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Volumn 1746, Issue 1, 2005, Pages 28-37

RGDS and DGEA-induced [Ca2+]i signalling in human dermal fibroblasts

Author keywords

Ca2+ signalling; DGEA; Fibroblast; Integrin; RGDS

Indexed keywords

ARGINYLGLYCYLASPARTYLSERINE; ASPARTYLGLYCYLGLUTAMYLALANINE; CALCIUM; INOSITOL TRISPHOSPHATE; INTEGRIN; PEPTIDE DERIVATIVE; PHOSPHATASE; PHOSPHOLIPASE C; PROTEIN TYROSINE KINASE; TRYPSIN; UNCLASSIFIED DRUG;

EID: 26944450904     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2005.07.004     Document Type: Article
Times cited : (15)

References (58)
  • 1
    • 0027397549 scopus 로고
    • Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium
    • M.A. Schwartz Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium J. Cell Biol. 120 1993 1003 1020
    • (1993) J. Cell Biol. , vol.120 , pp. 1003-1020
    • Schwartz, M.A.1
  • 2
    • 0031740739 scopus 로고    scopus 로고
    • Cell interactions with collagen matrices in vivo and in vitro depend on phosphatidylinositol 3-kinase and free cytoplasmic calcium
    • K. Ahlen, A. Berg, F. Stiger, A. Tengholm, A. Siegbahn, E. Gylfe, R.K. Reed, and K. Rubin Cell interactions with collagen matrices in vivo and in vitro depend on phosphatidylinositol 3-kinase and free cytoplasmic calcium Cell Adhes. Commun. 5 1998 461 473
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 461-473
    • Ahlen, K.1    Berg, A.2    Stiger, F.3    Tengholm, A.4    Siegbahn, A.5    Gylfe, E.6    Reed, R.K.7    Rubin, K.8
  • 3
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • M.D. Pierschbacher, and E. Ruoslahti Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule Nature 309 1984 30 33
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 4
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • E. Ruoslahti RGD and other recognition sequences for integrins Annu. Rev. Cell Dev. Biol. 12 1996 697 715
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 5
    • 0031025120 scopus 로고    scopus 로고
    • Integrin-mediated calcium signalling and regulation of cell adhesion by intracellular calcium
    • M.D. Sjaastad, and W.J. Nelson Integrin-mediated calcium signalling and regulation of cell adhesion by intracellular calcium BioEssays 19 1997 47 55
    • (1997) BioEssays , vol.19 , pp. 47-55
    • Sjaastad, M.D.1    Nelson, W.J.2
  • 6
    • 0026782146 scopus 로고
    • Analysis of α1β1, α2β1 and α3β1 integrins in cell-collagen interactions: Identification of conformation dependent α1β1 binding sites in collagen type I
    • D. Gullberg, K.R. Gehlen, D.C. Turner, K. Ahlen, L.S. Zijenah, M.J. Barnes, and K. Rubin Analysis of α1β1, α2β1 and α3β1 integrins in cell-collagen interactions: identification of conformation dependent α1β1 binding sites in collagen type I EMBO J. 11 1992 3865 3873
    • (1992) EMBO J. , vol.11 , pp. 3865-3873
    • Gullberg, D.1    Gehlen, K.R.2    Turner, D.C.3    Ahlen, K.4    Zijenah, L.S.5    Barnes, M.J.6    Rubin, K.7
  • 7
    • 0023555151 scopus 로고
    • Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cells possessing unique alpha and common beta subunits
    • E.A. Wayner, and W.G. Carter Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cells possessing unique alpha and common beta subunits J. Cell Biol. 105 1987 1873 1884
    • (1987) J. Cell Biol. , vol.105 , pp. 1873-1884
    • Wayner, E.A.1    Carter, W.G.2
  • 8
    • 0024542439 scopus 로고
    • Identification of integrin collagen receptors on human melanoma cells
    • R.H. Kramer, and N. Marks Identification of integrin collagen receptors on human melanoma cells J. Biol. Chem. 264 1989 4684 4688
    • (1989) J. Biol. Chem. , vol.264 , pp. 4684-4688
    • Kramer, R.H.1    Marks, N.2
  • 9
    • 0033520330 scopus 로고    scopus 로고
    • CDNA cloning and chromosomal localization of human alpha(11) integrin. a collagen-binding I domain-containing beta(1)-associated integrin alpha-chain present in muscle tissues
    • T. Velling, M. Kusche-Gulberg, T. Sejersen, and D. Gullberg cDNA cloning and chromosomal localization of human alpha(11) integrin. A collagen-binding I domain-containing beta(1)-associated integrin alpha-chain present in muscle tissues J. Biol. Chem. 274 1999 25735 25742
    • (1999) J. Biol. Chem. , vol.274 , pp. 25735-25742
    • Velling, T.1    Kusche-Gulberg, M.2    Sejersen, T.3    Gullberg, D.4
  • 10
    • 0034614620 scopus 로고    scopus 로고
    • The collagen-binding A-domains of integrins alpha(1)beta(1) and alpha(2)beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens
    • C.G. Knight, L.F. Morton, A.R. Peachey, D.S. Tuckwell, R.W. Farndale, and M.J. Barnes The collagen-binding A-domains of integrins alpha(1)beta(1) and alpha(2)beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens J. Biol. Chem. 275 2000 35 40
    • (2000) J. Biol. Chem. , vol.275 , pp. 35-40
    • Knight, C.G.1    Morton, L.F.2    Peachey, A.R.3    Tuckwell, D.S.4    Farndale, R.W.5    Barnes, M.J.6
  • 13
    • 0025823208 scopus 로고
    • Identification of a tetrapeptide recognition sequence for the alpha 2 beta 1 integrin in collagen
    • W.D. Staatz, K.F. Fok, M.M. Zutter, S.P. Adams, B.A. Rodriguez, and S.A. Santoro Identification of a tetrapeptide recognition sequence for the alpha 2 beta 1 integrin in collagen J. Biol. Chem. 266 1991 7363 7367
    • (1991) J. Biol. Chem. , vol.266 , pp. 7363-7367
    • Staatz, W.D.1    Fok, K.F.2    Zutter, M.M.3    Adams, S.P.4    Rodriguez, B.A.5    Santoro, S.A.6
  • 14
    • 0030022560 scopus 로고    scopus 로고
    • Differentiation and cell surface expression of transforming growth factor-β receptors are regulated by interaction with matrix collagen in murine osteoblastic cells
    • Y. Takeuchi, K. Nakayama, and T. Matsumoto Differentiation and cell surface expression of transforming growth factor-β receptors are regulated by interaction with matrix collagen in murine osteoblastic cells J. Biol. Chem. 271 1996 3938 3944
    • (1996) J. Biol. Chem. , vol.271 , pp. 3938-3944
    • Takeuchi, Y.1    Nakayama, K.2    Matsumoto, T.3
  • 15
    • 0032412030 scopus 로고    scopus 로고
    • Induction of cellular processes containing collagenase and retinoid by integrin-binding to interstitial collagen in hepatic stellate cell culture
    • M. Sato, N. Kojima, M. Miura, K. Imai, and H. Senoo Induction of cellular processes containing collagenase and retinoid by integrin-binding to interstitial collagen in hepatic stellate cell culture Cell Biol. Int. 22 1998 115 125
    • (1998) Cell Biol. Int. , vol.22 , pp. 115-125
    • Sato, M.1    Kojima, N.2    Miura, M.3    Imai, K.4    Senoo, H.5
  • 16
    • 0032483809 scopus 로고    scopus 로고
    • Role of the α2-integrin in osteoblast-specific gene expression and activation of the Osf2 transcription factor
    • G. Xiao, D. Wang, M.D. Benson, G. Karsenty, and R.T. Franceschi Role of the α2-integrin in osteoblast-specific gene expression and activation of the Osf2 transcription factor J. Biol. Chem. 273 1998 32988 32994
    • (1998) J. Biol. Chem. , vol.273 , pp. 32988-32994
    • Xiao, G.1    Wang, D.2    Benson, M.D.3    Karsenty, G.4    Franceschi, R.T.5
  • 17
    • 0033919703 scopus 로고    scopus 로고
    • Type I collagen-induced osteoblastic differentiation of bone-marrow cells mediated by collagen α2β1 integrin interaction
    • M. Mizuno, R. Fujisawa, and Y. Kuboki Type I collagen-induced osteoblastic differentiation of bone-marrow cells mediated by collagen α2β1 integrin interaction J. Cell. Phys. 184 2000 207 213
    • (2000) J. Cell. Phys. , vol.184 , pp. 207-213
    • Mizuno, M.1    Fujisawa, R.2    Kuboki, Y.3
  • 18
    • 0034069043 scopus 로고    scopus 로고
    • Establishment and characterization of a human gastric carcinoma cell line that is highly metastatic to lymph nodes
    • K. Yamaguchi, H. Ura, T. Yasoshima, T. Shishido, R. Denno, and K. Hirata Establishment and characterization of a human gastric carcinoma cell line that is highly metastatic to lymph nodes J. Exp. Clin. Cancer Res. 19 2000 113 120
    • (2000) J. Exp. Clin. Cancer Res. , vol.19 , pp. 113-120
    • Yamaguchi, K.1    Ura, H.2    Yasoshima, T.3    Shishido, T.4    Denno, R.5    Hirata, K.6
  • 19
    • 0035122328 scopus 로고    scopus 로고
    • Osteoblast-related gene expression of bone marrow cells during the osteoblastic differentiation induced by type I collagen
    • M. Mizuno, and Y. Kuboki Osteoblast-related gene expression of bone marrow cells during the osteoblastic differentiation induced by type I collagen J. Biochem. 129 2001 133 138
    • (2001) J. Biochem. , vol.129 , pp. 133-138
    • Mizuno, M.1    Kuboki, Y.2
  • 20
    • 0031282464 scopus 로고    scopus 로고
    • A collagen peptide motif activates tyrosine kinase-dependent calcium signalling pathways in human osteoblast-like cells
    • T.J. McCann, W.T. Mason, M.C. Meikle, and F. McDonald A collagen peptide motif activates tyrosine kinase-dependent calcium signalling pathways in human osteoblast-like cells Matrix Biol. 16 1997 273 283
    • (1997) Matrix Biol. , vol.16 , pp. 273-283
    • McCann, T.J.1    Mason, W.T.2    Meikle, M.C.3    McDonald, F.4
  • 23
    • 0037096430 scopus 로고    scopus 로고
    • The neural cell adhesion molecule L1 potentiates integrin-dependent cell migration to extracellular matrix proteins
    • K. Thelen, V. Kedar, A.K. Panicker, R.S. Schmid, B.R. Midkiff, and P.F. Maness The neural cell adhesion molecule L1 potentiates integrin-dependent cell migration to extracellular matrix proteins J. Neurosci. 22 2002 4918 4931
    • (2002) J. Neurosci. , vol.22 , pp. 4918-4931
    • Thelen, K.1    Kedar, V.2    Panicker, A.K.3    Schmid, R.S.4    Midkiff, B.R.5    Maness, P.F.6
  • 25
    • 0025992778 scopus 로고
    • Measurement of mechanical forces generated by skin fibroblasts embedded in a three-dimensional collagen gel
    • P. Delvoye, P. Wiliquet, J.L. Leveque, B.V. Nusgens, and Ch.M. Lapière Measurement of mechanical forces generated by skin fibroblasts embedded in a three-dimensional collagen gel J. Invest. Dermatol. 97 1991 898 902
    • (1991) J. Invest. Dermatol. , vol.97 , pp. 898-902
    • Delvoye, P.1    Wiliquet, P.2    Leveque, J.L.3    Nusgens, B.V.4    Lapière, Ch.M.5
  • 26
    • 0021099233 scopus 로고
    • Domain structure of the carboxyl-terminal half of human plasma fibronectin
    • M. Hayashi, and K.M. Yamada Domain structure of the carboxyl-terminal half of human plasma fibronectin J. Biol. Chem. 258 1983 3332 3340
    • (1983) J. Biol. Chem. , vol.258 , pp. 3332-3340
    • Hayashi, M.1    Yamada, K.M.2
  • 27
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assay
    • T. Mosmann Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assay J. Immunol. Methods 65 1983 55 63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 28
    • 0032483327 scopus 로고    scopus 로고
    • An interleukin-1 loop is induced in human skin fibroblasts upon stress relaxation in a three-dimensional collagen gel but is not involved in the up-regulation of matrix metalloproteinase 1
    • C. Lambert, C. Lapière, and B. Nusgens An interleukin-1 loop is induced in human skin fibroblasts upon stress relaxation in a three-dimensional collagen gel but is not involved in the up-regulation of matrix metalloproteinase 1 J. Biol. Chem. 273 1998 23143 23149
    • (1998) J. Biol. Chem. , vol.273 , pp. 23143-23149
    • Lambert, C.1    Lapière, C.2    Nusgens, B.3
  • 29
    • 0024391789 scopus 로고
    • Photochemically generated cytosolic calcium pulses and their detection by fluo-3
    • J.P. Kao, A.T. Harootunian, and R.Y. Tsien Photochemically generated cytosolic calcium pulses and their detection by fluo-3 J. Biol. Chem. 264 1989 8179 8184
    • (1989) J. Biol. Chem. , vol.264 , pp. 8179-8184
    • Kao, J.P.1    Harootunian, A.T.2    Tsien, R.Y.3
  • 30
    • 0025332577 scopus 로고
    • Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase
    • O. Tharstrüp, P.J. Cullen, B.K. Drobak, M.R. Hanley, and A.P. Dawson Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase Proc. Natl. Acad. Sci. U. S. A. 87 1990 2466 2470
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 2466-2470
    • Tharstrüp, O.1    Cullen, P.J.2    Drobak, B.K.3    Hanley, M.R.4    Dawson, A.P.5
  • 31
    • 0030964614 scopus 로고    scopus 로고
    • Xestospongins: Potent membrane permeable blockers of the inositol 1,4,5-triposphate receptor
    • J. Gafni, J.A. Munsch, T.H. Lam, M.C. Catlin, L.G. Costa, T.G. Molinski, and I.N. Pessah Xestospongins: potent membrane permeable blockers of the inositol 1,4,5-triposphate receptor Cell 19 1997 723 733
    • (1997) Cell , vol.19 , pp. 723-733
    • Gafni, J.1    Munsch, J.A.2    Lam, T.H.3    Catlin, M.C.4    Costa, L.G.5    Molinski, T.G.6    Pessah, I.N.7
  • 32
    • 0035030795 scopus 로고    scopus 로고
    • Intracellular Ca(2+) signaling in endothelial cells by the angiogenesis inhibitors endostatin and angiostatin
    • L. Jiang, V. Jha, M. Dhanabal, V.P. Sukhatme, and S.L. Alper Intracellular Ca(2+) signaling in endothelial cells by the angiogenesis inhibitors endostatin and angiostatin Am. J. Physiol.: Cell Physiol. 280 2001 C1140 C1150
    • (2001) Am. J. Physiol.: Cell Physiol. , vol.280
    • Jiang, L.1    Jha, V.2    Dhanabal, M.3    Sukhatme, V.P.4    Alper, S.L.5
  • 33
    • 0027173096 scopus 로고
    • Integrin receptor-mediated mobilisation of intracellular calcium in rat osteoclasts
    • G. Shankar, I. Davison, M.H. Helfrich, W.T. Mason, and M.A. Horton Integrin receptor-mediated mobilisation of intracellular calcium in rat osteoclasts J. Cell Sci. 105 1993 61 68
    • (1993) J. Cell Sci. , vol.105 , pp. 61-68
    • Shankar, G.1    Davison, I.2    Helfrich, M.H.3    Mason, W.T.4    Horton, M.A.5
  • 35
    • 0038642118 scopus 로고    scopus 로고
    • Cell spreading controls endoplasmic and nuclear calcium: A physical gene regulation pathway from the cell surface to the nucleus
    • N. Itano, S. Okamoto, D. Zhang, S.A. Lipton, and E. Ruoslahti Cell spreading controls endoplasmic and nuclear calcium: a physical gene regulation pathway from the cell surface to the nucleus Proc. Natl. Acad. Sci. U. S. A. 100 2003 5181 5186
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5181-5186
    • Itano, N.1    Okamoto, S.2    Zhang, D.3    Lipton, S.A.4    Ruoslahti, E.5
  • 36
    • 0028179351 scopus 로고
    • Alpha v integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion
    • M.A. Schwartz, and K. Denninghoff Alpha v integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion J. Biol. Chem. 269 1994 11133 11137
    • (1994) J. Biol. Chem. , vol.269 , pp. 11133-11137
    • Schwartz, M.A.1    Denninghoff, K.2
  • 37
    • 0028786699 scopus 로고
    • Thrombospondin mediates calcium mobilization in fibroblasts via its Arg-Gly-Asp and carboxyl-terminal domains
    • P.W. Tsao, and S.A. Mousa Thrombospondin mediates calcium mobilization in fibroblasts via its Arg-Gly-Asp and carboxyl-terminal domains J. Biol. Chem. 270 1995 23747 23753
    • (1995) J. Biol. Chem. , vol.270 , pp. 23747-23753
    • Tsao, P.W.1    Mousa, S.A.2
  • 38
    • 0028050975 scopus 로고
    • Soluble alpha v beta 3-integrin ligands raise [Ca2+]i in rat osteoclasts and mouse-derived osteoclast-like cells
    • Z. Zimolo, G. Wesolowski, H. Tanaka, J.L. Hyman, J.R. Hoyer, and G.A. Rodan Soluble alpha v beta 3-integrin ligands raise [Ca2+]i in rat osteoclasts and mouse-derived osteoclast-like cells Am. J. Physiol. 266 1994 C376 C381
    • (1994) Am. J. Physiol. , vol.266
    • Zimolo, Z.1    Wesolowski, G.2    Tanaka, H.3    Hyman, J.L.4    Hoyer, J.R.5    Rodan, G.A.6
  • 39
    • 0027965069 scopus 로고
    • Feedback regulation of cell-substratum adhesion by integrin-mediated intracellular Ca2+ signalling
    • M.D. Sjaastad, B. Angres, R.S. Lewis, and W.J. Nelson Feedback regulation of cell-substratum adhesion by integrin-mediated intracellular Ca2+ signalling Proc. Natl. Acad. Sci. U. S. A. 91 1994 8214 8218
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 8214-8218
    • Sjaastad, M.D.1    Angres, B.2    Lewis, R.S.3    Nelson, W.J.4
  • 42
    • 0028170665 scopus 로고
    • Smoothly graded Ca2+ release from inositol 1,4,5-trisphosphate-sensitive Ca2+ stores
    • M.D. Bootman, T.R. Cheek, R.B. Moreton, D.L. Bennett, and M.J. Berridge Smoothly graded Ca2+ release from inositol 1,4,5-trisphosphate-sensitive Ca2+ stores J. Biol. Chem. 269 1994 24783 24791
    • (1994) J. Biol. Chem. , vol.269 , pp. 24783-24791
    • Bootman, M.D.1    Cheek, T.R.2    Moreton, R.B.3    Bennett, D.L.4    Berridge, M.J.5
  • 44
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism
    • W.T. Arthur, L.A. Petch, and K. Burridge Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism Curr. Biol. 10 2000 719 722
    • (2000) Curr. Biol. , vol.10 , pp. 719-722
    • Arthur, W.T.1    Petch, L.A.2    Burridge, K.3
  • 45
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • K.M. Yamada, and B. Geiger Molecular interactions in cell adhesion complexes Curr. Opin. Cell Biol. 9 1997 76 85
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2
  • 46
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • A. Hall Rho GTPases and the actin cytoskeleton Science 279 1998 509 514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 47
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases
    • N.A. Hotchin, and A. Hall The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases J. Cell Biol. 131 1995 1857 1865
    • (1995) J. Cell Biol. , vol.131 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 50
    • 0025887362 scopus 로고
    • Epiligrin, a new cell adhesion ligand for integrin alpha 3 beta 1 in epithelial basement membranes
    • W.G. Carter, M.C. Ryan, and P.J. Gahr Epiligrin, a new cell adhesion ligand for integrin alpha 3 beta 1 in epithelial basement membranes Cell 65 1991 599 610
    • (1991) Cell , vol.65 , pp. 599-610
    • Carter, W.G.1    Ryan, M.C.2    Gahr, P.J.3
  • 51
    • 0026725843 scopus 로고
    • The receptor for the basement membrane glycoprotein entactin is the integrin alpha3/beta1
    • S. Dedhar, K. Jewell, M. Rojiani, and V. Gray The receptor for the basement membrane glycoprotein entactin is the integrin alpha3/beta1 J. Biol. Chem. 267 1992 18908 18914
    • (1992) J. Biol. Chem. , vol.267 , pp. 18908-18914
    • Dedhar, S.1    Jewell, K.2    Rojiani, M.3    Gray, V.4
  • 52
    • 0033588298 scopus 로고    scopus 로고
    • Identification of an alpha(3)beta(1) integrin recognition sequence in thrombospondin-1
    • H.C. Krutzsch, B.J. Choe, J.M. Sipes, N.H. Guo, and D.D. Roberts Identification of an alpha(3)beta(1) integrin recognition sequence in thrombospondin-1 J. Biol. Chem. 274 1999 24080 24086
    • (1999) J. Biol. Chem. , vol.274 , pp. 24080-24086
    • Krutzsch, H.C.1    Choe, B.J.2    Sipes, J.M.3    Guo, N.H.4    Roberts, D.D.5
  • 53
    • 0036008473 scopus 로고    scopus 로고
    • Integrin α3β1 (CD49c/29) is a cellular receptor for Kaposi's sarcoma-associated herpesvirus (KSHV/HHV-8) entry into the target cells
    • S.M. Akula, N.P. Pramod, F.Z. Wang, and B. Chandran Integrin α3β1 (CD49c/29) is a cellular receptor for Kaposi's sarcoma-associated herpesvirus (KSHV/HHV-8) entry into the target cells Cell 108 2002 407 419
    • (2002) Cell , vol.108 , pp. 407-419
    • Akula, S.M.1    Pramod, N.P.2    Wang, F.Z.3    Chandran, B.4
  • 54
    • 0031850240 scopus 로고    scopus 로고
    • The cytoskeleton and cell signalling: Component localization and mechanical coupling
    • P.A. Janmey The cytoskeleton and cell signalling: component localization and mechanical coupling Physiol. Rev. 78 1998 763 781
    • (1998) Physiol. Rev. , vol.78 , pp. 763-781
    • Janmey, P.A.1
  • 55
    • 0026596337 scopus 로고
    • Distinct cellular functions mediated by different VLA integrin alpha subunit cytoplasmic domains
    • B.M. Chan, P.D. Kassner, J.A. Schiro, H.R. Byers, T.S. Kupper, and M.E. Hemler Distinct cellular functions mediated by different VLA integrin alpha subunit cytoplasmic domains Cell 68 1992 1051 1060
    • (1992) Cell , vol.68 , pp. 1051-1060
    • Chan, B.M.1    Kassner, P.D.2    Schiro, J.A.3    Byers, H.R.4    Kupper, T.S.5    Hemler, M.E.6
  • 57
    • 0034256024 scopus 로고    scopus 로고
    • Signalling networks linking integrins and Rho family GTPases
    • M.A. Schwartz, and S.J. Shattil Signalling networks linking integrins and Rho family GTPases TIBS 25 2000 388 391
    • (2000) TIBS , vol.25 , pp. 388-391
    • Schwartz, M.A.1    Shattil, S.J.2
  • 58
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • R. Visse, and H. Nagase Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry Circ. Res. 92 2003 827 839
    • (2003) Circ. Res. , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2


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