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Volumn 52, Issue 1, 2011, Pages 18-24

Collagen fibril surface displays a constellation of sites capable of promoting fibril assembly, stability, and hemostasis

Author keywords

Cell adhesion; Collagen; Extracellular matrix; Fibril; Hemostasis

Indexed keywords

COLLAGEN; COLLAGEN FIBRIL;

EID: 78650733361     PISSN: 03008207     EISSN: 16078438     Source Type: Journal    
DOI: 10.3109/03008207.2010.511354     Document Type: Article
Times cited : (48)

References (37)
  • 3
    • 33745181159 scopus 로고    scopus 로고
    • Microfibrillar structure of type I collagen in situ
    • U.S.A
    • Orgel, J., Irving, T., Miller, A., and Wess, T. (2006). Microfibrillar structure of type I collagen in situ. Proc. Natl. Acad. Sci. U.S.A. 103:9001-9005.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 9001-9005
    • Orgel, J.1    Irving, T.2    Miller, A.3    Wess, T.4
  • 4
    • 0001113489 scopus 로고
    • A subunit model for the tropocollagen macromolecule
    • U.S.A
    • Petruska, J., and Hodge, A. (1964). A Subunit Model for the Tropocollagen Macromolecule. Proc. Natl. Acad. Sci. U.S.A. 51:871-876.
    • (1964) Proc. Natl. Acad. Sci. , vol.51 , pp. 871-876
    • Petruska, J.1    Hodge, A.2
  • 5
    • 0002981867 scopus 로고
    • The structure of collagen fibrils
    • Bear, R. (1952). The structure of collagen fibrils. Adv. Protein Chem. 7:69-160.
    • (1952) Adv. Protein Chem. , vol.7 , pp. 69-160
    • Bear, R.1
  • 6
    • 0035912751 scopus 로고    scopus 로고
    • Corneal collagen fibril structure in three dimensions: Structural insights into fibril assembly mechanical properties and tissue organization
    • U.S.A
    • Holmes, D., Gilpin, C., Baldock, C., Ziese, U., Koster, A., and Kadler, K. (2001). Corneal collagen fibril structure in three dimensions: Structural insights into fibril assembly, mechanical properties, and tissue organization. Proc. Natl. Acad. Sci. U.S.A. 98:7307-7312.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 7307-7312
    • Holmes, D.1    Gilpin, C.2    Baldock, C.3    Ziese, U.4    Koster, A.5    Kadler, K.6
  • 7
    • 0016196786 scopus 로고
    • The staining pattern of collagen fibrils I an analysis of electron micrographs
    • Chapman, J. (1974). The staining pattern of collagen fibrils. I. An analysis of electron micrographs. Connect. Tissue Res. 2:137-150.
    • (1974) Connect. Tissue Res. , vol.2 , pp. 137-150
    • Chapman, J.1
  • 8
    • 36949016403 scopus 로고    scopus 로고
    • Type I collagen and collagen mimetics as angiogenesis promoting superpolymers
    • Twardowski, T., Fertala, A., Orgel, J., and San Antonio, J. (2007). Type I collagen and collagen mimetics as angiogenesis promoting superpolymers. Curr. Pharm. Des. 13:3608-3621.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 3608-3621
    • Twardowski, T.1    Fertala, A.2    Orgel, J.3    San Antonio, J.4
  • 9
    • 0037040286 scopus 로고    scopus 로고
    • Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human type I collagen
    • Di Lullo, G., Sweeney, S., Korkko, J., Ala-Kokko, L., and San Antonio, J. (2002). Mapping the ligand-binding sites and disease- associated mutations on the most abundant protein in the human, type I collagen. J. Biol. Chem. 277:4223-4231.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4223-4231
    • Di Lullo, G.1    Sweeney, S.2    Korkko, J.3    Ala-Kokko, L.4    San Antonio, J.5
  • 11
    • 42949135530 scopus 로고    scopus 로고
    • Collagen fibril architecture domain organization and triple-helical conformation govern its proteolysis
    • U.S.A
    • Perumal, S., Antipova, O., and Orgel, J. (2008). Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis. Proc. Natl. Acad. Sci. U.S.A. 105:2824-2829.
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 2824-2829
    • Perumal, S.1    Antipova, O.2    Orgel, J.3
  • 12
    • 0016162137 scopus 로고
    • The staining pattern of collagen fibrils II a comparison with patterns computergenerated from the amino acid sequence
    • Chapman, J., and Hardcastle, R. (1974). The staining pattern of collagen fibrils. II. A comparison with patterns computergenerated from the amino acid sequence. Connect. Tissue Res. 2:151-159.
    • (1974) Connect. Tissue Res. , vol.2 , pp. 151-159
    • Chapman, J.1    Hardcastle, R.2
  • 13
    • 0036838777 scopus 로고    scopus 로고
    • A statistically derived parameterization for the collagen triple-helix
    • Rainey, J., and Goh, M. (2002). A statistically derived parameterization for the collagen triple-helix. Protein Sci. 11:2748-2754.
    • (2002) Protein Sci. , vol.11 , pp. 2748-2754
    • Rainey, J.1    Goh, M.2
  • 14
    • 77951975886 scopus 로고    scopus 로고
    • A new method for describing the helical conformation of collagen: Dependence of the triple helical twist on amino acid sequence
    • Bella, J. (2010). A new method for describing the helical conformation of collagen: dependence of the triple helical twist on amino acid sequence. J. Struct. Biol. 170:377-391.
    • (2010) J. Struct. Biol. , vol.170 , pp. 377-391
    • Bella, J.1
  • 15
    • 70349330118 scopus 로고    scopus 로고
    • Decorin core protein decoron shape complements collagen fibril surface structure and mediates its binding
    • Orgel, J.P.R.O., Eid, A., Antipova, O., Bella, J., and Scott, J.E. (2009). Decorin Core Protein (Decoron) Shape Complements Collagen Fibril Surface Structure and Mediates Its Binding. PLoS ONE 4:e7028.
    • (2009) PLoS ONE , vol.4
    • Orgel, J.P.R.O.1    Eid, A.2    Antipova, O.3    Bella, J.4    Scott, J.E.5
  • 16
    • 0343403755 scopus 로고
    • Electron microscopy shows periodic structure in collagen fibril cross sections
    • U.S.A.
    • Hulmes, D., Jesior, J., Miller, A., Berthet-Colominas, C., and Wolff, C. (1981). Electron microscopy shows periodic structure in collagen fibril cross sections. Proc. Natl. Acad. Sci. U.S.A. 78:3567-3571.
    • (1981) Proc. Natl. Acad. Sci. , vol.78 , pp. 3567-3571
    • Hulmes, D.1    Jesior, J.2    Miller, A.3    Berthet-Colominas, C.4    Wolff, C.5
  • 17
    • 0028910961 scopus 로고
    • Radial packing, order, and disorder in collagen fibrils
    • Hulmes, D., Wess, T., Prockop, D., and Fratzl, P. (1995). Radial packing, order, and disorder in collagen fibrils. Biophys. J. 68:1661-1670.
    • (1995) Biophys. J. , vol.68 , pp. 1661-1670
    • Hulmes, D.1    Wess, T.2    Prockop, D.3    Fratzl, P.4
  • 18
    • 0025060137 scopus 로고
    • Characterization of a monoclonal-antibody against native human type-I collagen
    • Werkmeister, J., Ramshaw, J., and Ellender, G. (1990). Characterization of a monoclonal-antibody against native human type-I collagen. Eur. J. Biochem. 187:439-443.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 439-443
    • Werkmeister, J.1    Ramshaw, J.2    Ellender, G.3
  • 19
    • 67749124481 scopus 로고    scopus 로고
    • Structural insights into the interactions between platelet receptors and fibrillar collagen
    • Herr, A.B., and Farndale, R.W. (2009). Structural Insights into the 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
  • 20
    • 0030239753 scopus 로고    scopus 로고
    • Algorithms for finding the axis of a helix: Fast rotational and parametric least-squares methods
    • Christopher, J., Swanson, R., and Baldwin, T. (1996). Algorithms for finding the axis of a helix: fast rotational and parametric least-squares methods. Comput. Chem. 20:339-345.
    • (1996) Comput. Chem. , vol.20 , pp. 339-345
    • Christopher, J.1    Swanson, R.2    Baldwin, T.3
  • 21
    • 0034651554 scopus 로고    scopus 로고
    • The in situ conformation and axial location of the intermolecular cross-linked non-helical telopeptides of type I collagen
    • Orgel, J., Wess, T., and Miller, A. (2000). The in situ conformation and axial location of the intermolecular cross-linked non-helical telopeptides of type I collagen. Struct. Fold. Des. 8:137-142.
    • (2000) Struct. Fold. Des. , vol.8 , pp. 137-142
    • Orgel, J.1    Wess, T.2    Miller, A.3
  • 22
    • 0029812707 scopus 로고    scopus 로고
    • Collagen fibril surface: Tmafm FEG-SEM and freeze-etching observations
    • Raspanti, M., Alessandrini, A., Gobbi, P., and Ruggeri, A. (1996). Collagen Fibril Surface: TMAFM, FEG-SEM and Freeze- Etching Observations. Microsc. Res. Tech. 35:87-93.
    • (1996) Microsc. Res. Tech. , vol.35 , pp. 87-93
    • Raspanti, M.1    Alessandrini, A.2    Gobbi, P.3    Ruggeri, A.4
  • 23
    • 72449155751 scopus 로고    scopus 로고
    • Suprastructures of extracellular matrices: Paradigms of functions controlled by aggregates rather than molecules
    • Bruckner, P. (2010). Suprastructures of extracellular matrices: paradigms of functions controlled by aggregates rather than molecules. Cell Tissue Res. 339:7-18.
    • (2010) Cell Tissue Res. , vol.339 , pp. 7-18
    • Bruckner, P.1
  • 25
    • 33846032667 scopus 로고    scopus 로고
    • Sequence dependence of renucleation after a Gly mutation in model collagen peptides
    • Hyde, T.J., Bryan, M.A., Brodsky, B., and Baum, J. (2006). Sequence dependence of renucleation after a Gly mutation in model collagen peptides. J. Biol. Chem. 281:36937.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36937
    • Hyde, T.J.1    Bryan, M.A.2    Brodsky, B.3    Baum, J.4
  • 26
    • 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 glycineproline- hydroxyproline triplets
    • Smethurst, P.A., Onley, D.J., Jarvis, G.E., O'Connor, M.N., Knight, C.G., Herr, A.B., Ouwehand, W.H., and Farndale, R.W. (2007). Structural basis for the platelet-collagen interaction: the smallest motif within collagen that recognizes and activates platelet Glycoprotein VI contains two glycineproline- hydroxyproline triplets. J. Biol. Chem. 282:1296.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1296
    • Smethurst, P.A.1    Onley, D.J.2    Jarvis, G.E.3    O'Connor, M.N.4    Knight, C.G.5    Herr, A.B.6    Ouwehand, W.H.7    Farndale, R.W.8
  • 27
    • 4444322183 scopus 로고    scopus 로고
    • Platelet-collagen responses: Molecular basis and therapeutic promise
    • Kahn, M.L. (2004). 'Platelet-Collagen Responses: Molecular Basis and Therapeutic Promise.' in Seminars in Thrombosis& Hemostasis., 419.
    • (2004) Seminars in Thrombosis& Hemostasis , vol.419
    • Kahn, M.L.1
  • 28
    • 0030016013 scopus 로고    scopus 로고
    • Proteodermatan and proteokeratan sulfate decorin lumican/fibromodulin proteins are horseshoe shaped implications for their interactions with collagen
    • Scott, J. (1996). Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen. Biochemistry 35:8795-8799.
    • (1996) Biochemistry , vol.35 , pp. 8795-8799
    • Scott, J.1
  • 29
    • 0034671734 scopus 로고    scopus 로고
    • Multiple binding sites in collagen type I for the integrins alpha1beta1 and alpha2beta1
    • Xu, Y., Gurusiddappa, S., Rich, R., Owens, R., Keene, D., Mayne, R., Hook, A., and Hook, M. (2000). Multiple binding sites in collagen type I for the integrins alpha1beta1 and alpha2beta1. J. Biol. Chem. 275:38981-38989.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38981-38989
    • Xu, Y.1    Gurusiddappa, S.2    Rich, R.3    Owens, R.4    Keene, D.5    Mayne, R.6    Hook, A.7    Hook, M.8
  • 30
    • 0034614620 scopus 로고    scopus 로고
    • The collagenbinding A-domains of integrins alpha1beta1 and alpha2beta1 recognize the same specific amino acid sequence gfoger, in native triple-helical collagens
    • Knight, C.G., Morton, L.F., Peachey, A.R., Tuckwell, D.S., Farndale, R.W., and Barnes, M.J. (2000). The collagenbinding A-domains of integrins alpha1beta1 and alpha2beta1 recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens. J. Biol. Chem. 275:35-40.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35-40
    • Knight, C.G.1    Morton, L.F.2    Peachey, A.R.3    Tuckwell, D.S.4    Farndale, R.W.5    Barnes, M.J.6
  • 32
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht, M. and Werb, Z. (2001). How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol. 17:463-516.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.1    Werb, Z.2
  • 33
    • 24044459285 scopus 로고    scopus 로고
    • Matrix metalloproteinases and angiogenesis
    • Rundhaug, J.E. (2005). Matrix metalloproteinases and angiogenesis. J. Cell. Mol. Med. 9:267-285.
    • (2005) J. Cell. Mol. Med. , vol.9 , pp. 267-285
    • Rundhaug, J.E.1
  • 34
    • 64249129547 scopus 로고    scopus 로고
    • Platelet matrix metalloprotease-1 mediates thrombogenesis by activating par1 at a cryptic ligand site
    • Trivedi, V., Boire, A., Tchemychev, B., Kaneider, N., Leger, A., O'Callaghan, K., Covic, L., and Kuliopulos, A. (2009). Platelet Matrix Metalloprotease-1 Mediates Thrombogenesis by Activating PAR1 at a Cryptic Ligand Site. Cell 137:332-343.
    • (2009) Cell , vol.137 , pp. 332-343
    • Trivedi, V.1    Boire, A.2    Tchemychev, B.3    Kaneider, N.4    Leger, A.5    O'Callaghan, K.6    Covic, L.7    Kuliopulos, A.8
  • 35
    • 77950849488 scopus 로고    scopus 로고
    • Biochemical markers of bone cell activity in children with type 1 diabetes mellitus
    • Pater, A., Sypniewska, G., and Pilecki, O. (2010). Biochemical markers of bone cell activity in children with type 1 diabetes mellitus. J. Pediatr. Endocrinol. Metab. 23:81-86.
    • (2010) J. Pediatr. Endocrinol. Metab. , vol.23 , pp. 81-86
    • Pater, A.1    Sypniewska, G.2    Pilecki, O.3
  • 36
    • 1842815811 scopus 로고    scopus 로고
    • Early degradation and serum appearance of type I collagen fragments after myocardial infarction
    • Villarreal, F., Omens, J., Dillmann, W., Risteli, J., Nguyen, J., and Covell, J. (2004). Early degradation and serum appearance of type I collagen fragments after myocardial infarction. J. Mol. Cell. Cardiol. 36:597-601.
    • (2004) J. Mol. Cell. Cardiol. , vol.36 , pp. 597-601
    • Villarreal, F.1    Omens, J.2    Dillmann, W.3    Risteli, J.4    Nguyen, J.5    Covell, J.6
  • 37
    • 0027731043 scopus 로고
    • Backbone dynamics of pro-hyp-gly 10 and a designed collagen-like triple-helical peptide by 15N NMR relaxation and hydrogenexchange measurements
    • Fan, P., Li, M., Brodsky, B., and Baum, J. (1993). Backbone dynamics of (Pro-Hyp-Gly)10 and a designed collagen-like triple-helical peptide by 15N NMR relaxation and hydrogenexchange measurements. Biochemistry 32:13299-13309.
    • (1993) Biochemistry , vol.32 , pp. 13299-13309
    • Fan, P.1    Li, M.2    Brodsky, B.3    Baum, J.4


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