메뉴 건너뛰기




Volumn Part F2615, Issue , 2011, Pages 1-39

An Overview of Extracellular Matrix Structure and Function

Author keywords

Cartilage Oligomeric Matrix Protein; Domain Organization; Exon Shuffling; Multidomain Protein; Triple Helix

Indexed keywords


EID: 85194366689     PISSN: 08873224     EISSN: 21911959     Source Type: Book Series    
DOI: 10.1007/978-3-642-16555-9_1     Document Type: Chapter
Times cited : (23)

References (153)
  • 2
    • 46049083642 scopus 로고    scopus 로고
    • Bioinformatic analysis of adhesion proteins
    • Adams JC, Engel J (2007) Bioinformatic analysis of adhesion proteins. Methods Mol Biol 370:147–172
    • (2007) Methods Mol Biol , vol.370 , pp. 147-172
    • Adams, J.C.1    Engel, J.2
  • 4
    • 0027230170 scopus 로고
    • Regulation of development and differentiation by the extracellular matrix
    • Adams JC, Watt FM (1993) Regulation of development and differentiation by the extracellular matrix. Development 117:1183–1198
    • (1993) Development , vol.117 , pp. 1183-1198
    • Adams, J.C.1    Watt, F.M.2
  • 5
    • 0037466330 scopus 로고    scopus 로고
    • Characterisation of Drosophila thrombospondin defines an early origin of pentameric thrombospondins
    • Adams JC, Monk R, Taylor AL, Ozbek S, Fascetti N, Baumgartner S, Engel J (2003) Characterisation of Drosophila thrombospondin defines an early origin of pentameric thrombospondins. J Mol Biol 328:479–494
    • (2003) J Mol Biol , vol.328 , pp. 479-494
    • Adams, J.C.1    Monk, R.2    Taylor, A.L.3    Ozbek, S.4    Fascetti, N.5    Baumgartner, S.6    Engel, J.7
  • 6
    • 85194403025 scopus 로고    scopus 로고
    • Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002) Molecular biology of the cell, 4th edn. Garland Science, New York, Chapter 19
    • Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002) Molecular biology of the cell, 4th edn. Garland Science, New York, Chapter 19
  • 7
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics of integrin-based cell adhesion
    • Arnaout MA, Goodman SL, Xiong JP (2007) Structure and mechanics of integrin-based cell adhesion. Curr Opin Cell Biol 19:495–507
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 495-507
    • Arnaout, M.A.1    Goodman, S.L.2    Xiong, J.P.3
  • 8
    • 67650763823 scopus 로고    scopus 로고
    • Fibronectins in vascular morphogenesis
    • Astrof S, Hynes RO (2009) Fibronectins in vascular morphogenesis. Angiogenesis 12:165–175
    • (2009) Angiogenesis , vol.12 , pp. 165-175
    • Astrof, S.1    Hynes, R.O.2
  • 9
    • 19944380329 scopus 로고    scopus 로고
    • B€achinger HP, Engel J, Wiley-VHC, Hoboken, NJ
    • B€achinger HP, Engel J (eds) (2005) Protein folding handbook. Wiley-VHC, Hoboken, NJ
    • (2005) Protein Folding Handbook
  • 10
    • 0025705858 scopus 로고
    • Syndecan, a developmentally regulated cell surface proteoglycan that binds extracellular matrix and growth factors
    • Bernfield M, Sanderson RD (1990) Syndecan, a developmentally regulated cell surface proteoglycan that binds extracellular matrix and growth factors. Philos Trans R Soc Lond B Biol Sci 327:171–186
    • (1990) Philos Trans R Soc Lond B Biol Sci , vol.327 , pp. 171-186
    • Bernfield, M.1    Sanderson, R.D.2
  • 11
    • 33748309166 scopus 로고    scopus 로고
    • Adhesion-mediated mechanosensitivity: A time to experiment, and a time to theorize
    • Bershadsky A, Kozlov M, Geiger B (2006) Adhesion-mediated mechanosensitivity: a time to experiment, and a time to theorize. Curr Opin Cell Biol 18:472–481
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 472-481
    • Bershadsky, A.1    Kozlov, M.2    Geiger, B.3
  • 12
    • 0029777325 scopus 로고    scopus 로고
    • Structure and distribution of modules in extracellular proteins
    • Bork P, Downing AK, Kieffer B, Campbell ID (1996) Structure and distribution of modules in extracellular proteins. Q Rev Biophys 29:119–167
    • (1996) Q Rev Biophys , vol.29 , pp. 119-167
    • Bork, P.1    Downing, A.K.2    Kieffer, B.3    Campbell, I.D.4
  • 13
    • 69549130585 scopus 로고    scopus 로고
    • Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization fold
    • Boudko SP, Sasaki T, Engel J, Lerch TF, Nix J, Chapman MS, Bachinger HP (2009) Crystal structure of human collagen XVIII trimerization domain: a novel collagen trimerization fold. J Mol Biol 392:787–802
    • (2009) J Mol Biol , vol.392 , pp. 787-802
    • Boudko, S.P.1    Sasaki, T.2    Engel, J.3    Lerch, T.F.4    Nix, J.5    Chapman, M.S.6    Bachinger, H.P.7
  • 14
    • 0031440110 scopus 로고    scopus 로고
    • Genetic analysis of beta1 integrin function: Confirmed, new and revised roles for a crucial family of cell adhesion molecules
    • Brakebusch C, Hirsch E, Potocnik A, Fassler R (1997) Genetic analysis of beta1 integrin function: confirmed, new and revised roles for a crucial family of cell adhesion molecules. J Cell Sci 110 (Pt 23):2895–2904
    • (1997) J Cell Sci , vol.110 , Issue.23 , pp. 2895-2904
    • Brakebusch, C.1    Hirsch, E.2    Potocnik, A.3    Fassler, R.4
  • 15
    • 0036779358 scopus 로고    scopus 로고
    • Role of the extracellular matrix in cell-cell signalling: Paracrine paradigms
    • Brownlee C (2002) Role of the extracellular matrix in cell-cell signalling: paracrine paradigms. Curr Opin Plant Biol 5:396–401
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 396-401
    • Brownlee, C.1
  • 16
    • 0027321319 scopus 로고
    • A 60-kD protein mediates the binding of transforming growth factor-beta to cell surface and extracellular matrix proteoglycans
    • Butzow R, Fukushima D, Twardzik DR, Ruoslahti E (1993) A 60-kD protein mediates the binding of transforming growth factor-beta to cell surface and extracellular matrix proteoglycans. J Cell Biol 122:721–727
    • (1993) J Cell Biol , vol.122 , pp. 721-727
    • Butzow, R.1    Fukushima, D.2    Twardzik, D.R.3    Ruoslahti, E.4
  • 18
    • 44449174103 scopus 로고    scopus 로고
    • The mechanobiological effects of periosteal surface loads
    • Carpenter RD, Carter DR (2007) The mechanobiological effects of periosteal surface loads. Biomech Model Mechanobiol 7:227–242
    • (2007) Biomech Model Mechanobiol , vol.7 , pp. 227-242
    • Carpenter, R.D.1    Carter, D.R.2
  • 19
    • 56349169536 scopus 로고    scopus 로고
    • Mechanotransduction – a field pulling together?
    • Chen CS (2008) Mechanotransduction – a field pulling together? J Cell Sci 121:3285–3292
    • (2008) J Cell Sci , vol.121 , pp. 3285-3292
    • Chen, C.S.1
  • 20
    • 0024076043 scopus 로고
    • Attachment to an endogenous laminin-like protein initiates sprouting by leech neurons
    • Chiquet M, Masuda-Nakagawa L, Beck K (1988) Attachment to an endogenous laminin-like protein initiates sprouting by leech neurons. J Cell Biol 107:1189–1198
    • (1988) J Cell Biol , vol.107 , pp. 1189-1198
    • Chiquet, M.1    Masuda-Nakagawa, L.2    Beck, K.3
  • 21
    • 67349089040 scopus 로고    scopus 로고
    • From mechanotransduction to extracellular matrix gene expression in fibroblasts
    • Chiquet M, Gelman M, Lutz R, Maier S (2009) From mechanotransduction to extracellular matrix gene expression in fibroblasts. Biochim Biophys Acta 1793:911–920
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 911-920
    • Chiquet, M.1    Gelman, M.2    Lutz, R.3    Maier, S.4
  • 22
    • 0038236713 scopus 로고    scopus 로고
    • Tenascins: Regulation and putative functions during pathological stress
    • Chiquet-Ehrismann R, Chiquet M (2003) Tenascins: regulation and putative functions during pathological stress. J Pathol 200:488–499
    • (2003) J Pathol , vol.200 , pp. 488-499
    • Chiquet-Ehrismann, R.1    Chiquet, M.2
  • 24
    • 0026252643 scopus 로고
    • Tenascin variants: Differential binding to fibronectin and distinct distribution in cell cultures and tissues
    • Chiquet-Ehrismann R, Matsuoka Y, Hofer U, Spring J, Bernasconi C, Chiquet M (1991) Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues. Cell Regul 2:927–938
    • (1991) Cell Regul , vol.2 , pp. 927-938
    • Chiquet-Ehrismann, R.1    Matsuoka, Y.2    Hofer, U.3    Spring, J.4    Bernasconi, C.5    Chiquet, M.6
  • 25
    • 33745271833 scopus 로고    scopus 로고
    • Role of fibronectin assembly in platelet thrombus formation
    • Cho J, Mosher DF (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
  • 26
    • 0030994017 scopus 로고    scopus 로고
    • Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages
    • Choquet D, Felsenfeld DP, Sheetz MP (1997) Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages. Cell 88:39–48
    • (1997) Cell , vol.88 , pp. 39-48
    • Choquet, D.1    Felsenfeld, D.P.2    Sheetz, M.P.3
  • 27
    • 54049152026 scopus 로고    scopus 로고
    • The GPIIb/IIIa (integrin alphaIIbbeta3) odyssey: A technology-driven saga of a receptor with twists, turns, and even a bend
    • Coller BS, Shattil SJ (2008) The GPIIb/IIIa (integrin alphaIIbbeta3) odyssey: a technology-driven saga of a receptor with twists, turns, and even a bend. Blood 112:3011–3025
    • (2008) Blood , vol.112 , pp. 3011-3025
    • Coller, B.S.1    Shattil, S.J.2
  • 28
    • 33747749115 scopus 로고    scopus 로고
    • Darwin’s dilemma: The realities of the Cambrian ‘explosion’
    • Conway Morris S (2006) Darwin’s dilemma: the realities of the Cambrian ‘explosion’. Philos Trans R Soc Lond B Biol Sci 361:1069–1083
    • (2006) Philos Trans R Soc Lond B Biol Sci , vol.361 , pp. 1069-1083
    • Conway Morris, S.1
  • 29
    • 1642512352 scopus 로고    scopus 로고
    • The Cambrian “explosion” of metazoans and molecular biology: Would Darwin be satisfied?
    • Conway-Morris S (2003) The Cambrian “explosion” of metazoans and molecular biology: would Darwin be satisfied? Int J Dev Biol 47:505–515
    • (2003) Int J Dev Biol , vol.47 , pp. 505-515
    • Conway-Morris, S.1
  • 30
    • 73949132161 scopus 로고    scopus 로고
    • Segmentation, metamerism and the Cambrian explosion
    • Couso JP (2008) Segmentation, metamerism and the Cambrian explosion. Int J Dev Biol 53:1305–1316
    • (2008) Int J Dev Biol , vol.53 , pp. 1305-1316
    • Couso, J.P.1
  • 31
    • 33646358975 scopus 로고    scopus 로고
    • On the origin of pattern and form in early Metazoans
    • Cummings FW (2006) On the origin of pattern and form in early Metazoans. Int J Dev Biol 50:193–208
    • (2006) Int J Dev Biol , vol.50 , pp. 193-208
    • Cummings, F.W.1
  • 34
    • 0035839642 scopus 로고    scopus 로고
    • Real-time monitoring of the interactions of transforming growth factor-beta (TGF-beta ) isoforms with latency-associated protein and the ectodomains of the TGF-beta type II and III receptors reveals different kinetic models and stoichiometries of binding
    • De Crescenzo G, Grothe S, Zwaagstra J, Tsang M, O’Connor-McCourt MD (2001) Real-time monitoring of the interactions of transforming growth factor-beta (TGF-beta ) isoforms with latency-associated protein and the ectodomains of the TGF-beta type II and III receptors reveals different kinetic models and stoichiometries of binding. J Biol Chem 276:29632–29643
    • (2001) J Biol Chem , vol.276 , pp. 29632-29643
    • de Crescenzo, G.1    Grothe, S.2    Zwaagstra, J.3    Tsang, M.4    O’connor-McCourt, M.D.5
  • 35
    • 33846309701 scopus 로고    scopus 로고
    • Integrins and the actin cytoskeleton
    • Delon I, Brown NH (2007) Integrins and the actin cytoskeleton. Curr Opin Cell Biol 19:43–50
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 43-50
    • Delon, I.1    Brown, N.H.2
  • 36
    • 0034773348 scopus 로고    scopus 로고
    • Building the wall: Genes and enzyme complexes for polysaccharide synthases
    • Dhugga KS (2001) Building the wall: genes and enzyme complexes for polysaccharide synthases. Curr Opin Plant Biol 4:488–493
    • (2001) Curr Opin Plant Biol , vol.4 , pp. 488-493
    • Dhugga, K.S.1
  • 37
    • 0026817136 scopus 로고
    • Stein and Moore Award address. Reconstructing history with amino acid sequences
    • Doolittle RF (1992) Stein and Moore Award address. Reconstructing history with amino acid sequences. Protein Sci 1:191–200
    • (1992) Protein Sci , vol.1 , pp. 191-200
    • Doolittle, R.F.1
  • 39
    • 0026442649 scopus 로고
    • Laminins and other strange proteins
    • Engel J (1992) Laminins and other strange proteins. Biochemistry 31:10643–10651
    • (1992) Biochemistry , vol.31 , pp. 10643-10651
    • Engel, J.1
  • 40
    • 0028936928 scopus 로고
    • Electron microscopy of extracellular matrix components
    • Engel J (1994) Electron microscopy of extracellular matrix components. Methods Enzymol 245:469–488
    • (1994) Methods Enzymol , vol.245 , pp. 469-488
    • Engel, J.1
  • 41
    • 0030865343 scopus 로고    scopus 로고
    • Versatile collagens in invertebrates
    • Engel J (1997) Versatile collagens in invertebrates. Science 277:1785–1786
    • (1997) Science , vol.277 , pp. 1785-1786
    • Engel, J.1
  • 42
    • 33845322660 scopus 로고    scopus 로고
    • Visions for novel biophysical elucidations of extracellular matrix networks
    • Engel J (2007) Visions for novel biophysical elucidations of extracellular matrix networks. Int J Biochem Cell Biol 39:311–318
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 311-318
    • Engel, J.1
  • 43
    • 0019888221 scopus 로고
    • Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix
    • Engel J, Odermatt E, Engel A, Madri JA, Furthmayr H, Rohde H, Timpl R (1981) Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix. J Mol Biol 150:97–120
    • (1981) J Mol Biol , vol.150 , pp. 97-120
    • Engel, J.1    Odermatt, E.2    Engel, A.3    Madri, J.A.4    Furthmayr, H.5    Rohde, H.6    Timpl, R.7
  • 44
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • Engler AJ, Sen S, Sweeney HL, Discher DE (2006) Matrix elasticity directs stem cell lineage specification. Cell 126:677–689
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 45
    • 0034233877 scopus 로고    scopus 로고
    • Tracing the evolution of vertebrate fibrillar collagens from an ancestral alpha chain
    • Exposito J, Cluzel C, Lethias C, Garrone R (2000) Tracing the evolution of vertebrate fibrillar collagens from an ancestral alpha chain. Matrix Biol 19:275–279
    • (2000) Matrix Biol , vol.19 , pp. 275-279
    • Exposito, J.1    Cluzel, C.2    Lethias, C.3    Garrone, R.4
  • 47
    • 57649133947 scopus 로고    scopus 로고
    • Demosponge and sea anemone fibrillar collagen diversity reveals the early emergence of A/C clades and the maintenance of the modular structure of type V/XI collagens from sponge to human
    • Exposito JY, Larroux C, Cluzel C, Valcourt U, Lethias C, Degnan BM (2008) Demosponge and sea anemone fibrillar collagen diversity reveals the early emergence of A/C clades and the maintenance of the modular structure of type V/XI collagens from sponge to human. J Biol Chem 283:28226–28235
    • (2008) J Biol Chem , vol.283 , pp. 28226-28235
    • Exposito, J.Y.1    Larroux, C.2    Cluzel, C.3    Valcourt, U.4    Lethias, C.5    Degnan, B.M.6
  • 48
    • 33744471138 scopus 로고    scopus 로고
    • New avenues in protein function prediction
    • Friedberg I, Jambon M, Godzik A (2006) New avenues in protein function prediction. Protein Sci 15:1527–1529
    • (2006) Protein Sci , vol.15 , pp. 1527-1529
    • Friedberg, I.1    Jambon, M.2    Godzik, A.3
  • 50
    • 0036829981 scopus 로고    scopus 로고
    • Origin of multicellular organisms as an inevitable consequence of dynamical systems
    • Furusawa C, Kaneko K (2002) Origin of multicellular organisms as an inevitable consequence of dynamical systems. Anat Rec 268:327–342
    • (2002) Anat Rec , vol.268 , pp. 327-342
    • Furusawa, C.1    Kaneko, K.2
  • 51
    • 0028897167 scopus 로고
    • Acetylcholine receptor-aggregating activity of agrin isoforms and mapping of the active site
    • Gesemann M, Denzer AJ, Ruegg MA (1995) Acetylcholine receptor-aggregating activity of agrin isoforms and mapping of the active site. J Cell Biol 128:625–636
    • (1995) J Cell Biol , vol.128 , pp. 625-636
    • Gesemann, M.1    Denzer, A.J.2    Ruegg, M.A.3
  • 57
    • 0141595014 scopus 로고    scopus 로고
    • Extracellular matrix and sex-inducing pheromone in Volvox
    • Hallmann A (2003) Extracellular matrix and sex-inducing pheromone in Volvox. Int Rev Cytol 227:131–182
    • (2003) Int Rev Cytol , vol.227 , pp. 131-182
    • Hallmann, A.1
  • 61
    • 0036166823 scopus 로고    scopus 로고
    • Domain structure and organisation in extracellular matrix proteins
    • Hohenester E, Engel J (2002) Domain structure and organisation in extracellular matrix proteins. Matrix Biol 21:115–128
    • (2002) Matrix Biol , vol.21 , pp. 115-128
    • Hohenester, E.1    Engel, J.2
  • 62
    • 33745433344 scopus 로고    scopus 로고
    • Interaction of the guidance molecule slit with cellular receptors
    • Hohenester E, Hussain S, Howitt JA (2006) Interaction of the guidance molecule slit with cellular receptors. Biochem Soc Trans 34:418–421
    • (2006) Biochem Soc Trans , vol.34 , pp. 418-421
    • Hohenester, E.1    Hussain, S.2    Howitt, J.A.3
  • 64
    • 0022168434 scopus 로고
    • Molecular biology of fibronectin
    • Hynes R (1985) Molecular biology of fibronectin. Annu Rev Cell Biol 1:67–90
    • (1985) Annu Rev Cell Biol , vol.1 , pp. 67-90
    • Hynes, R.1
  • 65
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110:673–687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 66
    • 0034710157 scopus 로고    scopus 로고
    • The evolution of cell adhesion
    • Hynes RO, Zhao Q (2000) The evolution of cell adhesion. J Cell Biol 150:89–96
    • (2000) J Cell Biol , vol.150 , pp. 89-96
    • Hynes, R.O.1    Zhao, Q.2
  • 67
    • 33646340966 scopus 로고    scopus 로고
    • Mechanical control of tissue morphogenesis during embryological development
    • Ingber DE (2006) Mechanical control of tissue morphogenesis during embryological development. Int J Dev Biol 50:255–266
    • (2006) Int J Dev Biol , vol.50 , pp. 255-266
    • Ingber, D.E.1
  • 68
    • 50849145156 scopus 로고    scopus 로고
    • Collagen fibrillogenesis: Fibronectin, integrins, and minor collagens as organizers and nucleators
    • Kadler KE, Hill A, Canty-Laird EG (2008) Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators. Curr Opin Cell Biol 20:495–501
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 495-501
    • Kadler, K.E.1    Hill, A.2    Canty-Laird, E.G.3
  • 69
    • 0036851263 scopus 로고    scopus 로고
    • Signatures of domain shuffling in the human genome
    • Kaessmann H, Zollner S, Nekrutenko A, Li WH (2002) Signatures of domain shuffling in the human genome. Genome Res 12:1642–1650
    • (2002) Genome Res , vol.12 , pp. 1642-1650
    • Kaessmann, H.1    Zollner, S.2    Nekrutenko, A.3    Li, W.H.4
  • 70
    • 0025834976 scopus 로고
    • Differential regulation of extracellular matrix proteoglycan (PG) gene expression. Transforming growth factor-beta 1 up-regulates biglycan (PGI), and versican (large fibroblast PG) but down-regulates decorin (PGII) mRNA levels in human fibroblasts in culture
    • Kahari VM, Larjava H, Uitto J (1991a) Differential regulation of extracellular matrix proteoglycan (PG) gene expression. Transforming growth factor-beta 1 up-regulates biglycan (PGI), and versican (large fibroblast PG) but down-regulates decorin (PGII) mRNA levels in human fibroblasts in culture. J Biol Chem 266:10608–10615
    • (1991) J Biol Chem , vol.266 , pp. 10608-10615
    • Kahari, V.M.1    Larjava, H.2    Uitto, J.3
  • 71
    • 0025807907 scopus 로고
    • Differential modulation of basement membrane gene expression in human fibrosarcoma HT-1080 cells by transforming growth factor-beta 1. Enhanced type IV collagen and fibronectin gene expression correlates with altered culture phenotype of the cells
    • Kahari VM, Peltonen J, Chen YQ, Uitto J (1991b) Differential modulation of basement membrane gene expression in human fibrosarcoma HT-1080 cells by transforming growth factor-beta 1. Enhanced type IV collagen and fibronectin gene expression correlates with altered culture phenotype of the cells. Lab Invest 64:807–818
    • (1991) Lab Invest , vol.64 , pp. 807-818
    • Kahari, V.M.1    Peltonen, J.2    Chen, Y.Q.3    Uitto, J.4
  • 72
    • 0141763800 scopus 로고    scopus 로고
    • Roles of lumican and keratocan on corneal transparency
    • Kao WW, Liu CY (2002) Roles of lumican and keratocan on corneal transparency. Glycoconj J 19:275–285
    • (2002) Glycoconj J , vol.19 , pp. 275-285
    • Kao, W.W.1    Liu, C.Y.2
  • 74
    • 0033577911 scopus 로고    scopus 로고
    • Molecular evolution of immunoglobulin and fibronectin domains in titin and related muscle proteins
    • Kenny PA, Liston EM, Higgins DG (1999) Molecular evolution of immunoglobulin and fibronectin domains in titin and related muscle proteins. Gene 232:11–23
    • (1999) Gene , vol.232 , pp. 11-23
    • Kenny, P.A.1    Liston, E.M.2    Higgins, D.G.3
  • 76
    • 1642313674 scopus 로고    scopus 로고
    • Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading
    • Kjaer M (2004) Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading. Physiol Rev 84:649–698
    • (2004) Physiol Rev , vol.84 , pp. 649-698
    • Kjaer, M.1
  • 77
    • 0034003019 scopus 로고    scopus 로고
    • Control of extracellular matrix assembly by syndecan 2 proteoglycan
    • Klass CM, Couchman JR, Woods A (2000) Control of extracellular matrix assembly by syndecan 2 proteoglycan. J Cell Sci 113(Pt 3):493–506
    • (2000) J Cell Sci , vol.113 , Issue.3 , pp. 493-506
    • Klass, C.M.1    Couchman, J.R.2    Woods, A.3
  • 78
    • 0026716529 scopus 로고
    • A major oligomeric fibroblast proteoglycan identified as a novel large form of type-XII collagen
    • Koch M, Bernasconi C, Chiquet M (1992) A major oligomeric fibroblast proteoglycan identified as a novel large form of type-XII collagen. Eur J Biochem 207:847–856
    • (1992) Eur J Biochem , vol.207 , pp. 847-856
    • Koch, M.1    Bernasconi, C.2    Chiquet, M.3
  • 79
    • 0029093272 scopus 로고
    • Large and small splice variants of collagen XII: Differential expression and ligand binding
    • Koch M, Bohrmann B, Matthison M, Hagios C, Trueb B, Chiquet M (1995) Large and small splice variants of collagen XII: differential expression and ligand binding. J Cell Biol 130:1005–1014
    • (1995) J Cell Biol , vol.130 , pp. 1005-1014
    • Koch, M.1    Bohrmann, B.2    Matthison, M.3    Hagios, C.4    Trueb, B.5    Chiquet, M.6
  • 80
    • 0029893254 scopus 로고    scopus 로고
    • Conversion of the Kunitz-type module of collagen VI into a highly active trypsin inhibitor by site-directed mutagenesis
    • Kohfeldt E, Gohring W, Mayer U, Zweckstetter M, Holak TA, Chu ML, Timpl R (1996) Conversion of the Kunitz-type module of collagen VI into a highly active trypsin inhibitor by site-directed mutagenesis. Eur J Biochem 238:333–340
    • (1996) Eur J Biochem , vol.238 , pp. 333-340
    • Kohfeldt, E.1    Gohring, W.2    Mayer, U.3    Zweckstetter, M.4    Holak, T.A.5    Chu, M.L.6    Timpl, R.7
  • 81
    • 67649598285 scopus 로고    scopus 로고
    • Demonstration of catch bonds between an integrin and its ligand
    • Kong F, Garcia AJ, Mould AP, Humphries MJ, Zhu C (2009) Demonstration of catch bonds between an integrin and its ligand. J Cell Biol 185:1275–1284
    • (2009) J Cell Biol , vol.185 , pp. 1275-1284
    • Kong, F.1    Garcia, A.J.2    Mould, A.P.3    Humphries, M.J.4    Zhu, C.5
  • 82
    • 0035168796 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular matrix and growth control
    • Kresse H, Schonherr E (2001) Proteoglycans of the extracellular matrix and growth control. J Cell Physiol 189:266–274
    • (2001) J Cell Physiol , vol.189 , pp. 266-274
    • Kresse, H.1    Schonherr, E.2
  • 83
    • 0035476687 scopus 로고    scopus 로고
    • Structural basis for the high-affinity interaction of nidogen-1 with immunoglobulin-like domain 3 of perlecan
    • Kvansakul M, Hopf M, Ries A, Timpl R, Hohenester E (2001) Structural basis for the high-affinity interaction of nidogen-1 with immunoglobulin-like domain 3 of perlecan. EMBO J 20:5342–5346
    • (2001) EMBO J , vol.20 , pp. 5342-5346
    • Kvansakul, M.1    Hopf, M.2    Ries, A.3    Timpl, R.4    Hohenester, E.5
  • 84
    • 1942535754 scopus 로고    scopus 로고
    • Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats
    • Kvansakul M, Adams JC, Hohenester E (2004) Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats. EMBO J 23:1223–1233
    • (2004) EMBO J , vol.23 , pp. 1223-1233
    • Kvansakul, M.1    Adams, J.C.2    Hohenester, E.3
  • 86
    • 33947109970 scopus 로고    scopus 로고
    • Mammalian collagen receptors
    • Leitinger B, Hohenester E (2007) Mammalian collagen receptors. Matrix Biol 26:146–155
    • (2007) Matrix Biol , vol.26 , pp. 146-155
    • Leitinger, B.1    Hohenester, E.2
  • 88
    • 0029911261 scopus 로고    scopus 로고
    • The crystal structure of a five-stranded coiled coil in COMP: A prototype ion channel?
    • Malashkevich VN, Kammerer RA, Efimov VP, Schulthess T, Engel J (1996) The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel? Science 274:761–765
    • (1996) Science , vol.274 , pp. 761-765
    • Malashkevich, V.N.1    Kammerer, R.A.2    Efimov, V.P.3    Schulthess, T.4    Engel, J.5
  • 89
  • 90
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell-mediated matrix assembly process
    • Mao Y, Schwarzbauer JE (2005) Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix Biol 24:389–399
    • (2005) Matrix Biol , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 92
    • 0028072632 scopus 로고
    • Recombinant expression and properties of the Kunitz-type protease-inhibitor module from human type VI collagen alpha 3(VI) chain
    • Mayer U, Poschl E, Nischt R, Specks U, Pan TC, Chu ML, Timpl R (1994) Recombinant expression and properties of the Kunitz-type protease-inhibitor module from human type VI collagen alpha 3(VI) chain. Eur J Biochem 225:573–580
    • (1994) Eur J Biochem , vol.225 , pp. 573-580
    • Mayer, U.1    Poschl, E.2    Nischt, R.3    Specks, U.4    Pan, T.C.5    Chu, M.L.6    Timpl, R.7
  • 93
    • 0030957797 scopus 로고    scopus 로고
    • Drosophila laminin binds to mammalian nidogen and to heparan sulfate proteoglycan
    • Mayer U, Mann K, Fessler LI, Fessler JH, Timpl R (1997a) Drosophila laminin binds to mammalian nidogen and to heparan sulfate proteoglycan. Eur J Biochem 245:745–750
    • (1997) Eur J Biochem , vol.245 , pp. 745-750
    • Mayer, U.1    Mann, K.2    Fessler, L.I.3    Fessler, J.H.4    Timpl, R.5
  • 95
    • 0142211233 scopus 로고    scopus 로고
    • Alpha-helical coiled-coil oligomerization domains are almost ubiquitous in the collagen superfamily
    • McAlinden A, Smith TA, Sandell LJ, Ficheux D, Parry DA, Hulmes DJ (2003) Alpha-helical coiled-coil oligomerization domains are almost ubiquitous in the collagen superfamily. J Biol Chem 278:42200–42207
    • (2003) J Biol Chem , vol.278 , pp. 42200-42207
    • McAlinden, A.1    Smith, T.A.2    Sandell, L.J.3    Ficheux, D.4    Parry, D.A.5    Hulmes, D.J.6
  • 96
    • 33646771386 scopus 로고    scopus 로고
    • Phylogenomic analysis of vertebrate thrombospondins reveals fish-specific paralogues, ancestral gene relationships and a tetrapod innovation
    • McKenzie P, Chadalavada SC, Bohrer J, Adams JC (2006) Phylogenomic analysis of vertebrate thrombospondins reveals fish-specific paralogues, ancestral gene relationships and a tetrapod innovation. BMC Evol Biol 6:33
    • (2006) BMC Evol Biol , vol.6
    • McKenzie, P.1    Chadalavada, S.C.2    Bohrer, J.3    Adams, J.C.4
  • 97
    • 13944265302 scopus 로고    scopus 로고
    • Basic mechanism of three-dimensional collagen fibre transport by fibroblasts
    • Meshel AS, Wei Q, Adelstein RS, Sheetz MP (2005) Basic mechanism of three-dimensional collagen fibre transport by fibroblasts. Nat Cell Biol 7:157–164
    • (2005) Nat Cell Biol , vol.7 , pp. 157-164
    • Meshel, A.S.1    Wei, Q.2    Adelstein, R.S.3    Sheetz, M.P.4
  • 98
    • 9444297917 scopus 로고    scopus 로고
    • Coregulation of fibronectin signaling and matrix contraction by tenascin-C and syndecan-4
    • Midwood KS, Valenick LV, Hsia HC, Schwarzbauer JE (2004) Coregulation of fibronectin signaling and matrix contraction by tenascin-C and syndecan-4. Mol Biol Cell 15:5670–5677
    • (2004) Mol Biol Cell , vol.15 , pp. 5670-5677
    • Midwood, K.S.1    Valenick, L.V.2    Hsia, H.C.3    Schwarzbauer, J.E.4
  • 99
    • 0026701960 scopus 로고
    • Retention of the transforming growth factor-beta 1 precursor in the Golgi complex in a latent endoglycosidase H-sensitive form
    • Miyazono K, Thyberg J, Heldin CH (1992) Retention of the transforming growth factor-beta 1 precursor in the Golgi complex in a latent endoglycosidase H-sensitive form. J Biol Chem 267:5668–5675
    • (1992) J Biol Chem , vol.267 , pp. 5668-5675
    • Miyazono, K.1    Thyberg, J.2    Heldin, C.H.3
  • 100
    • 0026703257 scopus 로고
    • Electron microscopy of native cartilage oligomeric matrix protein purified from the Swarm rat chondrosarcoma reveals a five-armed structure
    • Morgelin M, Heinegard D, Engel J, Paulsson M (1992) Electron microscopy of native cartilage oligomeric matrix protein purified from the Swarm rat chondrosarcoma reveals a five-armed structure. J Biol Chem 267:6137–6141
    • (1992) J Biol Chem , vol.267 , pp. 6137-6141
    • Morgelin, M.1    Heinegard, D.2    Engel, J.3    Paulsson, M.4
  • 103
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • Myllyharju J, Kivirikko KI (2004) Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet 20:33–43
    • (2004) Trends Genet , vol.20 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 104
    • 22244450719 scopus 로고    scopus 로고
    • Protein families and their evolution-a structural perspective
    • Orengo CA, Thornton JM (2005) Protein families and their evolution-a structural perspective. Annu Rev Biochem 74:867–900
    • (2005) Annu Rev Biochem , vol.74 , pp. 867-900
    • Orengo, C.A.1    Thornton, J.M.2
  • 105
    • 51349107479 scopus 로고    scopus 로고
    • Fifty years of coiled-coils and alpha-helical bundles: A close relationship between sequence and structure
    • Parry DA, Fraser RD, Squire JM (2008) Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure. J Struct Biol 163:258–269
    • (2008) J Struct Biol , vol.163 , pp. 258-269
    • Parry, D.A.1    Fraser, R.D.2    Squire, J.M.3
  • 106
    • 0038306145 scopus 로고    scopus 로고
    • Modular assembly of genes and the evolution of new functions
    • Patthy L (2003) Modular assembly of genes and the evolution of new functions. Genetica 118:217–231
    • (2003) Genetica , vol.118 , pp. 217-231
    • Patthy, L.1
  • 107
    • 0023660965 scopus 로고
    • Structure of low density heparan sulfate proteoglycan isolated from a mouse tumor basement membrane
    • Paulsson M, Yurchenco PD, Ruben GC, Engel J, Timpl R (1987) Structure of low density heparan sulfate proteoglycan isolated from a mouse tumor basement membrane. J Mol Biol 197:297–313
    • (1987) J Mol Biol , vol.197 , pp. 297-313
    • Paulsson, M.1    Yurchenco, P.D.2    Ruben, G.C.3    Engel, J.4    Timpl, R.5
  • 108
    • 21444453832 scopus 로고    scopus 로고
    • Prediction of collagen stability from amino acid sequence
    • Persikov AV, Ramshaw JA, Brodsky B (2005) Prediction of collagen stability from amino acid sequence. J Biol Chem 280:19343–19349
    • (2005) J Biol Chem , vol.280 , pp. 19343-19349
    • Persikov, A.V.1    Ramshaw, J.A.2    Brodsky, B.3
  • 109
    • 0035794672 scopus 로고    scopus 로고
    • The hairpin structure of the (6) F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding
    • Pickford AR, Smith SP, Staunton D, Boyd J, Campbell ID (2001) The hairpin structure of the (6) F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. EMBO J 20:1519–1529
    • (2001) EMBO J , vol.20 , pp. 1519-1529
    • Pickford, A.R.1    Smith, S.P.2    Staunton, D.3    Boyd, J.4    Campbell, I.D.5
  • 110
    • 0030298383 scopus 로고    scopus 로고
    • Structure and function of fibronectin modules
    • Potts JR, Campbell ID (1996) Structure and function of fibronectin modules. Matrix Biol 15:313–320
    • (1996) Matrix Biol , vol.15 , pp. 313-320
    • Potts, J.R.1    Campbell, I.D.2
  • 111
    • 66149129195 scopus 로고    scopus 로고
    • Glycosaminoglycan characterization methodologies: Probing biomolecular interactions
    • Prabhakar V, Capila I, Sasisekharan R (2009) Glycosaminoglycan characterization methodologies: probing biomolecular interactions. Methods Mol Biol 534:331–340
    • (2009) Methods Mol Biol , vol.534 , pp. 331-340
    • Prabhakar, V.1    Capila, I.2    Sasisekharan, R.3
  • 112
    • 67649354634 scopus 로고    scopus 로고
    • Extracellular microfibrils in vertebrate development and disease processes
    • Ramirez F, Dietz HC (2009) Extracellular microfibrils in vertebrate development and disease processes. J Biol Chem 284:14677–14681
    • (2009) J Biol Chem , vol.284 , pp. 14677-14681
    • Ramirez, F.1    Dietz, H.C.2
  • 113
    • 70349325817 scopus 로고    scopus 로고
    • Extracellular microfibrils: Contextual platforms for TGFbeta and BMP signaling
    • Ramirez F, Rifkin DB (2009) Extracellular microfibrils: contextual platforms for TGFbeta and BMP signaling. Curr Opin Cell Biol 21:616–622
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 616-622
    • Ramirez, F.1    Rifkin, D.B.2
  • 114
    • 27644484968 scopus 로고    scopus 로고
    • Clinging to life: Cell to matrix adhesion and cell survival
    • Reddig PJ, Juliano RL (2005) Clinging to life: cell to matrix adhesion and cell survival. Cancer Metastasis Rev 24:425–439
    • (2005) Cancer Metastasis Rev , vol.24 , pp. 425-439
    • Reddig, P.J.1    Juliano, R.L.2
  • 115
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism
    • Riveline D, Zamir E, Balaban NQ, Schwarz US, Ishizaki T, Narumiya S, Kam Z, Geiger B, Bershadsky AD (2001) Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism. J Cell Biol 153:1175–1186
    • (2001) J Cell Biol , vol.153 , pp. 1175-1186
    • Riveline, D.1    Zamir, E.2    Balaban, N.Q.3    Schwarz, U.S.4    Ishizaki, T.5    Narumiya, S.6    Kam, Z.7    Geiger, B.8    Bershadsky, A.D.9
  • 118
    • 0033840527 scopus 로고    scopus 로고
    • Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGFbeta
    • Saharinen J, Keski-Oja J (2000) Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGFbeta. Mol Biol Cell 11:2691–2704
    • (2000) Mol Biol Cell , vol.11 , pp. 2691-2704
    • Saharinen, J.1    Keski-Oja, J.2
  • 120
    • 19544373776 scopus 로고    scopus 로고
    • Multicellularity, stem cells, and the neoblasts of the planarian Schmidtea mediterranea
    • Sanchez Alvarado A, Kang H (2005) Multicellularity, stem cells, and the neoblasts of the planarian Schmidtea mediterranea. Exp Cell Res 306:299–308
    • (2005) Exp Cell Res , vol.306 , pp. 299-308
    • Sanchez Alvarado, A.1    Kang, H.2
  • 124
    • 0032570809 scopus 로고    scopus 로고
    • Mechanical stressing of integrin receptors induces enhanced tyrosine phosphorylation of cytoskeletally anchored proteins
    • Schmidt C, Pommerenke H, Durr F, Nebe B, Rychly J (1998) Mechanical stressing of integrin receptors induces enhanced tyrosine phosphorylation of cytoskeletally anchored proteins. J Biol Chem 273:5081–5085
    • (1998) J Biol Chem , vol.273 , pp. 5081-5085
    • Schmidt, C.1    Pommerenke, H.2    Durr, F.3    Nebe, B.4    Rychly, J.5
  • 126
    • 48449097540 scopus 로고    scopus 로고
    • A new model for growth factor activation: Type II receptors compete with the prodomain for BMP-7
    • Sengle G, Ono RN, Lyons KM, Bachinger HP, Sakai LY (2008b) A new model for growth factor activation: type II receptors compete with the prodomain for BMP-7. J Mol Biol 381:1025–1039
    • (2008) J Mol Biol , vol.381 , pp. 1025-1039
    • Sengle, G.1    Ono, R.N.2    Lyons, K.M.3    Bachinger, H.P.4    Sakai, L.Y.5
  • 127
    • 0024347096 scopus 로고
    • Two contrary functions of tenascin: Dissection of the active sites by recombinant tenascin fragments
    • Spring J, Beck K, Chiquet-Ehrismann R (1989) Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments. Cell 59:325–334
    • (1989) Cell , vol.59 , pp. 325-334
    • Spring, J.1    Beck, K.2    Chiquet-Ehrismann, R.3
  • 129
    • 35548939067 scopus 로고    scopus 로고
    • Structural basis for ligand recognition by integrins
    • Takagi J (2007) Structural basis for ligand recognition by integrins. Curr Opin Cell Biol 19:557–564
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 557-564
    • Takagi, J.1
  • 130
    • 7744232293 scopus 로고    scopus 로고
    • Activation of a signaling cascade by cytoskeleton stretch
    • Tamada M, Sheetz MP, Sawada Y (2004) Activation of a signaling cascade by cytoskeleton stretch. Dev Cell 7:709–718
    • (2004) Dev Cell , vol.7 , pp. 709-718
    • Tamada, M.1    Sheetz, M.P.2    Sawada, Y.3
  • 131
    • 0032978988 scopus 로고    scopus 로고
    • ADAMTS: A novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats
    • Tang BL, Hong W (1999) ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats. FEBS Lett 445:223–225
    • (1999) FEBS Lett , vol.445 , pp. 223-225
    • Tang, B.L.1    Hong, W.2
  • 132
    • 18344390410 scopus 로고    scopus 로고
    • The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link
    • Than ME, Henrich S, Huber R, Ries A, Mann K, Kuhn K, Timpl R, Bourenkov GP, Bartunik HD, Bode W (2002) The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link. Proc Natl Acad Sci USA 99:6607–6612
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6607-6612
    • Than, M.E.1    Henrich, S.2    Huber, R.3    Ries, A.4    Mann, K.5    Kuhn, K.6    Timpl, R.7    Bourenkov, G.P.8    Bartunik, H.D.9    Bode, W.10
  • 133
    • 34347383963 scopus 로고    scopus 로고
    • Protein evolution constraints and model-based techniques to study them
    • Thorne JL (2007) Protein evolution constraints and model-based techniques to study them. Curr Opin Struct Biol 17:337–341
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 337-341
    • Thorne, J.L.1
  • 134
    • 56949084574 scopus 로고    scopus 로고
    • Evidence for the evolution of tenascin and fibronectin early in the chordate lineage
    • Tucker RP, Chiquet-Ehrismann R (2009) Evidence for the evolution of tenascin and fibronectin early in the chordate lineage. Int J Biochem Cell Biol 41:424–434
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 424-434
    • Tucker, R.P.1    Chiquet-Ehrismann, R.2
  • 136
    • 0035182916 scopus 로고    scopus 로고
    • Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability
    • Vitagliano L, Berisio R, Mastrangelo A, Mazzarella L, Zagari A (2001) Preferred proline puckerings in cis and trans peptide groups: implications for collagen stability. Protein Sci 10:2627–2632
    • (2001) Protein Sci , vol.10 , pp. 2627-2632
    • Vitagliano, L.1    Berisio, R.2    Mastrangelo, A.3    Mazzarella, L.4    Zagari, A.5
  • 137
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • Vogel V, Sheetz M (2006) Local force and geometry sensing regulate cell functions. Nat Rev Mol Cell Biol 7:265–275
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 139
    • 12344261833 scopus 로고    scopus 로고
    • The relationship between domain duplication and recombination
    • Vogel C, Teichmann SA, Pereira-Leal J (2005) The relationship between domain duplication and recombination. J Mol Biol 346:355–365
    • (2005) J Mol Biol , vol.346 , pp. 355-365
    • Vogel, C.1    Teichmann, S.A.2    Pereira-Leal, J.3
  • 141
    • 67650875881 scopus 로고    scopus 로고
    • Vascular extracellular matrix and arteria mechanics
    • Wagenseil JE, Mecham RP (2009) Vascular extracellular matrix and arteria mechanics. Physiol Rev 89:957–989
    • (2009) Physiol Rev , vol.89 , pp. 957-989
    • Wagenseil, J.E.1    Mecham, R.P.2
  • 142
    • 6344256567 scopus 로고    scopus 로고
    • The biochemical response of the heart to hypertension and exercise
    • Wakatsuki T, Schlessinger J, Elson EL (2004) The biochemical response of the heart to hypertension and exercise. Trends Biochem Sci 29:609–617
    • (2004) Trends Biochem Sci , vol.29 , pp. 609-617
    • Wakatsuki, T.1    Schlessinger, J.2    Elson, E.L.3
  • 145
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • Xiao T, Takagi J, Coller BS, Wang JH, Springer TA (2004) Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature 432:59–67
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    Coller, B.S.3    Wang, J.H.4    Springer, T.A.5
  • 146
    • 33745394130 scopus 로고    scopus 로고
    • Alternative splicing and RNA selection pressure–evolutionary consequences for eukaryotic genomes
    • Xing Y, Lee C (2006) Alternative splicing and RNA selection pressure–evolutionary consequences for eukaryotic genomes. Nat Rev Genet 7:499–509
    • (2006) Nat Rev Genet , vol.7 , pp. 499-509
    • Xing, Y.1    Lee, C.2
  • 149
    • 0019126260 scopus 로고
    • The collagen gene: Evidence for its evolutinary assembly by amplification of a DNA segment containing an exon of 54 bp
    • Yamada Y, Avvedimento VE, Mudryj M, Ohkubo H, Vogeli G, Irani M, Pastan I, de Crombrugghe B (1980) The collagen gene: evidence for its evolutinary assembly by amplification of a DNA segment containing an exon of 54 bp. Cell 22:887–892
    • (1980) Cell , vol.22 , pp. 887-892
    • Yamada, Y.1    Avvedimento, V.E.2    Mudryj, M.3    Ohkubo, H.4    Vogeli, G.5    Irani, M.6    Pastan, I.7    de Crombrugghe, B.8
  • 150
    • 1442310569 scopus 로고    scopus 로고
    • Basement membrane assembly, stability and activities observed through a developmental lens
    • Yurchenco PD, Amenta PS, Patton BL (2004) Basement membrane assembly, stability and activities observed through a developmental lens. Matrix Biol 22:521–538
    • (2004) Matrix Biol , vol.22 , pp. 521-538
    • Yurchenco, P.D.1    Amenta, P.S.2    Patton, B.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.