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Volumn 287, Issue 21, 2012, Pages 17578-17588

Extra-domain B in oncofetal fibronectin structurally promotes fibrillar head-to-tail dimerization of extracellular matrix protein

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTICAL ULTRACENTRIFUGATION; CELL SURFACES; DIMER FORMATION; DISULFIDE BRIDGE; EXTRACELLULAR MATRIX PROTEIN; FIBRIL FORMATION; HOMODIMERS; INTEGRINS; INTRACELLULAR SIGNALING; NEOANGIOGENESIS; THREE-DIMENSIONAL STRUCTURE; X-RAY STRUCTURE;

EID: 84861204373     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.303131     Document Type: Article
Times cited : (34)

References (72)
  • 1
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell-mediated matrix assembly process
    • DOI 10.1016/j.matbio.2005.06.008, PII S0945053X05000855
    • Mao, Y., and Schwarzbauer, J. E. (2005) Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix Biol. 24, 389-399 (Pubitemid 41765018)
    • (2005) Matrix Biology , vol.24 , Issue.6 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 2
    • 0001876846 scopus 로고
    • Fibronectins
    • (Rich, A. ed.), Springer-Verlag, New York
    • Hynes, R. O. (1990) Fibronectins in Springer's Series in Molecular Biology (Rich, A. ed.), pp. 546, Springer-Verlag, New York
    • (1990) Springer's Series in Molecular Biology , pp. 546
    • Hynes, R.O.1
  • 3
    • 0030818072 scopus 로고    scopus 로고
    • Fibronectins are essential for heart and blood vessel morphogenesis but are dispensable for initial specification of precursor cells
    • George, E. L., Baldwin, H. S., and Hynes, R. O. (1997) Fibronectins are essential for heart and blood vessel morphogenesis but are dispensable for initial specification of precursor cells. Blood 90, 3073-3081 (Pubitemid 27444201)
    • (1997) Blood , vol.90 , Issue.8 , pp. 3073-3081
    • George, E.L.1    Baldwin, H.S.2    Hynes, R.O.3
  • 4
    • 0025896188 scopus 로고
    • Identification of the fibronectin sequences required for assembly of a fibrillar matrix
    • Schwarzbauer, J. E. (1991) Identification of the fibronectin sequences required for assembly of a fibrillar matrix. J. Cell Biol. 113, 1463-1473
    • (1991) J. Cell Biol. , vol.113 , pp. 1463-1473
    • Schwarzbauer, J.E.1
  • 5
    • 33749676409 scopus 로고    scopus 로고
    • Heparin-II domain of fibronectin is a vascular endothelial growth factor-binding domain: Enhancement of VEGF biological activity by a singular growth factor/matrix protein synergism
    • DOI 10.1161/01.RES.0000246849.17887.66, PII 0000301220061013000011
    • Wijelath, E. S., Rahman, S., Namekata, M., Murray, J., Nishimura, T., Mostafavi-Pour, Z., Patel, Y., Suda, Y., Humphries, M. J., and Sobel, M. (2006) Heparin-II domain of fibronectin is a vascular endothelial growth factor-binding domain: enhancement of VEGF biological activity by a singular growth factor/matrix protein synergism. Circ. Res. 99, 853-860 (Pubitemid 44556384)
    • (2006) Circulation Research , vol.99 , Issue.8 , pp. 853-860
    • Wijelath, E.S.1    Rahman, S.2    Namekata, M.3    Murray, J.4    Nishimura, T.5    Mostafavi-Pour, Z.6    Patel, Y.7    Suda, Y.8    Humphries, M.J.9    Sobel, M.10
  • 6
    • 78649727712 scopus 로고    scopus 로고
    • The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain
    • Martino, M. M., and Hubbell, J. A. (2010) The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain. FASEB J. 24, 4711-4721
    • (2010) FASEB J. , vol.24 , pp. 4711-4721
    • Martino, M.M.1    Hubbell, J.A.2
  • 7
    • 0042887252 scopus 로고    scopus 로고
    • The ins and outs of fibronectin matrix assembly
    • DOI 10.1242/jcs.00670
    • Wierzbicka-Patynowski, I., and Schwarzbauer, J. E. (2003) The ins and outs of fibronectin matrix assembly. J. Cell Sci. 116, 3269-3276 (Pubitemid 37038975)
    • (2003) Journal of Cell Science , vol.116 , Issue.16 , pp. 3269-3276
    • Wierzbicka-Patynowski, I.1    Schwarzbauer, J.E.2
  • 8
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: Not just pretty fibrils
    • Hynes, R. O. (2009) The extracellular matrix: Not just pretty fibrils. Science 326, 1216-1219
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 9
    • 0020569136 scopus 로고
    • Plasma fibronectin is synthesized and secreted by hepatocytes
    • Tamkun, J. W., and Hynes, R. O. (1983) Plasma fibronectin is synthesized and secreted by hepatocytes. J. Biol. Chem. 258, 4641-4647 (Pubitemid 13080691)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.7 , pp. 4641-4647
    • Tamkun, J.W.1    Hynes, R.O.2
  • 10
    • 4143130159 scopus 로고    scopus 로고
    • Assembly of exogenous fibronectin by fibronectin-null cells is dependent on the adhesive substrate
    • DOI 10.1074/jbc.M406283200
    • Bae, E., Sakai, T., and Mosher, D. F. (2004) Assembly of exogenous fibronectin by fibronectin-null cells is dependent on the adhesive substrate. J. Biol. Chem. 279, 35749-35759 (Pubitemid 39100580)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35749-35759
    • Bae, E.1    Sakai, T.2    Mosher, D.F.3
  • 11
    • 0036166823 scopus 로고    scopus 로고
    • Domain structure and organisation in extracellular matrix proteins
    • DOI 10.1016/S0945-053X(01)00191-3, PII S0945053X01001913
    • Hohenester, E., and Engel, J. (2002) Domain structure and organization in extracellular matrix proteins. Matrix Biol. 21, 115-128 (Pubitemid 34145238)
    • (2002) Matrix Biology , vol.21 , Issue.2 , pp. 115-128
    • Hohenester, E.1    Engel, J.2
  • 12
    • 0028043949 scopus 로고
    • Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule
    • Aguirre, K. M., McCormick, R. J., and Schwarzbauer, J. E. (1994) Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule. J. Biol. Chem. 269, 27863-27868 (Pubitemid 24354509)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.45 , pp. 27863-27868
    • Aguirre, K.M.1    McCormick, R.J.2    Schwarzbauer, J.E.3
  • 13
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • DOI 10.1242/jcs.00059
    • Pankov, R., and Yamada, K. M. (2002) Fibronectin at a glance. J. Cell Sci. 115, 3861-3863 (Pubitemid 35256486)
    • (2002) Journal of Cell Science , vol.115 , Issue.20 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 14
    • 50249176028 scopus 로고    scopus 로고
    • New insights into form and function of fibronectin splice variants
    • White, E. S., Baralle, F. E., and Muro, A. F. (2008) New insights into form and function of fibronectin splice variants. J. Pathol. 216, 1-14
    • (2008) J. Pathol. , vol.216 , pp. 1-14
    • White, E.S.1    Baralle, F.E.2    Muro, A.F.3
  • 15
    • 0036488496 scopus 로고    scopus 로고
    • Specialization of tumor vasculature
    • Ruoslahti, E. (2002) Specialization of tumor vasculature. Nat. Rev. Cancer 2, 83-90
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 83-90
    • Ruoslahti, E.1
  • 16
    • 0021770759 scopus 로고
    • Human fibronectin: Cell-specific alternative mRNA splicing generates polypeptide chains differing in the number of internal repeats
    • Kornblihtt, A. R., Vibe-Pedersen, K., and Baralle, F. E. (1984) Human fibronectin: Cell-specific alternative mRNA splicing generates polypeptide chains differing in the number of internal repeats. Nucleic Acids Res. 12, 5853-5868
    • (1984) Nucleic Acids Res. , vol.12 , pp. 5853-5868
    • Kornblihtt, A.R.1    Vibe-Pedersen, K.2    Baralle, F.E.3
  • 17
    • 0023392493 scopus 로고
    • Transformed human cells produce a new fibronectin isoform by preferential alternative splicing of a previously unobserved exon
    • Zardi, L., Carnemolla, B., Siri, A., Petersen, T. E., Paolella, G., Sebastio, G., and Baralle, F. E. (1987) Transformed human cells produce a new fibronectin isoform by preferential alternative splicing of a previously unobserved exon. EMBO J. 6, 2337-2342
    • (1987) EMBO J. , vol.6 , pp. 2337-2342
    • Zardi, L.1    Carnemolla, B.2    Siri, A.3    Petersen, T.E.4    Paolella, G.5    Sebastio, G.6    Baralle, F.E.7
  • 18
    • 35848962936 scopus 로고    scopus 로고
    • Antibody-based targeting of the tumor vasculature
    • DOI 10.1016/j.bbcan.2007.08.002, PII S0304419X07000285
    • Schliemann, C., and Neri, D. (2007) Antibody-based targeting of the tumor vasculature. Biochim. Biophys. Acta 1776, 175-192 (Pubitemid 350061071)
    • (2007) Biochimica et Biophysica Acta - Reviews on Cancer , vol.1776 , Issue.2 , pp. 175-192
    • Schliemann, C.1    Neri, D.2
  • 19
    • 0024594936 scopus 로고
    • A tumor-associated fibronectin isoform generated by alternative splicing of messenger RNA precursors
    • DOI 10.1083/jcb.108.3.1139
    • Carnemolla, B., Balza, E., Siri, A., Zardi, L., Nicotra, M. R., Bigotti, A., and Natali, P. G. (1989) A tumor-associated fibronectin isoform generated by alternative splicing of messenger RNA precursors. J. Cell Biol. 108, 1139-1148 (Pubitemid 19083757)
    • (1989) Journal of Cell Biology , vol.108 , Issue.3 , pp. 1139-1148
    • Carnemolla, B.1    Balza, E.2    Siri, A.3    Zardi, L.4    Nicotra, M.R.5    Bigotti, A.6    Natali, P.G.7
  • 21
    • 0035822678 scopus 로고    scopus 로고
    • Recognition of fibronectin by the platelet integrin αIIbβ3 involves an extended interface with multiple electrostatic interactions
    • DOI 10.1021/bi010503x
    • Kauf, A. C., Hough, S. M., and Bowditch, R. D. (2001) Recognition of fibronectin by the platelet integrinα IIb β 3 involves an extended interface with multiple electrostatic interactions. Biochemistry 40, 9159-9166 (Pubitemid 32730037)
    • (2001) Biochemistry , vol.40 , Issue.31 , pp. 9159-9166
    • Kauf, A.C.W.1    Hough, S.M.2    Bowditch, R.D.3
  • 22
    • 0034678405 scopus 로고    scopus 로고
    • Defining Fibronectin's cell adhesion synergy site by site-directed mutagenesis
    • DOI 10.1083/jcb.149.2.521
    • Redick, S. D., Settles, D. L., Briscoe, G., and Erickson, H. P. (2000) Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis. J. Cell Biol. 149, 521-527 (Pubitemid 30227165)
    • (2000) Journal of Cell Biology , vol.149 , Issue.2 , pp. 521-527
    • Redick, S.D.1    Settles, D.L.2    Briscoe, G.3    Erickson, H.P.4
  • 23
    • 0030993915 scopus 로고    scopus 로고
    • Structural requirements for biological activity of the ninth and tenth FIII domains of human fibronectin
    • DOI 10.1074/jbc.272.10.6159
    • 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 (Pubitemid 27118083)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.10 , pp. 6159-6166
    • Grant, R.P.1    Spitzfaden, C.2    Altroff, H.3    Campbell, I.D.4    Mardon, H.J.5
  • 24
    • 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 (Pubitemid 24311733)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.40 , pp. 24756-24761
    • Aota, S.-I.1    Nomizu, M.2    Yamada, K.M.3
  • 26
    • 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 (Pubitemid 27528222)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.12 , pp. 2563-2573
    • Sechler, J.L.1    Corbett, S.A.2    Schwarzbauer, J.E.3
  • 28
    • 0030769052 scopus 로고    scopus 로고
    • The alternatively spliced domains EIIIB and EIIIA of human fibronectin affect cell adhesion and spreading
    • Hashimoto-Uoshima, M., Yan, Y. Z., Schneider, G., and Aukhil, I. (1997) The alternatively spliced domains EIIIB and EIIIA of human fibronectin affect cell adhesion and spreading. J. Cell Sci. 110, 2271-2280 (Pubitemid 27448371)
    • (1997) Journal of Cell Science , vol.110 , Issue.18 , pp. 2271-2280
    • Hashimoto-Uoshima, M.1    Yan, Y.Z.2    Schneider, G.3    Aukhil, I.4
  • 29
    • 0026476010 scopus 로고
    • The inclusion of the type III repeat ED-B in the fibronectin molecule generates conformational modifications that unmask a cryptic sequence
    • Carnemolla, B., Leprini, A., Allemanni, G., Saginati, M., and Zardi, L. (1992) The inclusion of the type III repeat ED-B in the fibronectin molecule generates conformational modifications that unmask a cryptic sequence. J. Biol. Chem. 267, 24689-24692
    • (1992) J. Biol. Chem. , vol.267 , pp. 24689-24692
    • Carnemolla, B.1    Leprini, A.2    Allemanni, G.3    Saginati, M.4    Zardi, L.5
  • 32
    • 77949344954 scopus 로고    scopus 로고
    • Alternative splicing of the angiogenesis associated extra-domain B of fibronectin regulates the accessibility of the B-C loop of the type III repeat 8
    • Ventura, E., Sassi, F., Parodi, A., Balza, E., Borsi, L., Castellani, P., Carnemolla, B., and Zardi, L. (2010) Alternative splicing of the angiogenesis associated extra-domain B of fibronectin regulates the accessibility of the B-C loop of the type III repeat 8. PLoS One 5, e9145
    • (2010) PLoS One , vol.5
    • Ventura, E.1    Sassi, F.2    Parodi, A.3    Balza, E.4    Borsi, L.5    Castellani, P.6    Carnemolla, B.7    Zardi, L.8
  • 33
    • 0028555357 scopus 로고
    • Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli
    • Skerra, A. (1994) Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli. Gene 151, 131-135
    • (1994) Gene , vol.151 , pp. 131-135
    • Skerra, A.1
  • 34
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy, D. J., Aukhil, I., and Erickson, H. P. (1996) 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84, 155-164
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 35
    • 0028243318 scopus 로고
    • The de novo design of an antibody combining site. Crystallographic analysis of the VL domain confirms the structural model
    • Essen, L. O., and Skerra, A. (1994) The de novo design of an antibody combining site. Crystallographic analysis of the VL domain confirms the structural model. J. Mol. Biol. 238, 226-244
    • (1994) J. Mol. Biol. , vol.238 , pp. 226-244
    • Essen, L.O.1    Skerra, A.2
  • 36
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and Moffatt, B. A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113-130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 37
    • 0028348843 scopus 로고
    • Ageneral vector, pASK84, for cloning, bacterial production, and single-step purification of antibody Fab fragments
    • Skerra, A. (1994)Ageneral vector, pASK84, for cloning, bacterial production, and single-step purification of antibody Fab fragments. Gene 141, 79-84
    • (1994) Gene , vol.141 , pp. 79-84
    • Skerra, A.1
  • 39
  • 44
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J., and Merritt, E. A. (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62, 439-450
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 45
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS Refinement in REFMAC at Moderate Resolutions
    • DOI 10.1016/S0076-6879(03)74014-2
    • Winn, M. D., Murshudov, G. N., and Papiz, M. Z. (2003) Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 374, 300-321 (Pubitemid 37531815)
    • (2003) Methods in Enzymology , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 48
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983) Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 50
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • Krissinel, E., and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60, 2256-2268 (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 I , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 51
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 52
    • 36549052564 scopus 로고    scopus 로고
    • Quality control and validation
    • Kleywegt, G. J. (2007) Quality control and validation. Methods Mol. Biol. 364, 255-272
    • (2007) Methods Mol. Biol. , vol.364 , pp. 255-272
    • Kleywegt, G.J.1
  • 53
    • 0033560794 scopus 로고    scopus 로고
    • NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis
    • DOI 10.1016/S0969-2126(99)80051-3
    • Fattorusso, R., Pellecchia, M., Viti, F., Neri, P., Neri, D., and Wuthrich, K. (1999) NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis. Structure 7, 381-390 (Pubitemid 29190472)
    • (1999) Structure , vol.7 , Issue.4 , pp. 381-390
    • Fattorusso, R.1    Pellecchia, M.2    Viti, F.3    Neri, P.4    Neri, D.5    Wuthrich, K.6
  • 54
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • DOI 10.1006/jmbi.1993.1648
    • Lawrence, M. C., and Colman, P. M. (1993) Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234, 946-950 (Pubitemid 24027225)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.4 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 56
    • 29144459934 scopus 로고    scopus 로고
    • Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry
    • DOI 10.1021/pr0502065
    • Liu, T., Qian, W. J., Gritsenko, M. A., Camp, D. G., 2nd, Monroe, M. E., Moore, R. J., and Smith, R. D. (2005) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 4, 2070-2080 (Pubitemid 41814273)
    • (2005) Journal of Proteome Research , vol.4 , Issue.6 , pp. 2070-2080
    • Liu, T.1    Qian, W.-J.2    Gritsenko, M.A.3    Camp II, D.G.4    Monroe, M.E.5    Moore, R.J.6    Smith, R.D.7
  • 57
    • 0025940655 scopus 로고
    • Arrangement of cellular fibronectin in noncollagenous fibrils in human fibroblast cultures
    • Dzamba, B. J., and Peters, D. M. (1991) Arrangement of cellular fibronectin in noncollagenous fibrils in human fibroblast cultures. J. Cell Sci. 100, 605-612
    • (1991) J. Cell Sci. , vol.100 , pp. 605-612
    • Dzamba, B.J.1    Peters, D.M.2
  • 58
    • 0033016468 scopus 로고    scopus 로고
    • The compact conformation of fibronectin is determined by intramolecular ionic interactions
    • Johnson, K. J., Sage, H., Briscoe, G., and Erickson, H. P. (1999) The compact conformation of fibronectin is determined by intramolecular ionic interactions. J. Biol. Chem. 274, 15473-15479
    • (1999) J. Biol. Chem. , vol.274 , pp. 15473-15479
    • Johnson, K.J.1    Sage, H.2    Briscoe, G.3    Erickson, H.P.4
  • 59
    • 0036790091 scopus 로고    scopus 로고
    • Mice lacking the EDB segment of fibronectin develop normally but exhibit reduced cell growth and fibronectin matrix assembly in vitro
    • Fukuda, T., Yoshida, N., Kataoka, Y., Manabe, R., Mizuno-Horikawa, Y., Sato, M., Kuriyama, K., Yasui, N., and Sekiguchi, K. (2002) Mice lacking the EDB segment of fibronectin develop normally but exhibit reduced cell growth and fibronectin matrix assembly in vitro. Cancer Res. 62, 5603-5610
    • (2002) Cancer Res. , vol.62 , pp. 5603-5610
    • Fukuda, T.1    Yoshida, N.2    Kataoka, Y.3    Manabe, R.4    Mizuno-Horikawa, Y.5    Sato, M.6    Kuriyama, K.7    Yasui, N.8    Sekiguchi, K.9
  • 60
    • 0032579376 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis involves the heparin II binding domain of fibronectin
    • DOI 10.1074/jbc.273.5.2601
    • Bultmann, H., Santas, A. J., and Peters, D. M. (1998) Fibronectin fibrillo-genesis involves the heparin II binding domain of fibronectin. J. Biol. Chem. 273, 2601-2609 (Pubitemid 28133901)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.5 , pp. 2601-2609
    • Bultmann, H.1    Santas, A.J.2    Pesciotta, P.D.M.3
  • 61
    • 0028364087 scopus 로고
    • Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin
    • Hocking, D. C., Sottile, J., and McKeown-Longo, P. J. (1994) Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin. J. Biol. Chem. 269, 19183-19187
    • (1994) J. Biol. Chem. , vol.269 , pp. 19183-19187
    • Hocking, D.C.1    Sottile, J.2    McKeown-Longo, P.J.3
  • 62
    • 77953566262 scopus 로고    scopus 로고
    • Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding
    • Graille, M., Pagano, M., Rose, T., Ravaux, M. R., and van Tilbeurgh, H. (2010) Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding. Structure 18, 710-718
    • (2010) Structure , vol.18 , pp. 710-718
    • Graille, M.1    Pagano, M.2    Rose, T.3    Ravaux, M.R.4    Van Tilbeurgh, H.5
  • 63
    • 33745271833 scopus 로고    scopus 로고
    • Role of fibronectin assembly in platelet thrombus formation
    • Cho, J., and Mosher, D. F. (2006) Role of fibronectin assembly in platelet thrombus formation. J. Thromb. Haemost. 4, 1461-1469
    • (2006) J. Thromb. Haemost. , vol.4 , pp. 1461-1469
    • Cho, J.1    Mosher, D.F.2
  • 64
    • 0023409308 scopus 로고
    • Multiple sites of alternative splicing of the rat fibronectin gene transcript
    • Schwarzbauer, J. E., Patel, R. S., Fonda, D., and Hynes, R. O. (1987) Multiple sites of alternative splicing of the rat fibronectin gene transcript. EMBO J. 6, 2573-2580
    • (1987) EMBO J. , vol.6 , pp. 2573-2580
    • Schwarzbauer, J.E.1    Patel, R.S.2    Fonda, D.3    Hynes, R.O.4
  • 66
    • 3042708208 scopus 로고    scopus 로고
    • Deletion of the alternatively spliced fibronectin EIIIA domain in mice reduces atherosclerosis
    • DOI 10.1182/blood-2003-09-3363
    • Tan, M. H., Sun, Z., Opitz, S. L., Schmidt, T. E., Peters, J. H., and George, E. L. (2004) Deletion of the alternatively spliced fibronectin EIIIA domain in mice reduces atherosclerosis. Blood 104, 11-18 (Pubitemid 38879830)
    • (2004) Blood , vol.104 , Issue.1 , pp. 11-18
    • Tan, M.H.1    Sun, Z.2    Opitz, S.L.3    Schmidt, T.E.4    Peters, J.H.5    George, E.L.6
  • 67
    • 35348890874 scopus 로고    scopus 로고
    • Multiple cardiovascular defects caused by the absence of alternatively spliced segments of fibronectin
    • DOI 10.1016/j.ydbio.2007.07.005, PII S0012160607011803
    • Astrof, S., Crowley, D., and Hynes, R. O. (2007) Multiple cardiovascular defects caused by the absence of alternatively spliced segments of fibronectin. Dev. Biol. 311, 11-24 (Pubitemid 47588228)
    • (2007) Developmental Biology , vol.311 , Issue.1 , pp. 11-24
    • Astrof, S.1    Crowley, D.2    Hynes, R.O.3
  • 68
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F. G., and Ruoslahti, E. (1999) Integrin signaling. Science 285, 1028-1032
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 71
    • 0033843942 scopus 로고    scopus 로고
    • Regulation of angiogenesis in vivo by ligation of integrin α5β1 with the central cell-binding domain of fibronectin
    • Kim, S., Bell, K., Mousa, S. A., and Varner, J. A. (2000) Regulation of angiogenesis in vivo by ligation of integrin α5β1 with the central cell-binding domain of fibronectin. Am. J. Pathol. 156, 1345-1362 (Pubitemid 30660012)
    • (2000) American Journal of Pathology , vol.156 , Issue.4 , pp. 1345-1362
    • Kim, S.1    Bell, K.2    Mousa, S.A.3    Varner, J.A.4
  • 72
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
    • DOI 10.1126/science.1069040
    • Xiong, J. P., Stehle, T., Zhang, R., Joachimiak, A., Frech, M., Goodman, S. L., and Arnaout, M. A. (2002) Crystal structure of the extracellular segment of integrin αvβ3 in complex with an Arg-Gly-Asp ligand. Science 296, 151-155 (Pubitemid 34280076)
    • (2002) Science , vol.296 , Issue.5565 , pp. 151-155
    • Xiong, J.-P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7


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