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Volumn , Issue , 2012, Pages 592-602

Collagen-binding proteins

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EID: 84957841715     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (1)

References (55)
  • 1
    • 79952489518 scopus 로고    scopus 로고
    • Exome sequencing identifies truncating mutations in human SERPNF1 in autosomal-recessive osteogenesis imperfecta
    • Becker, J., Semler, O., Gilissen, C., et al. (2011). Exome sequencing identifies truncating mutations in human SERPNF1 in autosomal-recessive osteogenesis imperfecta. Am J Hum Genet 88, 362-371.
    • (2011) Am J Hum Genet , vol.88 , pp. 362-371
    • Becker, J.1    Semler, O.2    Gilissen, C.3
  • 2
    • 0035234139 scopus 로고    scopus 로고
    • SPARC, a matricellular protein: At the crossroads of cell-matrix communication
    • Brekken, R. A., and Sage, E. H. (2001). SPARC, a matricellular protein: at the crossroads of cell-matrix communication. Matrix Biol 19, 816-827.
    • (2001) Matrix Biol , vol.19 , pp. 816-827
    • Brekken, R.A.1    Sage, E.H.2
  • 3
    • 77949887189 scopus 로고    scopus 로고
    • Crystal structure and collagen-binding site of immune inhibitory receptor LAIR-1: Unexpected implications for collagen binding by platelet receptor GPVI
    • Brondijk, T. H. C., de Ruiter, T., Ballering, J., et al. (2010). Crystal structure and collagen-binding site of immune inhibitory receptor LAIR-1: unexpected implications for collagen binding by platelet receptor GPVI. Blood 1 15, 1364-1373.
    • (2010) Blood 1 , vol.15 , pp. 1364-1373
    • Brondijk, T.H.C.1    de Ruiter, T.2    Ballering, J.3
  • 4
    • 74549171003 scopus 로고    scopus 로고
    • Aegyptin displays high-affinity for the von Willebrand factor binding site (RGQOGVMGF) in collagen and inhibits carotid thrombus formation in vivo
    • Calvo E., Tokumasu, F., Mizurini, D. M., et al. (2010). Aegyptin displays high-affinity for the von Willebrand factor binding site (RGQOGVMGF) in collagen and inhibits carotid thrombus formation in vivo. FEBS J 277, 413-427.
    • (2010) FEBS J , vol.277 , pp. 413-427
    • Calvo, E.1    Tokumasu, F.2    Mizurini, D.M.3
  • 5
    • 71049118163 scopus 로고    scopus 로고
    • Crystallographic insight into collagen recognition by discoidin domain receptor 2
    • Carafoli, F., Bihan, D., Stathopoulos, S., et al. (2009). Crystallographic insight into collagen recognition by discoidin domain receptor 2. Structure 17, 1573-1581.
    • (2009) Structure , vol.17 , pp. 1573-1581
    • Carafoli, F.1    Bihan, D.2    Stathopoulos, S.3
  • 6
    • 77949262259 scopus 로고    scopus 로고
    • Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta
    • Christiansen, H. E., Schwarze, U., Pyott, S. M., et al. (2010). Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta. Am J Hum Genet 86, 389-398.
    • (2010) Am J Hum Genet , vol.86 , pp. 389-398
    • Christiansen, H.E.1    Schwarze, U.2    Pyott, S.M.3
  • 7
    • 0037040286 scopus 로고    scopus 로고
    • Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in human, type I collagen
    • Di Lullo, G. A., Sweeney, S. M., Körkkö, J., Ala-Kokko, L., and San Antonio, J. D. (2002). Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in human, type I collagen. J Biol Chem 277, 4223-4231.
    • (2002) J Biol Chem , vol.277 , pp. 4223-4231
    • Di Lullo, G.A.1    Sweeney, S.M.2    Körkkö, J.3    Ala-Kokko, L.4    San Antonio, J.D.5
  • 8
    • 0038240367 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor regulates the vasculature and mass of the prostate and pancreas
    • Doll J. A., Stellmach V. M., Bouck N. P., et al. (2003). Pigment epithelium-derived factor regulates the vasculature and mass of the prostate and pancreas. Nat Med 9, 774-780.
    • (2003) Nat Med , vol.9 , pp. 774-780
    • Doll, J.A.1    Stellmach, V.M.2    Bouck, N.P.3
  • 10
    • 63149115283 scopus 로고    scopus 로고
    • Identification and structural analysis of type I collagen sites in complex with fibronectin fragments
    • Erat, M. C., Slatter, D. A., Lowe, E. D., et al. (2009). Identification and structural analysis of type I collagen sites in complex with fibronectin fragments. Proc Natl Acad Sci USA 106, 4195-4200.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4195-4200
    • Erat, M.C.1    Slatter, D.A.2    Lowe, E.D.3
  • 11
    • 42449113812 scopus 로고    scopus 로고
    • Cell-collagen interactions: The use of peptide Toolkits to investigate collagen-receptor interactions
    • Farndale, R. W., Lisman, T., Bihan, D., et al. (2008). Cell-collagen interactions: the use of peptide Toolkits to investigate collagen-receptor interactions. Biochem Soc Trans 36, 241-250.
    • (2008) Biochem Soc Trans , vol.36 , pp. 241-250
    • Farndale, R.W.1    Lisman, T.2    Bihan, D.3
  • 13
    • 0036869706 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor (PEDF), a serpin with potent anti-angiogenic and neurite outgrowth-promoting properties
    • Gettins, P. G. W., Simonovic, M., and Volz, K. (2002). Pigment epithelium-derived factor (PEDF), a serpin with potent anti-angiogenic and neurite outgrowth-promoting properties. Biol Chem 383, 1677-1682.
    • (2002) Biol Chem , vol.383 , pp. 1677-1682
    • Gettins, P.G.W.1    Simonovic, M.2    Volz, K.3
  • 14
    • 50349096759 scopus 로고    scopus 로고
    • Mapping of SPARC/BM-40/osteonectin-binding sites on fibrillar collagens
    • Giudici, C., Raynal, N., Wiedemann, H., et al. (2008). Mapping of SPARC/BM-40/osteonectin-binding sites on fibrillar collagens. J Biol Chem 283, 19551-19560.
    • (2008) J Biol Chem , vol.283 , pp. 19551-19560
    • Giudici, C.1    Raynal, N.2    Wiedemann, H.3
  • 15
    • 67749124481 scopus 로고    scopus 로고
    • Structural insights into interactions between platelet receptors and fibrillar collagen
    • Herr, A. B., and Farndale, R. W. (2009). Structural insights into interactions between platelet receptors and fibrillar collagen. J Biol Chem 284, 19781-19785.
    • (2009) J Biol Chem , vol.284 , pp. 19781-19785
    • Herr, A.B.1    Farndale, R.W.2
  • 17
    • 0030995856 scopus 로고    scopus 로고
    • Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40
    • Hohenester, E., Maurer, P., and Timpl, R. (1997). Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. EMBO J 16, 3778-3786.
    • (1997) EMBO J , vol.16 , pp. 3778-3786
    • Hohenester, E.1    Maurer, P.2    Timpl, R.3
  • 19
    • 33746658013 scopus 로고    scopus 로고
    • Structural basis for platelet collagen responses by the immune-type receptor glycoprotein VI
    • Horii, K., Kahn, M. L., and Herr, A. B. (2006). Structural basis for platelet collagen responses by the immune-type receptor glycoprotein VI. Blood 108, 936-942.
    • (2006) Blood , vol.108 , pp. 936-942
    • Horii, K.1    Kahn, M.L.2    Herr, A.B.3
  • 20
    • 23944468522 scopus 로고    scopus 로고
    • Involvement of the collagen I-binding motif in the anti-angiogenic activity of pigment epithelium-derived factor
    • Hosomichi, J., Yasui, N., Koide, T., Soma, K., and Morita, I. (2005). Involvement of the collagen I-binding motif in the anti-angiogenic activity of pigment epithelium-derived factor. Biochem Biophys Res Commun 335, 756-761.
    • (2005) Biochem Biophys Res Commun , vol.335 , pp. 756-761
    • Hosomichi, J.1    Yasui, N.2    Koide, T.3    Soma, K.4    Morita, I.5
  • 21
    • 0004043397 scopus 로고
    • New York: Springer-Verlag
    • Hynes, R. O. (1990). Fibronectin. New York: Springer-Verlag.
    • (1990) Fibronectin
    • Hynes, R.O.1
  • 22
    • 79959326422 scopus 로고    scopus 로고
    • Hsp47 as a collagen-specific molecular chaperone
    • Ishida, Y., and Nagata, K. (2011). Hsp47 as a collagen-specific molecular chaperone. Methods Enzymol 499, 167-182.
    • (2011) Methods Enzymol , vol.499 , pp. 167-182
    • Ishida, Y.1    Nagata, K.2
  • 23
    • 46749100659 scopus 로고    scopus 로고
    • Identification of a major GpVI-binding locus in human type III collagen
    • Jarvis, G. E., Raynal, N., Langford, J. P., et al. (2008). Identification of a major GpVI-binding locus in human type III collagen. Blood 118, 4986-4996.
    • (2008) Blood , vol.118 , pp. 4986-4996
    • Jarvis, G.E.1    Raynal, N.2    Langford, J.P.3
  • 24
    • 34447536155 scopus 로고    scopus 로고
    • The decorin sequence SYIRIADTNIT binds collagen type I
    • Kalamajski, S., Aspberg, A., and Oldberg, Å. (2007). The decorin sequence SYIRIADTNIT binds collagen type I. J Biol Chem 282, 16062-16067.
    • (2007) J Biol Chem , vol.282 , pp. 16062-16067
    • Kalamajski, S.1    Aspberg, A.2    Oldberg, A.3
  • 25
    • 70349772632 scopus 로고    scopus 로고
    • Asporin competes with decorin for collagen binding, binds calcium and promotes osteoblast collagen mineralization
    • Kalamajski, S., Aspberg, A., Lindblom, K., Heinegard, D., and Oldberg, Å. (2009). Asporin competes with decorin for collagen binding, binds calcium and promotes osteoblast collagen mineralization. Biochem J 423, 53-59.
    • (2009) Biochem J , vol.423 , pp. 53-59
    • Kalamajski, S.1    Aspberg, A.2    Lindblom, K.3    Heinegard, D.4    Oldberg, A.5
  • 26
    • 34848851981 scopus 로고    scopus 로고
    • Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11
    • Kalamajski, S., and Oldberg, A. (2007). Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11. J Biol Chem 282, 26740-26745.
    • (2007) J Biol Chem , vol.282 , pp. 26740-26745
    • Kalamajski, S.1    Oldberg, A.2
  • 27
    • 58649096818 scopus 로고    scopus 로고
    • Homologous sequence in lumican and fibromodulin leucine-rich repeat 5-7 competes for collagen binding
    • Kalamajski, S., and Oldberg, A. (2009). Homologous sequence in lumican and fibromodulin leucine-rich repeat 5-7 competes for collagen binding. J Biol Chem 284, 534-539.
    • (2009) J Biol Chem , vol.284 , pp. 534-539
    • Kalamajski, S.1    Oldberg, A.2
  • 28
    • 77952550108 scopus 로고    scopus 로고
    • The role of small leucine-rich proteoglycan in collagen fibrillogenesis
    • Kalamajski, S., and Oldberg, A. (2010). The role of small leucine-rich proteoglycan in collagen fibrillogenesis. Matrix Biol 29, 248-253.
    • (2010) Matrix Biol , vol.29 , pp. 248-253
    • Kalamajski, S.1    Oldberg, A.2
  • 29
    • 33744956370 scopus 로고    scopus 로고
    • Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins
    • Koide, T., Nishikawa, Y., Asada, S., et al. (2006). Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins. J Biol Chem 281, 11177-11185.
    • (2006) J Biol Chem , vol.281 , pp. 11177-11185
    • Koide, T.1    Nishikawa, Y.2    Asada, S.3
  • 30
    • 42449119742 scopus 로고    scopus 로고
    • Characterization of high affinity binding motifs for the discoidin domain receptor DDR2 in collagen
    • Konitsiotis, A. D., Raynal, N., Bihan, D., Hohenester, E., Farndale, R. W., and Leitinger, B. (2008). Characterization of high affinity binding motifs for the discoidin domain receptor DDR2 in collagen. J Biol Chem 283, 6861-6868.
    • (2008) J Biol Chem , vol.283 , pp. 6861-6868
    • Konitsiotis, A.D.1    Raynal, N.2    Bihan, D.3    Hohenester, E.4    Farndale, R.W.5    Leitinger, B.6
  • 31
    • 33745043235 scopus 로고    scopus 로고
    • Collagens are functional, high affinity ligands for the inhibitory immune receptor LAIR-1
    • Lebbink, R. J., de Ruiter, T., Adelmeijer, J., et al. (2006). Collagens are functional, high affinity ligands for the inhibitory immune receptor LAIR-1. J Exp Med 203, 1419-1425.
    • (2006) J Exp Med , vol.203 , pp. 1419-1425
    • Lebbink, R.J.1    de Ruiter, T.2    Adelmeijer, J.3
  • 32
    • 67349140403 scopus 로고    scopus 로고
    • Identification of multiple potent binding sites for human leukocyte associated Ig-like receptor LAIR on collagen II and III
    • Lebbink, R. J., Raynal, N., de Ruiter, T., Bihan, D. G., Farndale, R. W., and Meyaard, L. (2009). Identification of multiple potent binding sites for human leukocyte associated Ig-like receptor LAIR on collagen II and III. Matrix Biol 28, 202-210.
    • (2009) Matrix Biol , vol.28 , pp. 202-210
    • Lebbink, R.J.1    Raynal, N.2    de Ruiter, T.3    Bihan, D.G.4    Farndale, R.W.5    Meyaard, L.6
  • 33
    • 33947109970 scopus 로고    scopus 로고
    • Mammalian collagen receptors
    • Leitinger, B., and Hohenester, H. (2007). Mammalian collagen receptors. Matrix Biol 26, 146-155.
    • (2007) Matrix Biol , vol.26 , pp. 146-155
    • Leitinger, B.1    Hohenester, H.2
  • 34
    • 33845268866 scopus 로고    scopus 로고
    • A single high-affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple-helical peptides
    • Lisman, T., Raynal, N., Groeneveld, D., et al. (2006). A single high-affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple-helical peptides. Blood 108, 3753-3756.
    • (2006) Blood , vol.108 , pp. 3753-3756
    • Lisman, T.1    Raynal, N.2    Groeneveld, D.3
  • 35
    • 79952105767 scopus 로고    scopus 로고
    • Chaperoning osteogenesis: New proteinfolding disease paradigms
    • Makareeva, E., Aviles, N. A., and Leikin, S. (2011). Chaperoning osteogenesis: new proteinfolding disease paradigms. Trends Cell Biol 21, 168-176.
    • (2011) Trends Cell Biol , vol.21 , pp. 168-176
    • Makareeva, E.1    Aviles, N.A.2    Leikin, S.3
  • 36
    • 0023264336 scopus 로고
    • Solubilization of protein BM-40 from a basement membrane tumor with chelating agents and evidence for its identity with osteonectin and SPARC
    • Mann, K., Deutzmann, R., Paulsson, M., and Timpl, R. (1987). Solubilization of protein BM-40 from a basement membrane tumor with chelating agents and evidence for its identity with osteonectin and SPARC. FEBS Lett 218, 167-172.
    • (1987) FEBS Lett , vol.218 , pp. 167-172
    • Mann, K.1    Deutzmann, R.2    Paulsson, M.3    Timpl, R.4
  • 37
    • 0022749227 scopus 로고
    • Evidence from molecular cloning that SPARC, a major product of mouse embryo parietal endoderm, is related to an endothelial cell "culture shock" glycoprotein of Mr 43,000
    • Mason, I. J., Taylor, A., Williams, J. G., Sage, H., and Hogan, B. L. M. (1986). Evidence from molecular cloning that SPARC, a major product of mouse embryo parietal endoderm, is related to an endothelial cell "culture shock" glycoprotein of Mr 43,000. EMBO J 5, 1465-1472.
    • (1986) EMBO J , vol.5 , pp. 1465-1472
    • Mason, I.J.1    Taylor, A.2    Williams, J.G.3    Sage, H.4    Hogan, B.L.M.5
  • 38
    • 0034683570 scopus 로고    scopus 로고
    • Embryonic lethality of molecular chaperone Hsp47 knockout mice is associated with defects in collagen biosynthesis
    • Nagai, N., Hosokawa, M., Itohara, S., et al. (2000). Embryonic lethality of molecular chaperone Hsp47 knockout mice is associated with defects in collagen biosynthesis. J Cell Biol 150, 1499-1506.
    • (2000) J Cell Biol , vol.150 , pp. 1499-1506
    • Nagai, N.1    Hosokawa, M.2    Itohara, S.3
  • 39
    • 0038494921 scopus 로고    scopus 로고
    • Platelet-collagen interaction: Is GPVI the central receptor
    • Nieswandt, B., and Watson, S. (2003). Platelet-collagen interaction: is GPVI the central receptor? Blood 102, 449-461.
    • (2003) Blood , vol.102 , pp. 449-461
    • Nieswandt, B.1    Watson, S.2
  • 41
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov, R., and Yamada, K. M. (2002). Fibronectin at a glance. J Cell Sci 115, 3861-3863.
    • (2002) J Cell Sci , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 42
    • 79960239007 scopus 로고    scopus 로고
    • SPARC promotes pericyte recruitment via inhibition of endoglin-dependent TGF-ß1 activity
    • Rivera L. B., and Brekken, R. A. (2011). SPARC promotes pericyte recruitment via inhibition of endoglin-dependent TGF-ß1 activity. J Cell Biol 193, 1305-1319.
    • (2011) J Cell Biol , vol.193 , pp. 1305-1319
    • Rivera, L.B.1    Brekken, R.A.2
  • 43
    • 1842338681 scopus 로고    scopus 로고
    • Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagens
    • Sasaki, T., Gohring, W., Mann, K., et al. (1997). Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagens. J Biol Chem 272, 9237-9243.
    • (1997) J Biol Chem , vol.272 , pp. 9237-9243
    • Sasaki, T.1    Gohring, W.2    Mann, K.3
  • 44
    • 0032536897 scopus 로고    scopus 로고
    • Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin
    • Sasaki, T., Hohenester, E., Gohring, W., and Timpl, R. (1998). Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin. EMBO J 17, 1625-1634.
    • (1998) EMBO J , vol.17 , pp. 1625-1634
    • Sasaki, T.1    Hohenester, E.2    Gohring, W.3    Timpl, R.4
  • 45
    • 0032704239 scopus 로고    scopus 로고
    • Immunochemical and tissue analysis of protease generated neoepitopes of BM-40 (osteonectin, SPARC) which are correlated to a higher affinity binding to collagens
    • Sasaki, T., Miosge, N., and Timpl, R. (1999). Immunochemical and tissue analysis of protease generated neoepitopes of BM-40 (osteonectin, SPARC) which are correlated to a higher affinity binding to collagens. Matrix Biol 18, 499-508.
    • (1999) Matrix Biol , vol.18 , pp. 499-508
    • Sasaki, T.1    Miosge, N.2    Timpl, R.3
  • 46
    • 79960676666 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor (PEDF) shares binding sites in collagen with heparin/heparin sulphate proteoglycans
    • Sekiya, A., Okano-Kosugi, H., Yamazaki, C. M., and Koide, T. (2011). Pigment epithelium-derived factor (PEDF) shares binding sites in collagen with heparin/heparin sulphate proteoglycans. J Biol Chem 286, 26364-26374.
    • (2011) J Biol Chem , vol.286 , pp. 26364-26374
    • Sekiya, A.1    Okano-Kosugi, H.2    Yamazaki, C.M.3    Koide, T.4
  • 47
    • 0029794908 scopus 로고    scopus 로고
    • A host-guest set of triple-helical peptides: Stability of Gly-X-Y triplets containing common nonpolar residues
    • Shah, N. K., Ramshaw, J. A., Kirkpatrick, A., Shah, C., and Brodsky, B. (1996). A host-guest set of triple-helical peptides: stability of Gly-X-Y triplets containing common nonpolar residues. Biochemistry 35, 10262-10268.
    • (1996) Biochemistry , vol.35 , pp. 10262-10268
    • Shah, N.K.1    Ramshaw, J.A.2    Kirkpatrick, A.3    Shah, C.4    Brodsky, B.5
  • 48
    • 33847736329 scopus 로고    scopus 로고
    • Structural basis for the platelet-collagen interaction. The smallest motif within collagen that recognizes and activates platelet glycoprotein VI contains two glycine-proline-hydroxyproline triplets
    • Smethurst, P. A., Onley, D. J., Jarvis, G. E., et al. (2007). Structural basis for the platelet-collagen interaction. The smallest motif within collagen that recognizes and activates platelet glycoprotein VI contains two glycine-proline-hydroxyproline triplets. J Biol Chem 282, 1296-1304.
    • (2007) J Biol Chem , vol.282 , pp. 1296-1304
    • Smethurst, P.A.1    Onley, D.J.2    Jarvis, G.E.3
  • 49
    • 33748743639 scopus 로고    scopus 로고
    • Matricellular hevin regulates decorin production and collagen assembly
    • Sullivan, M. M., Barker, T. H., Funk, S. E., et al. (2006). Matricellular hevin regulates decorin production and collagen assembly. J Biol Chem 281, 27621-27632.
    • (2006) J Biol Chem , vol.281 , pp. 27621-27632
    • Sullivan, M.M.1    Barker, T.H.2    Funk, S.E.3
  • 50
    • 51049121850 scopus 로고    scopus 로고
    • Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates
    • Sweeney, S. M., Orgel, J. P., Fertala, A., et al. (2008). Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates. J Biol Chem 283, 21187-21197.
    • (2008) J Biol Chem , vol.283 , pp. 21187-21197
    • Sweeney, S.M.1    Orgel, J.P.2    Fertala, A.3
  • 52
    • 33646341752 scopus 로고    scopus 로고
    • Sensing extracellular matrix: An update on discoidin domain receptor function
    • Vogel, W. F., Abdulhussein, R., and Ford, D. E. (2006). Sensing extracellular matrix: an update on discoidin domain receptor function. Cell Signal 18, 1108-1116.
    • (2006) Cell Signal , vol.18 , pp. 1108-1116
    • Vogel, W.F.1    Abdulhussein, R.2    Ford, D.E.3
  • 54
    • 78951473449 scopus 로고    scopus 로고
    • Collagen binding specificity of the discoidin domain receptors: Binding sites on collagen II and III and molecular determinants for collagen IV recognition by DDR1
    • Xu, H., Raynal, N., Stathopoulos, S., Myllyharju, J., Farndale, R. W., and Leitinger, B. (2011). Collagen binding specificity of the discoidin domain receptors: binding sites on collagen II and III and molecular determinants for collagen IV recognition by DDR1. Matrix Biol 30, 16-26.
    • (2011) Matrix Biol , vol.30 , pp. 16-26
    • Xu, H.1    Raynal, N.2    Stathopoulos, S.3    Myllyharju, J.4    Farndale, R.W.5    Leitinger, B.6
  • 55
    • 0037465705 scopus 로고    scopus 로고
    • Dual-site recognition of different extracellular matrix components by anti-angiogenic/neurotrophic serpin, PEDF
    • Yasui, N., Mori, T., Morito, D., et al. (2003). Dual-site recognition of different extracellular matrix components by anti-angiogenic/neurotrophic serpin, PEDF. Biochemistry 42, 3160-3167.
    • (2003) Biochemistry , vol.42 , pp. 3160-3167
    • Yasui, N.1    Mori, T.2    Morito, D.3


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