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Volumn 288, Issue 29, 2013, Pages 21329-21340

SLLISWD sequence in the 10FNIII domain initiates fibronectin fibrillogenesis

Author keywords

[No Author keywords available]

Indexed keywords

FIBRILLOGENESIS; FIBRONECTIN MATRIX; MATRIX ASSEMBLY; MULTIMERIZATION; TISSUE REPAIR;

EID: 84880540675     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.462077     Document Type: Article
Times cited : (24)

References (62)
  • 2
    • 0035895247 scopus 로고    scopus 로고
    • A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis
    • Yi, M., and Ruoslahti, E. (2001) A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis. Proc. Natl. Acad. Sci. U.S.A. 98, 620-624
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 620-624
    • Yi, M.1    Ruoslahti, E.2
  • 4
    • 0037423391 scopus 로고    scopus 로고
    • Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan
    • Mongiat, M., Sweeney, S. M., San Antonio, J. D., Fu, J., and Iozzo, R. V. (2003) Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan. J. Biol. Chem. 278, 4238-4249
    • (2003) J. Biol. Chem. , vol.278 , pp. 4238-4249
    • Mongiat, M.1    Sweeney, S.M.2    San Antonio, J.D.3    Fu, J.4    Iozzo, R.V.5
  • 5
    • 38949195313 scopus 로고    scopus 로고
    • Basement membrane derived fibulin-1 and fibulin-5 function as angiogenesis inhibitors and suppress tumor growth
    • Xie, L., Palmsten, K., MacDonald, B., Kieran, M. W., Potenta, S., Vong, S., and Kalluri, R. (2008) Basement membrane derived fibulin-1 and fibulin-5 function as angiogenesis inhibitors and suppress tumor growth. Exp. Biol. Med. (Maywood) 233, 155-162
    • (2008) Exp. Biol. Med. (Maywood) , vol.233 , pp. 155-162
    • Xie, L.1    Palmsten, K.2    Macdonald, B.3    Kieran, M.W.4    Potenta, S.5    Vong, S.6    Kalluri, R.7
  • 7
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong, C., Chrzanowska-Wodnicka, M., Brown, J., Shaub, A., Belkin, A. M., and Burridge, K. (1998) Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 141, 539-551
    • (1998) J. Cell Biol. , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6
  • 8
    • 0034796439 scopus 로고    scopus 로고
    • Regulation of cell polarity, radial intercalation and epiboly in Xenopus. Novel roles for integrin and fibronectin
    • Marsden, M., and DeSimone, D. W. (2001) Regulation of cell polarity, radial intercalation and epiboly in Xenopus. Novel roles for integrin and fibronectin. Development 128, 3635-3647
    • (2001) Development , vol.128 , pp. 3635-3647
    • Marsden, M.1    Desimone, D.W.2
  • 9
    • 0016719143 scopus 로고
    • Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor
    • Mosher, D. F. (1975) Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor. J. Biol. Chem. 250, 6614-6621
    • (1975) J. Biol. Chem. , vol.250 , pp. 6614-6621
    • Mosher, D.F.1
  • 10
    • 77953809406 scopus 로고    scopus 로고
    • Atheroprone hemodynamics regulate fibronectin deposition to create positive feedback that sustains endothelial inflammation
    • Feaver, R. E., Gelfand, B. D., Wang, C., Schwartz, M. A., and Blackman, B. R. (2010) Atheroprone hemodynamics regulate fibronectin deposition to create positive feedback that sustains endothelial inflammation. Circ. Res. 106, 1703-1711
    • (2010) Circ. Res. , vol.106 , pp. 1703-1711
    • Feaver, R.E.1    Gelfand, B.D.2    Wang, C.3    Schwartz, M.A.4    Blackman, B.R.5
  • 12
    • 0345164291 scopus 로고
    • Alteration of cell-surface proteins by viral transformation and by proteolysis
    • Hynes, R. O. (1973) Alteration of cell-surface proteins by viral transformation and by proteolysis. Proc. Natl. Acad. Sci. U.S.A. 70, 3170-3174
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 3170-3174
    • Hynes, R.O.1
  • 14
    • 0025362679 scopus 로고
    • Inhibition ofbinding of fibronectin to matrix assembly sites byanti-integ-rin (α5β1) antibodies
    • Fogerty, F. J., Akiyama, S. K., Yamada, K. M., and Mosher, D. F. (1990) Inhibition ofbinding of fibronectin to matrix assembly sites byanti-integ-rin (α5β1) antibodies. J. Cell Biol. 111, 699-708
    • (1990) J. Cell Biol. , vol.111 , pp. 699-708
    • Fogerty, F.J.1    Akiyama, S.K.2    Yamada, K.M.3    Mosher, D.F.4
  • 15
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher, M. D., and Ruoslahti, E. (1984) Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309, 30-33
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 16
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix
    • Wu, C., Keivens, V. M., O'Toole, T. E., McDonald, J. A., and Ginsberg, M. H. (1995) Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix. Cell 83, 715-724
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Keivens, V.M.2    O'Toole, T.E.3    McDonald, J.A.4    Ginsberg, M.H.5
  • 17
    • 0023178166 scopus 로고
    • Fibronectin's cell-adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix
    • McDonald, J. A., Quade, B. J., Broekelmann, T. J., LaChance, R., Forsman, K., Hasegawa, E., and Akiyama, S. (1987) Fibronectin's cell-adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix. J. Biol. Chem. 262,2957-2967
    • (1987) J. Biol. Chem. , vol.262 , pp. 2957-2967
    • McDonald, J.A.1    Quade, B.J.2    Broekelmann, T.J.3    Lachance, R.4    Forsman, K.5    Hasegawa, E.6    Akiyama, S.7
  • 20
    • 79960686720 scopus 로고    scopus 로고
    • Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility
    • Lemmon, C. A., Ohashi, T., and Erickson, H. P. (2011) Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility. J. Biol. Chem. 286, 26375-26382
    • (2011) J. Biol. Chem. , vol.286 , pp. 26375-26382
    • Lemmon, C.A.1    Ohashi, T.2    Erickson, H.P.3
  • 21
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix- cytoskeleton crosstalk
    • Geiger, B., Bershadsky, A., Pankov, R., and Yamada, K. M. (2001) Transmembrane crosstalk between the extracellular matrix- cytoskeleton crosstalk. Nat. Rev. Mol. Cell Biol. 2, 793-805
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 22
    • 0025948419 scopus 로고
    • Monoclonal antibody characterization of two distant sites required for function of the central cell-binding domain of fibronectin in cell adhesion, cell migration, and matrix assembly
    • Nagai, T., Yamakawa, N., Aota, S., Yamada, S. S., Akiyama, S. K., Olden, K., and Yamada, K. M. (1991) Monoclonal antibody characterization of two distant sites required for function of the central cell-binding domain of fibronectin in cell adhesion, cell migration, and matrix assembly. J. Cell Biol. 114,1295-1305
    • (1991) J. Cell Biol. , vol.114 , pp. 1295-1305
    • Nagai, T.1    Yamakawa, N.2    Aota, S.3    Yamada, S.S.4    Akiyama, S.K.5    Olden, K.6    Yamada, K.M.7
  • 23
    • 1642493664 scopus 로고    scopus 로고
    • Tuning the mechanical stability of fibronectin type III modules through sequence variations
    • Craig, D., Gao, M., Schulten, K., and Vogel, V. (2004) Tuning the mechanical stability of fibronectin type III modules through sequence variations. Structure 12, 21-30
    • (2004) Structure , vol.12 , pp. 21-30
    • Craig, D.1    Gao, M.2    Schulten, K.3    Vogel, V.4
  • 24
    • 0029897753 scopus 로고    scopus 로고
    • A novel role for the integrin-binding III-10 module in fibronectin matrix assembly
    • Hocking, D. C., Smith, R. K., and McKeown-Longo, P. J. (1996) A novel role for the integrin-binding III-10 module in fibronectin matrix assembly. J. Cell Biol. 133, 431-444
    • (1996) J. Cell Biol. , vol.133 , pp. 431-444
    • Hocking, D.C.1    Smith, R.K.2    McKeown-Longo, P.J.3
  • 26
    • 48649102251 scopus 로고    scopus 로고
    • Fibronectin unfolding revisited. Modeling cell traction-mediated unfolding of the tenth type-III repeat
    • Gee, E. P., Ingber, D. E., and Stultz, C. M. (2008) Fibronectin unfolding revisited. Modeling cell traction-mediated unfolding of the tenth type-III repeat. PLoS One 3, e2373
    • (2008) PLoS One , vol.3
    • Gee, E.P.1    Ingber, D.E.2    Stultz, C.M.3
  • 27
    • 0036428792 scopus 로고    scopus 로고
    • Identifyingunfolding intermediates of FN-III(10) by steered molecular dynamics
    • Gao, M., Craig, D., Vogel, V., and Schulten, K. (2002) Identifyingunfolding intermediates of FN-III(10) by steered molecular dynamics. J. Mol. Biol. 323, 939-950
    • (2002) J. Mol. Biol. , vol.323 , pp. 939-950
    • Gao, M.1    Craig, D.2    Vogel, V.3    Schulten, K.4
  • 28
    • 0033531973 scopus 로고    scopus 로고
    • Forced unfolding of fibronectin type 3 modules. An analysis by biased molecular dynamics simulations
    • Paci, E., and Karplus, M. (1999) Forced unfolding of fibronectin type 3 modules. An analysis by biased molecular dynamics simulations. J. Mol. Biol. 288, 441-459
    • (1999) J. Mol. Biol. , vol.288 , pp. 441-459
    • Paci, E.1    Karplus, M.2
  • 29
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4, 2411-2423
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 30
    • 23344453824 scopus 로고    scopus 로고
    • Fibronectin's central cell-binding domain supports focal adhesion formation and Rho signal transduction
    • Wang, R., Clark, R. A., Mosher, D. F., and Ren, X. D. (2005) Fibronectin's central cell-binding domain supports focal adhesion formation and Rho signal transduction. J. Biol. Chem. 280, 28803-28810
    • (2005) J. Biol. Chem. , vol.280 , pp. 28803-28810
    • Wang, R.1    Clark, R.A.2    Mosher, D.F.3    Ren, X.D.4
  • 31
    • 0016375591 scopus 로고
    • The use of fluorescent probes for the study of membranes
    • Azzi, A. (1974) The use of fluorescent probes for the study of membranes. Methods Enzymol. 32, 234-246
    • (1974) Methods Enzymol. , vol.32 , pp. 234-246
    • Azzi, A.1
  • 32
    • 0032830122 scopus 로고    scopus 로고
    • In vitro immunoglobulin light chain fibrillogenesis
    • Wall, J., Murphy, C. L., and Solomon, A. (1999) In vitro immunoglobulin light chain fibrillogenesis. Methods Enzymol. 309, 204-217
    • (1999) Methods Enzymol. , vol.309 , pp. 204-217
    • Wall, J.1    Murphy, C.L.2    Solomon, A.3
  • 33
    • 0020601855 scopus 로고
    • Binding of plasma fibronectin to cell layers of human skin fibroblasts
    • McKeown-Longo, P. J., and Mosher, D. F. (1983) Binding of plasma fibronectin to cell layers of human skin fibroblasts. J. Cell Biol. 97,466-472
    • (1983) J. Cell Biol. , vol.97 , pp. 466-472
    • McKeown-Longo, P.J.1    Mosher, D.F.2
  • 34
    • 0028069348 scopus 로고
    • Superfibronectin is a functionally distinct form of fibronectin
    • Morla, A., Zhang, Z., and Ruoslahti, E. (1994) Superfibronectin is a functionally distinct form of fibronectin. Nature 367,193-196
    • (1994) Nature , vol.367 , pp. 193-196
    • Morla, A.1    Zhang, Z.2    Ruoslahti, E.3
  • 35
    • 0019311578 scopus 로고
    • Characterization of fibronectin interactions with glycosaminoglycans and identification of active proteolytic fragments
    • Yamada, K. M., Kennedy, D. W., Kimata, K., and Pratt, R. M. (1980) Characterization of fibronectin interactions with glycosaminoglycans and identification of active proteolytic fragments. J. Biol. Chem. 255, 6055-6063
    • (1980) J. Biol. Chem. , vol.255 , pp. 6055-6063
    • Yamada, K.M.1    Kennedy, D.W.2    Kimata, K.3    Pratt, R.M.4
  • 36
    • 0013800421 scopus 로고
    • The interaction ofa naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
    • Stryer, L. (1965) The interaction ofa naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13, 482-495
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 37
    • 66049096953 scopus 로고    scopus 로고
    • Transient opening of fibronectin type III (FNIII) domains. The interaction of the third FNIII domain of FN with anastellin
    • Ohashi, T., Augustus, A. M., and Erickson, H. P. (2009) Transient opening of fibronectin type III (FNIII) domains. The interaction of the third FNIII domain of FN with anastellin. Biochemistry 48, 4189-4197
    • (2009) Biochemistry , vol.48 , pp. 4189-4197
    • Ohashi, T.1    Augustus, A.M.2    Erickson, H.P.3
  • 38
    • 0032503933 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module
    • Litvinovich, S. V., Brew, S. A., Aota, S., Akiyama, S. K., Haudenschild, C., and Ingham, K. C. (1998) Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module. J. Mol. Biol. 280, 245-258
    • (1998) J. Mol. Biol. , vol.280 , pp. 245-258
    • Litvinovich, S.V.1    Brew, S.A.2    Aota, S.3    Akiyama, S.K.4    Haudenschild, C.5    Ingham, K.C.6
  • 39
    • 0031571127 scopus 로고    scopus 로고
    • Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin
    • Carr, P. A., Erickson, H. P., and Palmer, A. G., 3rd (1997) Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin. Structure 5, 949 -959
    • (1997) Structure , vol.5 , pp. 949-959
    • Carr, P.A.1    Erickson, H.P.2    Palmer Iii, A.G.3
  • 40
    • 28244461501 scopus 로고    scopus 로고
    • Domain unfolding plays a role in superfibronectin formation
    • Ohashi, T., and Erickson, H. P. (2005) Domain unfolding plays a role in superfibronectin formation. J. Biol. Chem. 280, 39143-39151
    • (2005) J. Biol. Chem. , vol.280 , pp. 39143-39151
    • Ohashi, T.1    Erickson, H.P.2
  • 41
    • 58149326746 scopus 로고    scopus 로고
    • Molecular mechanism of thioflavin-T binding to the surface of β-rich peptide self-assemblies
    • Biancalana, M., Makabe, K., Koide, A., and Koide, S. (2009) Molecular mechanism of thioflavin-T binding to the surface of β-rich peptide self-assemblies. J. Mol. Biol. 385, 1052-1063
    • (2009) J. Mol. Biol. , vol.385 , pp. 1052-1063
    • Biancalana, M.1    Makabe, K.2    Koide, A.3    Koide, S.4
  • 42
    • 0032773506 scopus 로고    scopus 로고
    • The immunoglobulin fold family. Sequence analysis and 3D structure comparisons
    • Halaby, D. M., Poupon, A., and Mornon, J. (1999) The immunoglobulin fold family. Sequence analysis and 3D structure comparisons. Protein Eng. 12, 563-571
    • (1999) Protein Eng. , vol.12 , pp. 563-571
    • Halaby, D.M.1    Poupon, A.2    Mornon, J.3
  • 43
    • 0034703474 scopus 로고    scopus 로고
    • Two proteins with the same structure respond very differently to mutation. The role of plasticity in protein stability
    • Cota, E., Hamill, S. J., Fowler, S. B., and Clarke, J. (2000) Two proteins with the same structure respond very differently to mutation. The role of plasticity in protein stability. J. Mol. Biol. 302, 713-725
    • (2000) J. Mol. Biol. , vol.302 , pp. 713-725
    • Cota, E.1    Hamill, S.J.2    Fowler, S.B.3    Clarke, J.4
  • 44
    • 0036473019 scopus 로고    scopus 로고
    • The incorporation of fibrinogen into extracellular matrix is dependent on active assembly of a fibronectin matrix
    • Pereira, M., Rybarczyk, B. J., Odrljin, T. M., Hocking, D. C., Sottile, J., and Simpson-Haidaris, P. J. (2002) The incorporation of fibrinogen into extracellular matrix is dependent on active assembly of a fibronectin matrix. J. Cell Sci. 115, 609-617
    • (2002) J. Cell Sci. , vol.115 , pp. 609-617
    • Pereira, M.1    Rybarczyk, B.J.2    Odrljin, T.M.3    Hocking, D.C.4    Sottile, J.5    Simpson-Haidaris, P.J.6
  • 45
    • 0042235309 scopus 로고    scopus 로고
    • Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors
    • Briknarova, K., Akerman, M. E., Hoyt, D. W., Ruoslahti, E., and Ely, K. R. (2003) Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors. J. Mol. Biol. 332, 205-215
    • (2003) J. Mol. Biol. , vol.332 , pp. 205-215
    • Briknarova, K.1    Akerman, M.E.2    Hoyt, D.W.3    Ruoslahti, E.4    Ely, K.R.5
  • 46
    • 0029882793 scopus 로고    scopus 로고
    • Formation of sodium dodecyl sulfate-stable fibronectin multimers. Failure to detect products of thiol-disulfide exchange in cyanogen bromide or limited acid digests of stabilized matrix fibronectin
    • Chen, H., and Mosher, D. F. (1996) Formation of sodium dodecyl sulfate-stable fibronectin multimers. Failure to detect products of thiol-disulfide exchange in cyanogen bromide or limited acid digests of stabilized matrix fibronectin. J. Biol. Chem. 271, 9084-9089
    • (1996) J. Biol. Chem. , vol.271 , pp. 9084-9089
    • Chen, H.1    Mosher, D.F.2
  • 47
    • 71949122441 scopus 로고    scopus 로고
    • Stretched extracellular matrix proteins turn fouling and are functionally rescued by the chaperones albumin and casein
    • Little, W. C., Schwartlander, R., Smith, M. L., Gourdon, D., and Vogel, V. (2009) Stretched extracellular matrix proteins turn fouling and are functionally rescued by the chaperones albumin and casein. Nano Lett. 9, 4158-4167
    • (2009) Nano Lett. , vol.9 , pp. 4158-4167
    • Little, W.C.1    Schwartlander, R.2    Smith, M.L.3    Gourdon, D.4    Vogel, V.5
  • 48
    • 0034730203 scopus 로고    scopus 로고
    • Designed protein tetramer zipped together with a hydrophobic Alzheimer homology. A structural clue to amyloid assembly
    • Otzen, D. E., Kristensen, O., and Oliveberg, M. (2000) Designed protein tetramer zipped together with a hydrophobic Alzheimer homology. A structural clue to amyloid assembly. Proc. Natl. Acad. Sci. U.S.A. 97, 9907-9912
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 9907-9912
    • Otzen, D.E.1    Kristensen, O.2    Oliveberg, M.3
  • 49
    • 50149117570 scopus 로고    scopus 로고
    • High-throughput analysis of the protein sequence-stability landscape using a quantitative yeast surface two-hybrid system and fragment reconstitution
    • Dutta, S., Koide, A., and Koide, S. (2008) High-throughput analysis of the protein sequence-stability landscape using a quantitative yeast surface two-hybrid system and fragment reconstitution. J. Mol. Biol. 382, 721-733
    • (2008) J. Mol. Biol. , vol.382 , pp. 721-733
    • Dutta, S.1    Koide, A.2    Koide, S.3
  • 50
    • 13844315323 scopus 로고    scopus 로고
    • Angiostatic peptides use plasma fibronectin to home to angiogenic vasculature
    • Akerman, M. E., Pilch, J., Peters, D., and Ruoslahti, E. (2005) Angiostatic peptides use plasma fibronectin to home to angiogenic vasculature. Proc. Natl. Acad. Sci. U.S.A. 102, 2040 -2045
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 2040-2045
    • Akerman, M.E.1    Pilch, J.2    Peters, D.3    Ruoslahti, E.4
  • 51
    • 84861557846 scopus 로고    scopus 로고
    • CLT1 targets angiogenic endothelium through CLIC1 and fibronectin
    • Knowles, L. M., Malik, G., Hood, B. L., Conrads, T. P., and Pilch, J. (2012) CLT1 targets angiogenic endothelium through CLIC1 and fibronectin. Angiogenesis 15,115-129
    • (2012) Angiogenesis , vol.15 , pp. 115-129
    • Knowles, L.M.1    Malik, G.2    Hood, B.L.3    Conrads, T.P.4    Pilch, J.5
  • 52
    • 65549112108 scopus 로고    scopus 로고
    • A novel fibronectin binding motif in MSCRAMMs targets F3 modules
    • Prabhakaran, S., Liang, X., Skare, J. T., Potts, J. R., and Höök, M. (2009) A novel fibronectin binding motif in MSCRAMMs targets F3 modules. PLoS One 4, e5412
    • (2009) PLoS One , vol.4
    • Prabhakaran, S.1    Liang, X.2    Skare, J.T.3    Potts, J.R.4    Höök, M.5
  • 53
    • 0028997623 scopus 로고
    • Interactions between type III domains in the 110-kDa cell-binding fragment of fibronectin
    • Litvinovich, S. V., and Ingham, K. C. (1995) Interactions between type III domains in the 110-kDa cell-binding fragment of fibronectin. J. Mol. Biol. 248, 611- 626
    • (1995) J. Mol. Biol. , vol.248 , pp. 611-626
    • Litvinovich, S.V.1    Ingham, K.C.2
  • 54
    • 0033957144 scopus 로고    scopus 로고
    • Folding of β-sandwich proteins. Three-state transition of a fibronectin type III module
    • Cota, E., and Clarke, J. (2000) Folding of β-sandwich proteins. Three-state transition of a fibronectin type III module. Protein Sci. 9, 112-120
    • (2000) Protein Sci. , vol.9 , pp. 112-120
    • Cota, E.1    Clarke, J.2
  • 55
    • 0034719137 scopus 로고    scopus 로고
    • Role of the β-strand insert in the central domain of the fibrinogen 7-module
    • Yakovlev, S., Litvinovich, S., Loukinov, D., and Medved, L. (2000) Role of the β-strand insert in the central domain of the fibrinogen 7-module. Biochemistry 39, 15721-15729
    • (2000) Biochemistry , vol.39 , pp. 15721-15729
    • Yakovlev, S.1    Litvinovich, S.2    Loukinov, D.3    Medved, L.4
  • 56
    • 0028245615 scopus 로고
    • Identification of a novel integrin binding site in fibronectin. Differential utilization by β3 integrins
    • Bowditch, R. D., Hariharan, M., Tominna, E. F., Smith, J. W., Yamada, K. M., Getzoff, E. D., and Ginsberg, M. H. (1994) Identification of a novel integrin binding site in fibronectin. Differential utilization by β3 integrins. J. Biol. Chem. 269,10856-10863
    • (1994) J. Biol. Chem. , vol.269 , pp. 10856-10863
    • Bowditch, R.D.1    Hariharan, M.2    Tominna, E.F.3    Smith, J.W.4    Yamada, K.M.5    Getzoff, E.D.6    Ginsberg, M.H.7
  • 57
    • 0027971378 scopus 로고
    • The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function
    • Aota, S., Nomizu, M., and Yamada, K. M. (1994) The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J.Biol. Chem. 269, 24756-24761
    • (1994) J.Biol. Chem. , vol.269 , pp. 24756-24761
    • Aota, S.1    Nomizu, M.2    Yamada, K.M.3
  • 58
    • 0029100101 scopus 로고
    • Requirement for the synergy site for cell adhesion to fibronectin depends on the activation state of integrin a5β1
    • Danen, E. H., Aota, S., van Kraats, A. A., Yamada, K. M., Ruiter, D. J., and van Muijen, G. N. (1995) Requirement for the synergy site for cell adhesion to fibronectin depends on the activation state of integrin a5β1. J. Biol. Chem 270, 21612-21618
    • (1995) J. Biol. Chem , vol.270 , pp. 21612-21618
    • Danen, E.H.1    Aota, S.2    Van Kraats, A.A.3    Yamada, K.M.4    Ruiter, D.J.5    Van Muijen, G.N.6
  • 59
    • 0030659845 scopus 로고    scopus 로고
    • Modulatory roles for integrin activation and the synergy site of fibronectin during matrix assembly
    • Sechler, J. L., Corbett, S. A., and Schwarzbauer, J. E. (1997) Modulatory roles for integrin activation and the synergy site of fibronectin during matrix assembly. Mol. Biol. Cell 8, 2563-2573
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2563-2573
    • Sechler, J.L.1    Corbett, S.A.2    Schwarzbauer, J.E.3
  • 60
    • 0030993915 scopus 로고    scopus 로고
    • Structural requirements for biological activity of the ninth and tenth FIII domains of human fibronectin
    • Grant, R. P., Spitzfaden, C., Altroff, H., Campbell, I. D., and Mardon, H. J. (1997) Structural requirements for biological activity of the ninth and tenth FIII domains of human fibronectin. J. Biol. Chem. 272, 6159 - 6166
    • (1997) J. Biol. Chem. , vol.272 , pp. 6159-6166
    • Grant, R.P.1    Spitzfaden, C.2    Altroff, H.3    Campbell, I.D.4    Mardon, H.J.5
  • 61
    • 0031556949 scopus 로고    scopus 로고
    • Module-module interactions in the cell binding region offibronectin. Stability, flexibility and specificity
    • Spitzfaden, C., Grant, R. P., Mardon, H. J., and Campbell, I. D. (1997) Module-module interactions in the cell binding region offibronectin. Stability, flexibility and specificity. J. Mol. Biol. 265, 565-579
    • (1997) J. Mol. Biol. , vol.265 , pp. 565-579
    • Spitzfaden, C.1    Grant, R.P.2    Mardon, H.J.3    Campbell, I.D.4
  • 62
    • 0344736695 scopus 로고    scopus 로고
    • Structure and functional significance of mechanically unfolded fi-bronectin type III1 intermediates
    • Gao, M., Craig, D., Lequin, O., Campbell, I. D., Vogel, V., and Schulten, K. (2003) Structure and functional significance of mechanically unfolded fi-bronectin type III1 intermediates. Proc. Natl. Acad. Sci. U.S.A. 100, 14784-14789
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 14784-14789
    • Gao, M.1    Craig, D.2    Lequin, O.3    Campbell, I.D.4    Vogel, V.5    Schulten, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.