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Volumn 115, Issue 7, 2005, Pages 1785-1796

Erratum: The cytoskeletal protein ezrin regulates EC proliferation and angiogenesis via TNF-α-induced transcriptional repression of cyclin A (Journal of Clinical Investigation (2005) 115 (1785-1796) DOI: 10.1172/JCI22849);The cytoskeletal protein ezrin regulates EC proliferation and angiogenesis via TNF-α-induced transcriptional repression of cyclin A

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN A; CYTOSKELETON PROTEIN; EZRIN; RHO KINASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 22144443812     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI22849E1     Document Type: Erratum
Times cited : (70)

References (59)
  • 1
    • 0017370183 scopus 로고
    • Migration and proliferation of endothelial cells in preformed and newly formed blood vessels during tumor angiogenesis
    • Ausprunk, D.H., and Folkman, J. 1977. Migration and proliferation of endothelial cells in preformed and newly formed blood vessels during tumor angiogenesis. Microvasc. Res. 14:53-65.
    • (1977) Microvasc. Res. , vol.14 , pp. 53-65
    • Ausprunk, D.H.1    Folkman, J.2
  • 2
    • 3543074874 scopus 로고
    • Human vascular smooth muscle cells both express and respond to heparin-binding growth factor I (endothelial cell growth factor)
    • Winkles, J.A., et al. 1987. Human vascular smooth muscle cells both express and respond to heparin-binding growth factor I (endothelial cell growth factor). Proc. Natl. Acad. Sci. U. S. A. 84:7124-7128.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 7124-7128
    • Winkles, J.A.1
  • 3
    • 0030010965 scopus 로고    scopus 로고
    • Endothelial cell inflammatory responses to tumor necrosis factor alpha. Ceramide-dependent and -independent mitogen-activated protein kinase cascades
    • Modur, V., Zimmerman, G.A., Prescott, S.M., and McIntyre, T.M. 1996. Endothelial cell inflammatory responses to tumor necrosis factor alpha. Ceramide-dependent and -independent mitogen-activated protein kinase cascades. J. Biol. Chem. 271:13094-13102.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13094-13102
    • Modur, V.1    Zimmerman, G.A.2    Prescott, S.M.3    McIntyre, T.M.4
  • 4
    • 0023192006 scopus 로고
    • Macrophage-induced angiogenesis is mediated by tumour necrosis factor-alpha
    • Leibovich, S.J., et al. 1987. Macrophage-induced angiogenesis is mediated by tumour necrosis factor-alpha. Nature. 329:630-632.
    • (1987) Nature , vol.329 , pp. 630-632
    • Leibovich, S.J.1
  • 5
    • 0031591681 scopus 로고    scopus 로고
    • Interference with c-myc expression and RB phosphorylation during TNF-mediated growth arrest in human endothelial cells
    • Lopez-Marure, R., Bernal, A.E., and Zentella, A. 1997. Interference with c-myc expression and RB phosphorylation during TNF-mediated growth arrest in human endothelial cells. Biochem. Biophys. Res. Commun. 236:819-824.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 819-824
    • Lopez-Marure, R.1    Bernal, A.E.2    Zentella, A.3
  • 6
    • 0032578990 scopus 로고    scopus 로고
    • Restoration of E2F expression rescues vascular endothelial cells from tumor necrosis factor-alpha-induced apoptosis
    • Spyridopoulos, I., et al. 1998. Restoration of E2F expression rescues vascular endothelial cells from tumor necrosis factor-alpha-induced apoptosis. Circulation. 98:2883-2890.
    • (1998) Circulation , vol.98 , pp. 2883-2890
    • Spyridopoulos, I.1
  • 7
    • 0035834031 scopus 로고    scopus 로고
    • In vivo blockade of tumor necrosis factor-alpha accelerates functional endothelial recovery after balloon angioplasty
    • Krasinski, K., Spyridopoulos, I., Kearney, M., and Losordo, D.W. 2001. In vivo blockade of tumor necrosis factor-alpha accelerates functional endothelial recovery after balloon angioplasty. Circulation. 104:1754-1756.
    • (2001) Circulation , vol.104 , pp. 1754-1756
    • Krasinski, K.1    Spyridopoulos, I.2    Kearney, M.3    Losordo, D.W.4
  • 8
    • 0033911968 scopus 로고    scopus 로고
    • Ceramide mimics tumour necrosis factor-alpha in the induction of cell cycle arrest in endothelial cells. Induction of the tumour suppressor p53 with decrease in retinoblastoma/protein levels
    • Lopez-Marure, R., Ventura, J.L., Sanchez, L., Montano, L.F., and Zentella, A. 2000. Ceramide mimics tumour necrosis factor-alpha in the induction of cell cycle arrest in endothelial cells. Induction of the tumour suppressor p53 with decrease in retinoblastoma/protein levels. Eur. J. Biochem. 267:4325-4333.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4325-4333
    • Lopez-Marure, R.1    Ventura, J.L.2    Sanchez, L.3    Montano, L.F.4    Zentella, A.5
  • 9
    • 0037163097 scopus 로고    scopus 로고
    • Functionally novel tumor necrosis factor-alpha-modulated CHR-binding protein mediates cyclin a transcriptional repression in vascular endothelial cells
    • Kishore, R., Spyri-dopoulos, I., Luedemann, C., and Losordo, DAV. 2002. Functionally novel tumor necrosis factor-alpha-modulated CHR-binding protein mediates cyclin A transcriptional repression in vascular endothelial cells. Circ. Res. 91:307-314.
    • (2002) Circ. Res. , vol.91 , pp. 307-314
    • Kishore, R.1    Spyri-dopoulos, I.2    Luedemann, C.3    Losordo, D.A.V.4
  • 10
    • 0030800927 scopus 로고    scopus 로고
    • The ezrin protein family: Membrane-cytoskeleton interactions and disease associations
    • Vaheri, A., et al. 1997. The ezrin protein family: membrane-cytoskeleton interactions and disease associations [review]. Curr. Opin. Cell Biol. 9:659-666.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 659-666
    • Vaheri, A.1
  • 11
    • 0031471375 scopus 로고    scopus 로고
    • Ezrin: A protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures
    • Bretscher, A., Reczek, D., and Berryman, M. 1997. Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J. Cell Sci. 110:3011-3018.
    • (1997) J. Cell Sci. , vol.110 , pp. 3011-3018
    • Bretscher, A.1    Reczek, D.2    Berryman, M.3
  • 12
    • 0033521010 scopus 로고    scopus 로고
    • Cortical actin organization: Lessons from ERM (ezrin/radixin/ moesin) proteins
    • Tsukita, S., and Yonemura, S. 1999. Cortical actin organization: lessons from ERM (ezrin/radixin/ moesin) proteins. J. Biol. Chem. 274:34507-34510.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34507-34510
    • Tsukita, S.1    Yonemura, S.2
  • 13
    • 0033523986 scopus 로고    scopus 로고
    • Activation of ERM proteins in vivo by Rho involves phosphatidyl-inositol 4-phosphate 5-kinase and not ROCK kinases
    • Matsui, T., Yonemura, S., and Tsukita, S. 1999. Activation of ERM proteins in vivo by Rho involves phosphatidyl-inositol 4-phosphate 5-kinase and not ROCK kinases. Curr. Biol. 9:1259-1262.
    • (1999) Curr. Biol. , vol.9 , pp. 1259-1262
    • Matsui, T.1    Yonemura, S.2    Tsukita, S.3
  • 14
    • 0029121577 scopus 로고
    • Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding sice
    • Gary, R., and Bretscher, A. 1995. Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding sice. Mol. Biol. Cell. 6:1061-1075.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1061-1075
    • Gary, R.1    Bretscher, A.2
  • 15
    • 0032547839 scopus 로고    scopus 로고
    • Suppression of radixin and moesin alters growth cone morphology, motility, and process formation in primary cultured neurons
    • Paglini, G., Kunda, P., Quiroga, S., Kosik, K., and Caceres, A. 1998. Suppression of radixin and moesin alters growth cone morphology, motility, and process formation in primary cultured neurons. J. Cell Biol. 143:443-455.
    • (1998) J. Cell Biol. , vol.143 , pp. 443-455
    • Paglini, G.1    Kunda, P.2    Quiroga, S.3    Kosik, K.4    Caceres, A.5
  • 16
    • 0033777011 scopus 로고    scopus 로고
    • ERM proteins: From cellular architecture to cell signaling
    • Louvet-Vallee, S. 2000. ERM proteins: from cellular architecture to cell signaling. Biol. Cell. 92:305-316.
    • (2000) Biol. Cell. , vol.92 , pp. 305-316
    • Louvet-Vallee, S.1
  • 17
    • 0036468423 scopus 로고    scopus 로고
    • ERM proteins and NF2 tumor suppressor: The Yin and Yang of cortical actin organization and cell growth signaling
    • Gautreau, A., Louvard, D., and Arpin, M. 2002. ERM proteins and NF2 tumor suppressor: the Yin and Yang of cortical actin organization and cell growth signaling [review]. Curr. Opin. Cell Biol. 14:104-109.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 104-109
    • Gautreau, A.1    Louvard, D.2    Arpin, M.3
  • 18
    • 2642615752 scopus 로고    scopus 로고
    • Regulation of TNF-alpha-induced reorganization of the actin cytoskeleton and cell-cell junctions by Rho, Rac, and Cdc42 in human endochelial cells
    • Wojciak-Stothard, B., Entwiscle, A., Garg, R., and Ridlev, A.J. 1998. Regulation of TNF-alpha-induced reorganization of the actin cytoskeleton and cell-cell junctions by Rho, Rac, and Cdc42 in human endochelial cells. J. Cell. Physiol. 176:150-165.
    • (1998) J. Cell. Physiol. , vol.176 , pp. 150-165
    • Wojciak-Stothard, B.1    Entwiscle, A.2    Garg, R.3    Ridlev, A.J.4
  • 19
    • 0037334827 scopus 로고    scopus 로고
    • Caspase-dependent cleavage of myosin light chain kinase (MLCK) is involved in TNF-alpha-mediated bovine pulmonary endothelial cell apoptosis
    • Petrache, I., et al. 2003. Caspase-dependent cleavage of myosin light chain kinase (MLCK) is involved in TNF-alpha-mediated bovine pulmonary endothelial cell apoptosis. FASEB J. 17:407-416.
    • (2003) FASEB J. , vol.17 , pp. 407-416
    • Petrache, I.1
  • 20
    • 0031781796 scopus 로고    scopus 로고
    • Mouse model of angiogenesis
    • Couffinhal, T., et al. 1998. Mouse model of angiogenesis. Am. J. Pathol. 152:1667-1679.
    • (1998) Am. J. Pathol. , vol.152 , pp. 1667-1679
    • Couffinhal, T.1
  • 21
    • 0026802046 scopus 로고
    • A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites
    • Sato, N., Funayama, N., Nagafuchi, A., Yonemura, S., and Tsukita, S. 1992. A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites J. Cell Sci. 103:131-143.
    • (1992) J. Cell Sci. , vol.103 , pp. 131-143
    • Sato, N.1    Funayama, N.2    Nagafuchi, A.3    Yonemura, S.4    Tsukita, S.5
  • 22
    • 0027183643 scopus 로고
    • Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells
    • Berryman, M., Franck, Z., and Bretscher, A. 1993. Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. J. Cell Sci. 105:1025-1043.
    • (1993) J. Cell Sci. , vol.105 , pp. 1025-1043
    • Berryman, M.1    Franck, Z.2    Bretscher, A.3
  • 23
    • 0028206028 scopus 로고
    • Radixin is a component of hepatocyte microvilli in situ
    • Amieva, M.R., Wilgenbus, K.K., and Furthmayr, H. 1994. Radixin is a component of hepatocyte microvilli in situ. Exp. Cell Res. 210:140-144.
    • (1994) Exp. Cell Res. , vol.210 , pp. 140-144
    • Amieva, M.R.1    Wilgenbus, K.K.2    Furthmayr, H.3
  • 24
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
    • Tsukita, S., Oishi, K., Sato, N., Sagara, J., and Kawai, A. 1994. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J. Cell Biol. 126:391-401.
    • (1994) J. Cell Biol. , vol.126 , pp. 391-401
    • Tsukita, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5
  • 25
    • 0029892980 scopus 로고    scopus 로고
    • Cytokine regulation of ezrin expression in the human colon cancer cell line HT29
    • Jiang, W.G., and Hiscox, S. 1996. Cytokine regulation of ezrin expression in the human colon cancer cell line HT29. Anticancer Res. 16:861-865.
    • (1996) Anticancer Res. , vol.16 , pp. 861-865
    • Jiang, W.G.1    Hiscox, S.2
  • 26
    • 0035892765 scopus 로고    scopus 로고
    • Ovarian epithelial carcinoma tyrosine phosphorylation, cell proliferation, and ezrin translocation are stimulated by interleukin 1alpha and epidermal growth factor
    • Chen, Z., et al. 2001. Ovarian epithelial carcinoma tyrosine phosphorylation, cell proliferation, and ezrin translocation are stimulated by interleukin 1alpha and epidermal growth factor. Cancer. 92:3068-3075.
    • (2001) Cancer , vol.92 , pp. 3068-3075
    • Chen, Z.1
  • 27
    • 13944284677 scopus 로고    scopus 로고
    • The cytoskeleton: From regulation to function
    • Conference: the 15th Meeting of the European Cytoskeleton Forum.
    • Bretscher, A. 2000. The cytoskeleton: from regulation to function. Conference: the 15th Meeting of the European Cytoskeleton Forum. EMBO Rep. 1:473-476.
    • (2000) EMBO Rep. , vol.1 , pp. 473-476
    • Bretscher, A.1
  • 28
    • 0033542725 scopus 로고    scopus 로고
    • Identification of a 55-kDa ezrin-related protein that induces cytoskeletal changes and localizes to the nucleolus
    • Kaul, S.C., et al. 1999. Identification of a 55-kDa ezrin-related protein that induces cytoskeletal changes and localizes to the nucleolus. Exp. Cell Res. 250:51-61.
    • (1999) Exp. Cell Res. , vol.250 , pp. 51-61
    • Kaul, S.C.1
  • 29
    • 0033828668 scopus 로고    scopus 로고
    • Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation
    • Wadham, C., Gamble, J.R., Vadas, M.A., and Khew-Goodall, Y. 2000. Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation. J. Cell Sci. 113:3117-3123.
    • (2000) J. Cell Sci. , vol.113 , pp. 3117-3123
    • Wadham, C.1    Gamble, J.R.2    Vadas, M.A.3    Khew-Goodall, Y.4
  • 30
    • 0032854671 scopus 로고    scopus 로고
    • Novel alternatively spliced isoforms of the neurofibromatosis type 2 tumor suppressor are targeted to the nucleus and cytoplasmic granules
    • Schmucker, B., Tang, Y., and Kressel, M. 1999. Novel alternatively spliced isoforms of the neurofibromatosis type 2 tumor suppressor are targeted to the nucleus and cytoplasmic granules. Hum. Mol. Genet. 8:1561-1570.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1561-1570
    • Schmucker, B.1    Tang, Y.2    Kressel, M.3
  • 31
    • 17944372904 scopus 로고    scopus 로고
    • Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility
    • Ng, T., et al. 2001. Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility. EMBO J. 20:2723-2741.
    • (2001) EMBO J. , vol.20 , pp. 2723-2741
    • Ng, T.1
  • 32
    • 0030712860 scopus 로고    scopus 로고
    • ERM (ezrin/radixm/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis
    • Kondo, T., et al. 1997. ERM (ezrin/radixm/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis. J. Cell Biol. 139:749-758.
    • (1997) J. Cell Biol. , vol.139 , pp. 749-758
    • Kondo, T.1
  • 33
    • 0034597013 scopus 로고    scopus 로고
    • CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: A novel regulatory mechanism of the CD95 apoptotic pathway
    • Parlato, S., et al. 2000. CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathway. EMBO J. 19:5123-5134.
    • (2000) EMBO J. , vol.19 , pp. 5123-5134
    • Parlato, S.1
  • 34
    • 0034547198 scopus 로고    scopus 로고
    • Retinoic acid-induced apoptotic pathway in T-cell lymphoma: Identification of four groups of genes with differential biological functions
    • Wang, K.C., Cheng, A.L., Chuang, S.E., Hsu, H.C., and Su, I.J. 2000. Retinoic acid-induced apoptotic pathway in T-cell lymphoma: identification of four groups of genes with differential biological functions. Exp. Hematol. 28:1441-1450.
    • (2000) Exp. Hematol. , vol.28 , pp. 1441-1450
    • Wang, K.C.1    Cheng, A.L.2    Chuang, S.E.3    Hsu, H.C.4    Su, I.J.5
  • 35
    • 0033594950 scopus 로고    scopus 로고
    • Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway
    • Gautreau, A., Poullet, P., Louvard, D., and Arpin, M. 1999. Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway. Proc. Natl. Acad. Sci. U. S. A. 96:7300-7305.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7300-7305
    • Gautreau, A.1    Poullet, P.2    Louvard, D.3    Arpin, M.4
  • 36
    • 0037042180 scopus 로고    scopus 로고
    • Ezrin, a membrane-cytoskeletal linking protein, is highly expressed in atypical endometrial hyperplasia and uterine endometrioid adenocarcinoma
    • Ohtani, K., et al. 2002. Ezrin, a membrane-cytoskeletal linking protein, is highly expressed in atypical endometrial hyperplasia and uterine endometrioid adenocarcinoma. Cancer Lett. 179:79-86.
    • (2002) Cancer Lett. , vol.179 , pp. 79-86
    • Ohtani, K.1
  • 37
    • 0030763919 scopus 로고    scopus 로고
    • Ezrin is an effector of hepatocyte growth factor-mediated migration and morphogenesis in epithelial cells
    • Crepaldi, T., Gautreau, A., Comoglio, P.M., Louvard, D., and Arpin, M. 1997. Ezrin is an effector of hepatocyte growth factor-mediated migration and morphogenesis in epithelial cells. J. Cell Biol. 138:423-434.
    • (1997) J. Cell Biol. , vol.138 , pp. 423-434
    • Crepaldi, T.1    Gautreau, A.2    Comoglio, P.M.3    Louvard, D.4    Arpin, M.5
  • 38
    • 0029830570 scopus 로고    scopus 로고
    • A highly expressed 81 kDa protein in immortalized mouse fibroblast: Its proliferative function and identity with ezrin
    • Kaui, S.C., Mitsui, Y., Komatsu, Y., Reddel, R.R., and Wadhwa, R. 1996. A highly expressed 81 kDa protein in immortalized mouse fibroblast: its proliferative function and identity with ezrin. Oncogene. 13:1231-1237.
    • (1996) Oncogene. , vol.13 , pp. 1231-1237
    • Kaui, S.C.1    Mitsui, Y.2    Komatsu, Y.3    Reddel, R.R.4    Wadhwa, R.5
  • 39
    • 0032830907 scopus 로고    scopus 로고
    • Ezrin regulates cell-cell and cell-matrix adhesion, a possible role with E-cadherin/beta-catenm
    • Hiscox, S., and Jiang, W.G. 1999. Ezrin regulates cell-cell and cell-matrix adhesion, a possible role with E-cadherin/beta-catenm. J. Cell Sci. 112:3081-3090.
    • (1999) J. Cell Sci. , vol.112 , pp. 3081-3090
    • Hiscox, S.1    Jiang, W.G.2
  • 40
    • 0036473018 scopus 로고    scopus 로고
    • Induction of chondrocyte growth arrest by FGF: Transcriptional and cytoskeletal alterations
    • Rozenblatt-Rosen, O., et al. 2002. Induction of chondrocyte growth arrest by FGF: transcriptional and cytoskeletal alterations. J. Cell Sci. 115:553-562.
    • (2002) J. Cell Sci. , vol.115 , pp. 553-562
    • Rozenblatt-Rosen, O.1
  • 41
    • 0032899713 scopus 로고    scopus 로고
    • Increased expression of the NF2 tumor suppressor gene product, merlin, impairs cell motility, adhesion and spreading
    • Gutmann, D.H., et al. 1999. Increased expression of the NF2 tumor suppressor gene product, merlin, impairs cell motility, adhesion and spreading. Hum. Mol. Genet. 8:267-275.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 267-275
    • Gutmann, D.H.1
  • 42
    • 0035029796 scopus 로고    scopus 로고
    • The protein 4.1 tumor suppressor, DAL-1, impairs cell motility, but regulates proliferation in a cell-type-specific fashion
    • Gutmann, D.H., Hirbe, A.C., Huang, Z.Y., and Haipek, C.A. 2001. The protein 4.1 tumor suppressor, DAL-1, impairs cell motility, but regulates proliferation in a cell-type-specific fashion. Neurobiol. Dis. 8:266-278.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 266-278
    • Gutmann, D.H.1    Hirbe, A.C.2    Huang, Z.Y.3    Haipek, C.A.4
  • 43
    • 0035871299 scopus 로고    scopus 로고
    • The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44
    • Morrison, H., et al. 2001. The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44. Genes Dev. 15:968-980.
    • (2001) Genes Dev. , vol.15 , pp. 968-980
    • Morrison, H.1
  • 44
    • 0029569120 scopus 로고
    • Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets
    • Nakamura, F., Amieva, M.R., and Furthmayr, H. 1995. Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets. J. Biol. Chem. 270:31377-31385,
    • (1995) J. Biol. Chem. , vol.270 , pp. 31377-31385
    • Nakamura, F.1    Amieva, M.R.2    Furthmayr, H.3
  • 45
    • 0036171199 scopus 로고    scopus 로고
    • Activation of the PK5/AKT pathway by ICAM-2
    • Perez, O.D., et al. 2002. Activation of the PK5/AKT pathway by ICAM-2. Immunity. 16:51-65.
    • (2002) Immunity , vol.16 , pp. 51-65
    • Perez, O.D.1
  • 46
    • 0345252019 scopus 로고    scopus 로고
    • A novel member of the NF2/ ERM/4.1 superfamily with growth suppressing properties in lung cancer
    • Tran, Y.K., et al. 1999. A novel member of the NF2/ ERM/4.1 superfamily with growth suppressing properties in lung cancer. Cancer Res. 59:35-43.
    • (1999) Cancer Res. , vol.59 , pp. 35-43
    • Tran, Y.K.1
  • 47
    • 0031907484 scopus 로고    scopus 로고
    • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
    • Shaw, R.J., Henry, M., Solomon, F., and Jacks, T. 1998. RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts. Mol. Biol. Cell. 9:403-419.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 403-419
    • Shaw, R.J.1    Henry, M.2    Solomon, F.3    Jacks, T.4
  • 48
    • 0037053360 scopus 로고    scopus 로고
    • RhoA and Rho kinase-dependent phosphorylation of moesin at Thr-558 in hippocampal neuronal cells by glutamate
    • Jeon, S., et al. 2002. RhoA and Rho kinase-dependent phosphorylation of moesin at Thr-558 in hippocampal neuronal cells by glutamate. J. Biol. Chem. 277:16576-16584.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16576-16584
    • Jeon, S.1
  • 49
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and D'Souza-Schorey, C. 1997. Rho GTPases and signaling networks. Genes Dev. 11:2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 50
  • 51
    • 0029861183 scopus 로고    scopus 로고
    • Expression of VEGF receptors in arteries after endothelial injury and lack of increased endothelial regrowth in response to VEGF
    • Lindner, V., and Reidy, M.A. 1996. Expression of VEGF receptors in arteries after endothelial injury and lack of increased endothelial regrowth in response to VEGF. Arterioscler Thromb. Vasc. Biol. 16:1399-1405.
    • (1996) Arterioscler Thromb. Vasc. Biol. , vol.16 , pp. 1399-1405
    • Lindner, V.1    Reidy, M.A.2
  • 52
    • 0029107232 scopus 로고
    • Expression of tumor necrosis factor and accumulation of fibronectin in coronary artery restenosis lesions retrieved by atherectomy
    • Clausell, N., et al. 1995. Expression of tumor necrosis factor and accumulation of fibronectin in coronary artery restenosis lesions retrieved by atherectomy. Br. Heart J. 73:534-539.
    • (1995) Br. Heart J. , vol.73 , pp. 534-539
    • Clausell, N.1
  • 53
    • 0035049575 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of dominant-negative rho-kinase induces a regression of coronary arteriosclerosis in pigs in vivo
    • Morishige, K., et al. 2001. Adenovirus-mediated transfer of dominant-negative rho-kinase induces a regression of coronary arteriosclerosis in pigs in vivo. Arterioscler. Thromb. Vasc. Biol. 21:548-554.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 548-554
    • Morishige, K.1
  • 54
    • 12944289797 scopus 로고    scopus 로고
    • Gene Transfer of dominant negative Rho kinase suppresses neointimal formation after balloon injury in pigs
    • Eco, Y., et al. 2000. Gene Transfer of dominant negative Rho kinase suppresses neointimal formation after balloon injury in pigs. Am. J. Physiol. Heart Circ. Physiol. 278:H1744-H1750.
    • (2000) Am. J. Physiol. Heart Circ. Physiol. , vol.278
    • Eco, Y.1
  • 55
    • 0027393093 scopus 로고
    • Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker
    • Algrain, M., Turunen, O., Vaheri, A., Louvard, D., and Arpin, M. 1993. Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J. Cell Biol. 120:129-139.
    • (1993) J. Cell Biol. , vol.120 , pp. 129-139
    • Algrain, M.1    Turunen, O.2    Vaheri, A.3    Louvard, D.4    Arpin, M.5
  • 56
    • 0033213878 scopus 로고    scopus 로고
    • Tumor gangliosides inhibit the tumor-specific immune response
    • McKallip, R., Li, R., and Ladisch, S. 1999. Tumor gangliosides inhibit the tumor-specific immune response. J. Immunol. 163:3718-3726.
    • (1999) J. Immunol. , vol.163 , pp. 3718-3726
    • McKallip, R.1    Li, R.2    Ladisch, S.3
  • 57
    • 0042266787 scopus 로고    scopus 로고
    • Engineering the response to vascular injury: Divergent effects of deregulated E2F1 expression on vascular smooth muscle cells and endothelial cells result in endothelial recovery and inhibition of neointimal growth
    • Goukassian, D.A., et al. 2003. Engineering the response to vascular injury: divergent effects of deregulated E2F1 expression on vascular smooth muscle cells and endothelial cells result in endothelial recovery and inhibition of neointimal growth. Circ. Res. 93:162-169.
    • (2003) Circ. Res. , vol.93 , pp. 162-169
    • Goukassian, D.A.1
  • 58
    • 0037432293 scopus 로고    scopus 로고
    • Stromal cell-derived factor-1 effects on ex vivo expanded endothelial progenitor cell recruitment for ischemic neovascularization
    • Yamaguchi J., et al. 2003. Stromal cell-derived factor-1 effects on ex vivo expanded endothelial progenitor cell recruitment for ischemic neovascularization. Circulation. 107:1322-1328.
    • (2003) Circulation , vol.107 , pp. 1322-1328
    • Yamaguchi, J.1
  • 59
    • 0034513628 scopus 로고    scopus 로고
    • Multiple downstream signalling pathways from ROCK, a target molecule of Rho small G protein, in reorganization of the actin cytoskeleton in Madin-Darby canine kidney cells
    • Takaishi, K., Matozaki, T., Nakano, K., and Takai, Y. 2000. Multiple downstream signalling pathways from ROCK, a target molecule of Rho small G protein, in reorganization of the actin cytoskeleton in Madin-Darby canine kidney cells. Genes Cells. 5:929-936.
    • (2000) Genes Cells. , vol.5 , pp. 929-936
    • Takaishi, K.1    Matozaki, T.2    Nakano, K.3    Takai, Y.4


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