C.2    Trusolino, L.3
  • 239
    • 0035807999 scopus 로고    scopus 로고
    • Protection against oxidized low-density lipoprotein-induced vascular endothelial cell death by integrin-linked kinase
    • Zhang, X., K. Hu & C. Y. Li: Protection against oxidized low-density lipoprotein-induced vascular endothelial cell death by integrin-linked kinase. Circulation, 104, 2762-6 (2001). (Pubitemid 33126647)
    • (2001) Circulation , vol.104 , Issue.23 , pp. 2762-2766
    • Zhang, X.1    Hu, K.2    Li, C.-Y.3
  • 240
    • 4444351635 scopus 로고    scopus 로고
    • Microarray analysis of extracellular matrix genes expression in myocardium of mouse with Coxsackie virus B3 myocarditis
    • Zhang, Z. C., S. J. Li, Y. Z. Yang, R. Z. Chen, J. B. Ge & H. Z. Chen: Microarray analysis of extracellular matrix genes expression in myocardium of mouse with Coxsackie virus B3 myocarditis. Chin Med J (Engl), 117, 1228-31 (2004).
    • (2004) Chin Med J (Engl) , vol.117 , pp. 1228-1231
    • Zhang, Z.C.1    Li, S.J.2    Yang, Y.Z.3    Chen, R.Z.4    Ge, J.B.5    Chen, H.Z.6
  • 248
    • 5644285411 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase inhibition improves cardiac function and attenuates left ventricular remodeling following myocardial infarction in the rat
    • DOI 10.1016/j.jacc.2004.07.038, PII S0735109704015372
    • See, F., W. Thomas, K. Way, A. Tzanidis, A. Kompa, D. Lewis, S. Itescu & H. Krum: p38 mitogen-activated protein kinase inhibition improves cardiac function and attenuates left ventricular remodeling following myocardial infarction in the rat. J Am Coll Cardiol, 44, 1679-89 (2004). (Pubitemid 39369804)
    • (2004) Journal of the American College of Cardiology , vol.44 , Issue.8 , pp. 1679-1689
    • See, F.1    Thomas, W.2    Way, K.3    Tzanidis, A.4    Kompa, A.5    Lewis, D.6    Itescu, S.7    Krum, H.8
  • 249
    • 13444256258 scopus 로고    scopus 로고
    • Inhibition of p38 mitogen-activated protein kinase protects the heart against cardiac remodeling in mice with heart failure resulting from myocardial infarction
    • DOI 10.1016/j.cardfail.2004.04.004
    • Liu, Y. H., D. Wang, N. E. Rhaleb, X. P. Yang, J. Xu, S. S. Sankey, A. E. Rudolph & O. A. Carretero: Inhibition of p38 mitogen-activated protein kinase protects the heart against cardiac remodeling in mice with heart failure resulting from myocardial infarction. J Card Fail, 11, 74-81 (2005). (Pubitemid 40215318)
    • (2005) Journal of Cardiac Failure , vol.11 , Issue.1 , pp. 74-81
    • Liu, Y.-H.1    Wang, D.2    Rhaleb, N.-E.3    Yang, X.-P.4    Xu, J.5    Sankey, S.S.6    Rudolph, A.E.7    Carretero, O.A.8
  • 250
    • 32444446597 scopus 로고    scopus 로고
    • Opposing effect of p38 MAP kinase and JNK inhibitors on the development of heart failure in the cardiomyopathic hamster
    • DOI 10.1016/j.cardiores.2005.11.015, PII S0008636305005274
    • Kyoi, S., H. Otani, S. Matsuhisa, Y. Akita, K. Tatsumi, C. Enoki, H. Fujiwara, H. Imamura, H. Kamihata & T. Iwasaka: Opposing effect of p38 MAP kinase and JNK inhibitors on the development of heart failure in the cardiomyopathic hamster. Cardiovasc Res, 69, 888-98 (2006). (Pubitemid 43227987)
    • (2006) Cardiovascular Research , vol.69 , Issue.4 , pp. 888-898
    • Kyoi, S.1    Otani, H.2    Matsuhisa, S.3    Akita, Y.4    Tatsumi, K.5    Enoki, C.6    Fujiwara, H.7    Imamura, H.8    Kamihata, H.9    Iwasaka, T.10
  • 251
    • 0344011971 scopus 로고    scopus 로고
    • Role of 14-3-3-Mediated p38 Mitogen-Activated Protein Kinase Inhibition in Cardiac Myocyte Survival
    • DOI 10.1161/01.RES.0000104084.88317.91
    • Zhang, S., J. Ren, C. E. Zhang, I. Treskov, Y. Wang & A. J. Muslin: Role of 14-3-3-mediated p38 mitogen-activated protein kinase inhibition in cardiac myocyte survival. Circ Res, 93, 1026-8 (2003). (Pubitemid 37485032)
    • (2003) Circulation Research , vol.93 , Issue.11 , pp. 1026-1028
    • Zhang, S.1    Ren, J.2    Zhang, C.E.3    Treskov, I.4    Wang, Y.5    Muslin, A.J.6
  • 252
    • 0142026209 scopus 로고    scopus 로고
    • P38 MAP kinases: Key signalling molecules as therapeutic targets for inflammatory diseases
    • Kumar, S., J. Boehm & J. C. Lee: p38 MAP kinases: key signalling molecules as therapeutic targets for inflammatory diseases. Nat Rev Drug Discov, 2, 717-26 (2003). (Pubitemid 37361787)
    • (2003) Nature Reviews Drug Discovery , vol.2 , Issue.9 , pp. 717-726
    • Kumar, S.1    Boehm, J.2    Lee, J.C.3
  • 253
    • 79959704816 scopus 로고    scopus 로고
    • TAB1{alpha}, but not TAB1{beta}, mediates cytokine-induced p38 MAPK phosphorylation and cell death in insulin producing cells
    • Makeeva, N., G. M. Roomans, J. W. Myers & N. Welsh: TAB1{alpha}, but not TAB1{beta}, mediates cytokine-induced p38 MAPK phosphorylation and cell death in insulin producing cells. Endocrinology (2007).
    • (2007) Endocrinology
    • Makeeva, N.1    Roomans, G.M.2    Myers, J.W.3    Welsh, N.4
  • 254
    • 1842681652 scopus 로고    scopus 로고
    • Feedback regulation of lymphocyte signalling
    • Reth, M. & T. Brummer: Feedback regulation of lymphocyte signalling. Nat Rev Immunol, 4, 269-77 (2004). (Pubitemid 38478662)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.4 , pp. 269-277
    • Reth, M.1    Brummer, T.2
  • 255
    • 0242473165 scopus 로고    scopus 로고
    • Feedback control of the protein kinase TAK1 by SAPK2a/p38α
    • DOI 10.1093/emboj/cdg552
    • Cheung, P. C., D. G. Campbell, A. R. Nebreda & P. Cohen: Feedback control of the protein kinase TAK1 by SAPK2a/p38alpha. Embo J, 22, 5793-805 (2003). (Pubitemid 37408818)
    • (2003) EMBO Journal , vol.22 , Issue.21 , pp. 5793-5805
    • Cheung, P.C.F.1    Campbell, D.G.2    Nebreda, A.R.3    Cohen, P.4
  • 256
    • 0032489550 scopus 로고    scopus 로고
    • 2-terminal kinase in ventricular muscle cells
    • DOI 10.1074/jbc.273.10.5423
    • Wang, Y., B. Su, V. P. Sah, J. H. Brown, J. Han & K. R. Chien: Cardiac hypertrophy induced by mitogenactivated protein kinase kinase 7, a specific activator for c-Jun NH2-terminal kinase in ventricular muscle cells. J Biol Chem, 273, 5423-6 (1998). (Pubitemid 28124000)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.10 , pp. 5423-5426
    • Wang, Y.1    Su, B.2    Sah, V.P.3    Brown, J.H.4    Han, J.5    Chien, K.R.6
  • 258
    • 1542613386 scopus 로고    scopus 로고
    • Stress-activated MAP kinases in cardiac remodeling and heart failure: New insights from transgenic studies
    • DOI 10.1016/j.tcm.2003.11.002, PII S1050173803001920
    • Petrich, B. G. & Y. Wang: Stress-activated MAP kinases in cardiac remodeling and heart failure; new insights from transgenic studies. Trends Cardiovasc Med, 14, 50-5 (2004). (Pubitemid 38340846)
    • (2004) Trends in Cardiovascular Medicine , vol.14 , Issue.2 , pp. 50-55
    • Petrich, B.G.1    Wang, Y.2
  • 260
    • 0141642015 scopus 로고    scopus 로고
    • C-Jun N-terminal kinases (JNK) antagonize cardiac growth through cross-talk with calcineurin-NFAT signaling
    • DOI 10.1093/emboj/cdg474
    • Liang, Q., O. F. Bueno, B. J. Wilkins, C. Y. Kuan, Y. Xia & J. D. Molkentin: c-Jun N-terminal kinases (JNK) antagonize cardiac growth through cross-talk with calcineurin-NFAT signaling. Embo J, 22, 5079-89 (2003). (Pubitemid 37222028)
    • (2003) EMBO Journal , vol.22 , Issue.19 , pp. 5079-5089
    • Liang, Q.1    Bueno, O.F.2    Wilkins, B.J.3    Kuan, C.-Y.4    Xia, Y.5    Molkentin, J.D.6
  • 261
    • 34548695952 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in heart development and diseases
    • DOI 10.1161/CIRCULATIONAHA.106.679589, PII 0000301720070918000015
    • Wang, Y.: Mitogen-activated protein kinases in heart development and diseases. Circulation, 116, 1413-23 (2007). (Pubitemid 47417568)
    • (2007) Circulation , vol.116 , Issue.12 , pp. 1413-1423
    • Wang, Y.1
  • 264
    • 0034829970 scopus 로고    scopus 로고
    • Stress-activated protein kinase phosphorylation during cardioprotection in the ischemic myocardium
    • Fryer, R. M., H. H. Patel, A. K. Hsu & G. J. Gross: Stress-activated protein kinase phosphorylation during cardioprotection in the ischemic myocardium. Am J Physiol Heart Circ Physiol, 281, H1184-92 (2001).
    • (2001) Am J Physiol Heart Circ Physiol , vol.281
    • Fryer, R.M.1    Patel, H.H.2    Hsu, A.K.3    Gross, G.J.4
  • 265
    • 0038004740 scopus 로고    scopus 로고
    • Targeting JNK for therapeutic benefit: From junk to gold?
    • DOI 10.1038/nrd1132
    • Manning, A. M. & R. J. Davis: Targeting JNK for therapeutic benefit: from junk to gold? Nat Rev Drug Discov, 2, 554-65 (2003). (Pubitemid 37361747)
    • (2003) Nature Reviews Drug Discovery , vol.2 , Issue.7 , pp. 554-565
    • Manning, A.M.1    Davis, R.J.2
  • 266
  • 270
    • 0037334137 scopus 로고    scopus 로고
    • 20 phosphorylation
    • DOI 10.1124/mol.63.3.714
    • Hunter, I., H. J. Cobban, P. Vandenabeele, D. J. MacEwan & G. F. Nixon: Tumor necrosis factor-alphainduced activation of RhoA in airway smooth muscle cells: role in the Ca2+ sensitization of myosin light chain20 phosphorylation. Mol Pharmacol, 63, 714-21 (2003). (Pubitemid 36297345)
    • (2003) Molecular Pharmacology , vol.63 , Issue.3 , pp. 714-721
    • Hunter, I.1    Cobban, H.J.2    Vandenabeele, P.3    Macewan, D.J.4    Nixon, G.F.5
  • 271
    • 0037310774 scopus 로고    scopus 로고
    • Rho kinase and matrix metalloproteinase inhibitors cooperate to inhibit angiogenesis and growth of human prostate cancer xenotransplants
    • DOI 10.1096/fj.02-0655com
    • Somlyo, A. V., C. Phelps, C. Dipierro, M. Eto, P. Read, M. Barrett, J. J. Gibson, M. C. Burnitz, C. Myers & A. P. Somlyo: Rho kinase and matrix metalloproteinase inhibitors cooperate to inhibit angiogenesis and growth of human prostate cancer xenotransplants. Faseb J, 17, 223-34 (2003). (Pubitemid 36164392)
    • (2003) FASEB Journal , vol.17 , Issue.2 , pp. 223-234
    • Somlyo, A.V.1    Phelps, C.2    Dipierro, C.3    Eto, M.4    Read, P.5    Barrett, M.6    Gibson, J.J.7    Burnitz, M.C.8    Myers, C.9    Somlyo, A.P.10
  • 273
    • 34249328150 scopus 로고    scopus 로고
    • Selective ROCK 2 inhibition attenuates arterial plaque formation in an ApoE knockout mouse model
    • Olivier Schueller, O., W. Tong, J. W. Ferkany & P. Sweetnam: Selective ROCK 2 Inhibition Attenuates Arterial Plaque Formation in an ApoE Knockout Mouse Model. Circulation, 114, II-228 (2006).
    • (2006) Circulation , vol.114
    • Olivier Schueller, O.1    Tong, W.2    Ferkany, J.W.3    Sweetnam, P.4
  • 274
    • 0023754423 scopus 로고
    • Discovery, biochemistry and biology of lovastatin
    • Alberts, A. W.: Discovery, biochemistry and biology of lovastatin. Am J Cardiol, 62, 10J-15J (1988). (Pubitemid 18263851)
    • (1988) American Journal of Cardiology , vol.62 , Issue.15
    • Alberts, A.W.1
  • 275
    • 18844476446 scopus 로고    scopus 로고
    • Rapid effect of 3-hydroxy-3-methylglutaryl coenzyme a reductase inhibition on coronary endothelial function
    • Wassmann, S., A. Faul, B. Hennen, B. Scheller, M. Bohm & G. Nickenig: Rapid effect of 3-hydroxy-3-methylglutaryl coenzyme a reductase inhibition on coronary endothelial function. Circ Res, 93, e98-103 (2003).
    • (2003) Circ Res , vol.93
    • Wassmann, S.1    Faul, A.2    Hennen, B.3    Scheller, B.4    Bohm, M.5    Nickenig, G.6
  • 276
    • 0032584177 scopus 로고    scopus 로고
    • Upregulation of endothelial nitric oxide synthase by HMG CoA reductase inhibitors
    • Laufs, U., V. La Fata, J. Plutzky & J. K. Liao: Upregulation of endothelial nitric oxide synthase by HMG CoA reductase inhibitors. Circulation, 97, 1129-35 (1998). (Pubitemid 28152885)
    • (1998) Circulation , vol.97 , Issue.12 , pp. 1129-1135
    • Laufs, U.1    La Fata, V.2    Plutzky, J.3    Liao, J.K.4
  • 277
    • 19044372537 scopus 로고    scopus 로고
    • Long-term inhibition of RhoA attenuates vascular contractility by enhancing endothelial NO production in an intact rabbit mesenteric artery
    • DOI 10.1161/01.RES.0000165483.34603.91
    • Shiga, N., K. Hirano, M. Hirano, J. Nishimura, H. Nawata & H. Kanaide: Long-term inhibition of RhoA attenuates vascular contractility by enhancing endothelial NO production in an intact rabbit mesenteric artery. Circ Res, 96, 1014-21 (2005). (Pubitemid 40712802)
    • (2005) Circulation Research , vol.96 , Issue.9 , pp. 1014-1021
    • Shiga, N.1    Hirano, K.2    Hirano, M.3    Nishimura, J.4    Nawata, H.5    Kanaide, H.6
  • 278
    • 0032745205 scopus 로고    scopus 로고
    • Simvastatin inhibits cardiac hypertrophy and angiotensin-converting enzyme activity in rats with aortic stenosis
    • DOI 10.1046/j.1440-1681.1999.03165.x
    • Luo, J. D., W. W. Zhang, G. P. Zhang, J. X. Guan & X. Chen: Simvastatin inhibits cardiac hypertrophy and angiotensin-converting enzyme activity in rats with aortic stenosis. Clin Exp Pharmacol Physiol, 26, 903-8 (1999). (Pubitemid 29513630)
    • (1999) Clinical and Experimental Pharmacology and Physiology , vol.26 , Issue.11 , pp. 903-908
    • Luo, J.-D.1    Zhang, W.-W.2    Zhang, G.-P.3    Guan, J.-X.4    Chen, X.5
  • 279
    • 0036165659 scopus 로고    scopus 로고
    • Effects of simvastatin on activities of endogenous antioxidant enzymes and angiotensin-converting enzyme in rat myocardium with pressure-overload cardiac hypertrophy
    • Luo, J. D., W. W. Zhang, G. P. Zhang, B. H. Zhong & H. J. Ou: Effects of simvastatin on activities of endogenous antioxidant enzymes and angiotensin-converting enzyme in rat myocardium with pressure-overload cardiac hypertrophy. Acta Pharmacol Sin, 23, 124-8 (2002).
    • (2002) Acta Pharmacol Sin , vol.23 , pp. 124-128
    • Luo, J.D.1    Zhang, W.W.2    Zhang, G.P.3    Zhong, B.H.4    Ou, H.J.5
  • 280
    • 34249034740 scopus 로고    scopus 로고
    • Effect of pravastatin on phenotypical transformation of fibroblasts and hypertrophy of cardiomyocytes in culture
    • DOI 10.1007/s10517-007-0015-0, This issue is a translation of Byullete, Eksperimentale;, oi Biologii i Meditsiny (Bulletin of Experimental Biology and Medicine) and Kletochnye Tekhnologii v Biologii i Meditsine (Cell T
    • Moiseeva, O. M., E. G. Semyonova, E. V. Polevaya & G. P. Pinayev: Effect of pravastatin on phenotypical transformation of fibroblasts and hypertrophy of cardiomyocytes in culture. Bull Exp Biol Med, 143, 54-7 (2007). (Pubitemid 46784874)
    • (2007) Bulletin of Experimental Biology and Medicine , vol.143 , Issue.1 , pp. 54-57
    • Moiseeva, O.M.1    Semyonova, E.G.2    Polevaya, E.V.3    Pinayev, G.P.4
  • 284
    • 33751226584 scopus 로고    scopus 로고
    • Integrin-linked kinase expression is elevated in human cardiac hypertrophy and induces hypertrophy in transgenic mice
    • DOI 10.1161/CIRCULATIONAHA.106.642330, PII 0000301720061121000013
    • Lu, H., P. W. Fedak, X. Dai, C. Du, Y. Q. Zhou, M. Henkelman, P. S. Mongroo, A. Lau, H. Yamabi, A. Hinek, M. Husain, G. Hannigan & J. G. Coles: Integrin-linked kinase expression is elevated in human cardiac hypertrophy and induces hypertrophy in transgenic mice. Circulation, 114, 2271-9 (2006). (Pubitemid 44789501)
    • (2006) Circulation , vol.114 , Issue.21 , pp. 2271-2279
    • Lu, H.1    Fedak, P.W.M.2    Dai, X.3    Du, C.4    Zhou, Y.-Q.5    Henkelman, M.6    Mongroo, P.S.7    Lau, A.8    Yamabi, H.9    Hinek, A.10    Husain, M.11    Hannigan, G.12    Coles, J.G.13


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