메뉴 건너뛰기




Volumn 48, Issue 3, 2007, Pages 1061-1071

Inhibition of human corneal epithelial production of fibrotic mediator TGF-β2 by basement membrane-like extracellular matrix

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN TYPE 4; EZRIN; GROWTH FACTOR; LAMININ; MATRIGEL; MESSENGER RNA; MOESIN; RADIXIN; SMAD3 PROTEIN; TRANSFORMING GROWTH FACTOR BETA2; BIOMATERIAL; COLLAGEN; CYTOSKELETON PROTEIN; PROTEOGLYCAN;

EID: 34047246332     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.06-0772     Document Type: Article
Times cited : (15)

References (56)
  • 1
    • 0017695640 scopus 로고
    • Regeneration of corneal tissue
    • Cintron C, Kublin CL. Regeneration of corneal tissue. Dev Biol. 1977;61:346-357.
    • (1977) Dev Biol , vol.61 , pp. 346-357
    • Cintron, C.1    Kublin, C.L.2
  • 2
    • 0033024366 scopus 로고    scopus 로고
    • Keratocyte and fibroblast phenotypes in the repairing cornea
    • Fini ME. Keratocyte and fibroblast phenotypes in the repairing cornea. Prog Retin Eye Res. 1999;18:529-551.
    • (1999) Prog Retin Eye Res , vol.18 , pp. 529-551
    • Fini, M.E.1
  • 3
    • 0027955331 scopus 로고
    • Fibroblasts, myofibroblasts, and wound contraction
    • Grinnell F. Fibroblasts, myofibroblasts, and wound contraction. J Cell Biol. 1994;124:401-404.
    • (1994) J Cell Biol , vol.124 , pp. 401-404
    • Grinnell, F.1
  • 4
    • 0002490354 scopus 로고
    • Oxford, UK: Blackwell Scientific Publications;
    • Weimar V. Healing Processes in the Cornea. Oxford, UK: Blackwell Scientific Publications; 1960:111-124.
    • (1960) Healing Processes in the Cornea , pp. 111-124
    • Weimar, V.1
  • 5
    • 2542505844 scopus 로고    scopus 로고
    • Scar-free healing: From embryonic mechanisms to adult therapeutic intervention
    • Ferguson MW, O'Kane S. Scar-free healing: from embryonic mechanisms to adult therapeutic intervention. Philos Trans R Soc Lond B Biol Sci. 2004;359:839-850.
    • (2004) Philos Trans R Soc Lond B Biol Sci , vol.359 , pp. 839-850
    • Ferguson, M.W.1    O'Kane, S.2
  • 7
    • 0030934532 scopus 로고    scopus 로고
    • Wound healing: Aiming for perfect skin regeneration
    • Martin P. Wound healing: aiming for perfect skin regeneration. Science. 1997;276:75-81.
    • (1997) Science , vol.276 , pp. 75-81
    • Martin, P.1
  • 8
    • 0031595120 scopus 로고    scopus 로고
    • Neutralizing antibody to TGFβ modulates stromal fibrosis but not regression of photoablative effect following PRK
    • Møller-Pedersen T, Cavanagh HD, Petroll WM, Jester JV. Neutralizing antibody to TGFβ modulates stromal fibrosis but not regression of photoablative effect following PRK. Curr Eye Res. 1998;17:736-747.
    • (1998) Curr Eye Res , vol.17 , pp. 736-747
    • Møller-Pedersen, T.1    Cavanagh, H.D.2    Petroll, W.M.3    Jester, J.V.4
  • 9
    • 0033517356 scopus 로고    scopus 로고
    • Cutaneous wound healing
    • Singer AJ, Clark RA. Cutaneous wound healing. N Engl J Med. 1999;341:738-746.
    • (1999) N Engl J Med , vol.341 , pp. 738-746
    • Singer, A.J.1    Clark, R.A.2
  • 10
    • 0034928852 scopus 로고    scopus 로고
    • The corneal wound healing response: Cytokine-mediated interaction of the epithelium, stroma, and inflammatory cells
    • Wilson SE, Mohan RR, Mohan RR, Ambrosio R Jr, Hong J, Lee J. The corneal wound healing response: cytokine-mediated interaction of the epithelium, stroma, and inflammatory cells. Prog Retin Eye Res. 2001;20:625-637.
    • (2001) Prog Retin Eye Res , vol.20 , pp. 625-637
    • Wilson, S.E.1    Mohan, R.R.2    Mohan, R.R.3    Ambrosio Jr, R.4    Hong, J.5    Lee, J.6
  • 11
    • 28044450903 scopus 로고    scopus 로고
    • How the cornea heals: Cornea-specific repair mechanisms impacting on surgical outcomes
    • Fini ME, Stramer BM. How the cornea heals: cornea-specific repair mechanisms impacting on surgical outcomes. Cornea. 2005;24(suppl 8):S2-S11.
    • (2005) Cornea , vol.24 , Issue.SUPPL. 8
    • Fini, M.E.1    Stramer, B.M.2
  • 12
    • 0141542547 scopus 로고    scopus 로고
    • Molecular mechanisms controlling the fibrotic repair phenotype in cornea: Implications for surgical outcomes
    • Stramer BM, Zieske JD, Jung JC, Austin JS, Fini ME. Molecular mechanisms controlling the fibrotic repair phenotype in cornea: implications for surgical outcomes. Invest Ophthalmol Vis Sci. 2003;44:4237-4246.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 4237-4246
    • Stramer, B.M.1    Zieske, J.D.2    Jung, J.C.3    Austin, J.S.4    Fini, M.E.5
  • 13
    • 6944224594 scopus 로고    scopus 로고
    • Growth factors in the anterior segment: Role in tissue maintenance, wound healing and ocular pathology
    • Klenkler B, Sheardown H. Growth factors in the anterior segment: role in tissue maintenance, wound healing and ocular pathology. Exp Eye Res. 2004;79:677-688.
    • (2004) Exp Eye Res , vol.79 , pp. 677-688
    • Klenkler, B.1    Sheardown, H.2
  • 14
    • 0028816424 scopus 로고
    • A corneal epithelial inhibitor of stromal cell collagenase synthesis identified as TGF-β2
    • Strissel KJ, Rinehart WB, Fini ME. A corneal epithelial inhibitor of stromal cell collagenase synthesis identified as TGF-β2. Invest Ophthalmol Vis Sci. 1995;36:151-162.
    • (1995) Invest Ophthalmol Vis Sci , vol.36 , pp. 151-162
    • Strissel, K.J.1    Rinehart, W.B.2    Fini, M.E.3
  • 15
    • 0031045650 scopus 로고    scopus 로고
    • Regulation of paracrine cytokine balance controlling collagenase synthesis by corneal cells
    • Strissel KJ, Rinehart WB, Fini ME. Regulation of paracrine cytokine balance controlling collagenase synthesis by corneal cells. Invest Ophthalmol Vis Sci. 1997;38:546-552.
    • (1997) Invest Ophthalmol Vis Sci , vol.38 , pp. 546-552
    • Strissel, K.J.1    Rinehart, W.B.2    Fini, M.E.3
  • 16
    • 0041342109 scopus 로고    scopus 로고
    • Evaluation of anti-TGF-β2 antibody as a new postoperative anti-scarring agent in glaucoma surgery
    • Mead AL, Wong TT, Cordeiro MF, Anderson IK, Khaw PT. Evaluation of anti-TGF-β2 antibody as a new postoperative anti-scarring agent in glaucoma surgery. Invest Ophthalmol Vis Sci. 2003;44:3394-3401.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 3394-3401
    • Mead, A.L.1    Wong, T.T.2    Cordeiro, M.F.3    Anderson, I.K.4    Khaw, P.T.5
  • 17
    • 14744269357 scopus 로고    scopus 로고
    • Selective reduction of fibrotic markers in repairing corneas of mice deficient in Smad3
    • Stramer BM, Austin JS, Roberts AB, Fini ME. Selective reduction of fibrotic markers in repairing corneas of mice deficient in Smad3. J Cell Physiol. 2005;203:226-232.
    • (2005) J Cell Physiol , vol.203 , pp. 226-232
    • Stramer, B.M.1    Austin, J.S.2    Roberts, A.B.3    Fini, M.E.4
  • 18
    • 0004191881 scopus 로고    scopus 로고
    • Regulation of MMP-9 activity in human tear fluid and corneal epithelial culture supernatant
    • Sobrin L, Liu Z, Monroy DC, et al. Regulation of MMP-9 activity in human tear fluid and corneal epithelial culture supernatant. Invest Ophthalmol Vis Sci. 2000;41:1703-1709.
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 1703-1709
    • Sobrin, L.1    Liu, Z.2    Monroy, D.C.3
  • 19
    • 0027165848 scopus 로고
    • Serum differentially modulates the clonal growth and differentiation of cultured limbal and corneal epithelium
    • Kruse FE, Tseng SC. Serum differentially modulates the clonal growth and differentiation of cultured limbal and corneal epithelium. Invest Ophthalmol Vis Sci. 1993;34:2976-2989.
    • (1993) Invest Ophthalmol Vis Sci , vol.34 , pp. 2976-2989
    • Kruse, F.E.1    Tseng, S.C.2
  • 20
    • 0025314312 scopus 로고
    • Epidermal growth factor or transforming growth factor alpha is required for kidney tubulogenesis in matrigel cultures in serum-free medium
    • Taub M, Wang Y, Szczesny TM, Kleinman HK. Epidermal growth factor or transforming growth factor alpha is required for kidney tubulogenesis in matrigel cultures in serum-free medium. Proc Natl Acad Sci USA. 1990;87:4002-4006.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4002-4006
    • Taub, M.1    Wang, Y.2    Szczesny, T.M.3    Kleinman, H.K.4
  • 21
    • 33745520093 scopus 로고    scopus 로고
    • Three-dimensional nanofibrillar surfaces covalently modified with tenascin-C-derived peptides enhance neuronal growth in vitro
    • Ahmed I, Liu HY, Mamiya PC, et al. Three-dimensional nanofibrillar surfaces covalently modified with tenascin-C-derived peptides enhance neuronal growth in vitro. J Biomed Mater Res A. 2006;76:851-860.
    • (2006) J Biomed Mater Res A , vol.76 , pp. 851-860
    • Ahmed, I.1    Liu, H.Y.2    Mamiya, P.C.3
  • 22
    • 0025917034 scopus 로고
    • Molecular cloning and structure of the human transforming growth factor-β2 gene promoter
    • Noma T, Glick AB, Geiser AG, et al. Molecular cloning and structure of the human transforming growth factor-β2 gene promoter. Growth Factors. 1991;4:247-255.
    • (1991) Growth Factors , vol.4 , pp. 247-255
    • Noma, T.1    Glick, A.B.2    Geiser, A.G.3
  • 23
    • 0028910192 scopus 로고
    • Inactive type II and type I receptors for TGFβ are dominant inhibitors of TGFβ-dependent transcription
    • Brand T, Schneider MD. Inactive type II and type I receptors for TGFβ are dominant inhibitors of TGFβ-dependent transcription. J Biol Chem. 1995;270:8274-8284.
    • (1995) J Biol Chem , vol.270 , pp. 8274-8284
    • Brand, T.1    Schneider, M.D.2
  • 24
    • 0024592174 scopus 로고
    • Expression of transforming growth factor-β in wound healing of vitamin A-deficient rat corneas
    • Hayashi K, Frangieh G, Wolf G, Kenyon KR. Expression of transforming growth factor-β in wound healing of vitamin A-deficient rat corneas. Invest Ophthalmol Vis Sci. 1989;30:239-247.
    • (1989) Invest Ophthalmol Vis Sci , vol.30 , pp. 239-247
    • Hayashi, K.1    Frangieh, G.2    Wolf, G.3    Kenyon, K.R.4
  • 25
    • 0028900002 scopus 로고
    • Three patterns of cytokine expression potentially involved in epithelial-fibroblast interactions of human ocular surface
    • Li DQ, Tseng SC. Three patterns of cytokine expression potentially involved in epithelial-fibroblast interactions of human ocular surface. J Cell Physiol. 1995;163:61-79.
    • (1995) J Cell Physiol , vol.163 , pp. 61-79
    • Li, D.Q.1    Tseng, S.C.2
  • 28
    • 0026594456 scopus 로고
    • EGF receptor, basic FGF, TGF β-1, and IL-1 alpha mRNA in human corneal epithelial cells and stromal fibroblasts
    • Wilson SE, He YG, Lloyd SA. EGF, EGF receptor, basic FGF, TGF β-1, and IL-1 alpha mRNA in human corneal epithelial cells and stromal fibroblasts. Invest Ophthalmol Vis Sci. 1992;33:1756-1765.
    • (1992) Invest Ophthalmol Vis Sci , vol.33 , pp. 1756-1765
    • Wilson, S.E.1    He, Y.G.2    Lloyd, S.E.3
  • 29
    • 0026752729 scopus 로고
    • EGF, basic FGF, and TGF β-1 messenger RNA production in rabbit corneal epithelial cells
    • Wilson SE, Lloyd SA, He YG. EGF, basic FGF, and TGF β-1 messenger RNA production in rabbit corneal epithelial cells. Invest Ophthalmol Vis Sci. 1992;33:1987-1995.
    • (1992) Invest Ophthalmol Vis Sci , vol.33 , pp. 1987-1995
    • Wilson, S.E.1    Lloyd, S.A.2    He, Y.G.3
  • 30
    • 0028136394 scopus 로고
    • Epidermal growth factor, transforming growth factor alpha, transforming growth factor β, acidic fibroblast growth factor, basic fibroblast growth factor, and interleukin-1 proteins in the cornea
    • Wilson SE, Schultz GS, Chegini N, Weng J, He YG. Epidermal growth factor, transforming growth factor alpha, transforming growth factor β, acidic fibroblast growth factor, basic fibroblast growth factor, and interleukin-1 proteins in the cornea. Exp Eye Res. 1994;59:63-71.
    • (1994) Exp Eye Res , vol.59 , pp. 63-71
    • Wilson, S.E.1    Schultz, G.S.2    Chegini, N.3    Weng, J.4    He, Y.G.5
  • 31
    • 0022470546 scopus 로고
    • Differentiation-related expression of a major 64K corneal keratin in vivo and in culture suggests limbal location of corneal epithelial stem cells
    • Schermer A, Galvin S, Sun TT. Differentiation-related expression of a major 64K corneal keratin in vivo and in culture suggests limbal location of corneal epithelial stem cells. J Cell Biol. 1986;103:49-62.
    • (1986) J Cell Biol , vol.103 , pp. 49-62
    • Schermer, A.1    Galvin, S.2    Sun, T.T.3
  • 32
    • 0004133195 scopus 로고
    • New York: Academic Press;
    • Colvin RB. Fibronectin. New York: Academic Press; 1989:213-252.
    • (1989) Fibronectin , pp. 213-252
    • Colvin, R.B.1
  • 34
    • 0026082034 scopus 로고
    • Transforming growth factor β type 1 binds to collagen IV of basement membrane matrix: Implications for development
    • Paralkar VM, Vukicevic S, Reddi AH. Transforming growth factor β type 1 binds to collagen IV of basement membrane matrix: implications for development. Dev Biol. 1991;143:303-308.
    • (1991) Dev Biol , vol.143 , pp. 303-308
    • Paralkar, V.M.1    Vukicevic, S.2    Reddi, A.H.3
  • 35
    • 33745726018 scopus 로고    scopus 로고
    • Schindler M, Nur EKA, Ahmed I, et al. Living in three dimensions: 3-D nanostructured environments for cell culture and regenerative medicine. Cell Biochem Biophys. 2006;45.215-228.
    • Schindler M, Nur EKA, Ahmed I, et al. Living in three dimensions: 3-D nanostructured environments for cell culture and regenerative medicine. Cell Biochem Biophys. 2006;45.215-228.
  • 36
    • 18044380649 scopus 로고    scopus 로고
    • A synthetic nanofibrillar matrix promotes in vivo-like organization and morphogenesis for cells in culture
    • Schindler M, Ahmed I, Kamal J, et al. A synthetic nanofibrillar matrix promotes in vivo-like organization and morphogenesis for cells in culture. Biomaterials. 2005;26:5624-5631.
    • (2005) Biomaterials , vol.26 , pp. 5624-5631
    • Schindler, M.1    Ahmed, I.2    Kamal, J.3
  • 38
    • 0035185853 scopus 로고    scopus 로고
    • Transforming growth factor-β1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism
    • Bhowmick NA, Ghiassi M, Bakin A, et al. Transforming growth factor-β1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism. Mol Biol Cell. 2001;12:27-36.
    • (2001) Mol Biol Cell , vol.12 , pp. 27-36
    • Bhowmick, N.A.1    Ghiassi, M.2    Bakin, A.3
  • 39
    • 0036467496 scopus 로고    scopus 로고
    • TGF-β signaling: Positive and negative effects on tumorigenesis
    • Wakefield LM, Roberts AB. TGF-β signaling: positive and negative effects on tumorigenesis. Curr Opin Genet Dev. 2002;12:22-29.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 22-29
    • Wakefield, L.M.1    Roberts, A.B.2
  • 40
    • 0033611058 scopus 로고    scopus 로고
    • Ezrin promotes morphogenesis of apical microvilli and basal infoldings in retinal pigment epithelium
    • Bonilha VL, Finnemann SC, Rodriguez-Boulan E. Ezrin promotes morphogenesis of apical microvilli and basal infoldings in retinal pigment epithelium. J Cell Biol. 1999;147:1533-1548.
    • (1999) J Cell Biol , vol.147 , pp. 1533-1548
    • Bonilha, V.L.1    Finnemann, S.C.2    Rodriguez-Boulan, E.3
  • 42
    • 0028247080 scopus 로고
    • Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members
    • Takeuchi K, Sato N, Kasahara H, et al. Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members. J Cell Biol. 1994;125:1371-1384.
    • (1994) J Cell Biol , vol.125 , pp. 1371-1384
    • Takeuchi, K.1    Sato, N.2    Kasahara, H.3
  • 43
    • 0035873075 scopus 로고    scopus 로고
    • Ezrin-dependent promotion of glioma cell clonogenicity, motility, and invasion mediated by BCL-2 and transforming growth factor-β2
    • Wick W, Grimmel C, Wild-Bode C, Platten M, Arpin M, Weller M. Ezrin-dependent promotion of glioma cell clonogenicity, motility, and invasion mediated by BCL-2 and transforming growth factor-β2. J Neurosci. 2001;21:3360-3368.
    • (2001) J Neurosci , vol.21 , pp. 3360-3368
    • Wick, W.1    Grimmel, C.2    Wild-Bode, C.3    Platten, M.4    Arpin, M.5    Weller, M.6
  • 44
    • 0023886444 scopus 로고
    • Latent transforming growth factor-β from human platelets: A high molecular weight complex containing precursor sequences
    • Wakefield LM, Smith DM, Flanders KC, Sporn MB. Latent transforming growth factor-β from human platelets: a high molecular weight complex containing precursor sequences. J Biol Chem. 1988;263:7646-7654.
    • (1988) J Biol Chem , vol.263 , pp. 7646-7654
    • Wakefield, L.M.1    Smith, D.M.2    Flanders, K.C.3    Sporn, M.B.4
  • 45
    • 0026701960 scopus 로고
    • Retention of the transforming growth factor-β 1 precursor in the Golgi complex in a latent endoglycosidase H-sensitive form
    • Miyazono K, Thyberg J, Heldin CH. Retention of the transforming growth factor-β 1 precursor in the Golgi complex in a latent endoglycosidase H-sensitive form. J Biol Chem. 1992;267:5668-5675.
    • (1992) J Biol Chem , vol.267 , pp. 5668-5675
    • Miyazono, K.1    Thyberg, J.2    Heldin, C.H.3
  • 46
    • 0025765844 scopus 로고
    • A role of the latent TGF-β 1-binding protein in the assembly and secretion of TGF-β 1
    • Miyazono K, Olofsson A, Colosetti P, Heldin CH. A role of the latent TGF-β 1-binding protein in the assembly and secretion of TGF-β 1. EMBO J. 1991;10:1091-1101.
    • (1991) EMBO J , vol.10 , pp. 1091-1101
    • Miyazono, K.1    Olofsson, A.2    Colosetti, P.3    Heldin, C.H.4
  • 47
    • 0025632985 scopus 로고
    • Recombinant latent transforming growth factor β1 has a longer plasma half-life in rats than active transforming growth factor β1, and a different tissue distribution
    • Wakefield LM, Winokur TS, Hollands RS, Christopherson K, Levinson AD, Sporn MB. Recombinant latent transforming growth factor β1 has a longer plasma half-life in rats than active transforming growth factor β1, and a different tissue distribution. J Clin Invest. 1990;86:1976-1984.
    • (1990) J Clin Invest , vol.86 , pp. 1976-1984
    • Wakefield, L.M.1    Winokur, T.S.2    Hollands, R.S.3    Christopherson, K.4    Levinson, A.D.5    Sporn, M.B.6
  • 48
    • 0026708669 scopus 로고
    • Post-transcriptional regulation of the human transforming growth factor-β1 gene
    • Kim SJ, Park K, Koeller D, et al. Post-transcriptional regulation of the human transforming growth factor-β1 gene. J Biol Chem. 1992;267:13702-13707.
    • (1992) J Biol Chem , vol.267 , pp. 13702-13707
    • Kim, S.J.1    Park, K.2    Koeller, D.3
  • 49
    • 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, Berryman M. Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J Cell Sci. 1997;110:3011-3018.
    • (1997) J Cell Sci , vol.110 , pp. 3011-3018
    • Bretscher, A.1    Reczek, D.2    Berryman, M.3
  • 50
    • 0032559362 scopus 로고    scopus 로고
    • GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science. 1998;279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Rho, H.A.1
  • 51
    • 0034725593 scopus 로고    scopus 로고
    • Integrins and actin filaments: Reciprocal regulation of cell adhesion and signaling
    • Calderwood DA, Shattil SJ, Ginsberg MH. Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling. J Biol Chem. 2000;275:22607-22610.
    • (2000) J Biol Chem , vol.275 , pp. 22607-22610
    • Calderwood, D.A.1    Shattil, S.J.2    Ginsberg, M.H.3
  • 52
    • 0036535898 scopus 로고    scopus 로고
    • The cytoplasmic face of cell contact sites
    • Pokutta S, Weis WI. The cytoplasmic face of cell contact sites. Curr Opin Struct Biol. 2002;12:255-262.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 255-262
    • Pokutta, S.1    Weis, W.I.2
  • 53
    • 0033521010 scopus 로고    scopus 로고
    • Cortical actin organization: Lessons from ERM (ezrin/radixin/moesin) proteins
    • Tsukita S, Yonemura S. Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins. J Biol Chem. 1999;274:34507-34510.
    • (1999) J Biol Chem , vol.274 , pp. 34507-34510
    • Tsukita, S.1    Yonemura, S.2
  • 54
    • 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, Arpin M. ERM proteins and NF2 tumor suppressor: the Yin and Yang of cortical actin organization and cell growth signaling. Curr Opin Cell Biol. 2002;14:104-109.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 104-109
    • Gautreau, A.1    Louvard, D.2    Arpin, M.3
  • 55
    • 0033777011 scopus 로고    scopus 로고
    • ERM proteins, from cellular architecture to cell signaling
    • Louvet-Vallee S. ERM proteins, from cellular architecture to cell signaling. Biol Cell. 2000;92:305-316.
    • (2000) Biol Cell , vol.92 , pp. 305-316
    • Louvet-Vallee, S.1
  • 56
    • 0034333146 scopus 로고    scopus 로고
    • Integrins as receptors for laminins
    • Belkin AM, Stepp MA. Integrins as receptors for laminins. Microsc Res Tech. 2000;51:280-301.
    • (2000) Microsc Res Tech , vol.51 , pp. 280-301
    • Belkin, A.M.1    Stepp, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.