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Volumn 183, Issue 3, 2013, Pages 394-403

Quantitative analysis of type I collagen fibril regulation by lumican and decorin using AFM

Author keywords

AFM; Decorin; Fibrillogenesis; Lumican; SLRP; Type I collagen

Indexed keywords

COLLAGEN FIBRIL; COLLAGEN TYPE 1; DECORIN; LUMICAN; NANOFIBER; PROTEOGLYCAN; RECOMBINANT DECORIN; RECOMBINANT LUMICAN; RECOMBINANT PROTEIN; SMALL LEUCINE RICH REPEAT PROTEOGLYCAN; UNCLASSIFIED DRUG;

EID: 84883445244     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2013.05.022     Document Type: Article
Times cited : (43)

References (71)
  • 1
    • 0036744260 scopus 로고    scopus 로고
    • Mice deficient in small leucine-rich proteoglycans: novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases
    • Ameye L., Young M.F. Mice deficient in small leucine-rich proteoglycans: novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases. Glycobiology 2002, 12:107R-116R.
    • (2002) Glycobiology , vol.12
    • Ameye, L.1    Young, M.F.2
  • 2
    • 0023202453 scopus 로고
    • The morphogenesis of the chick primary corneal stroma. I. New observations on collagen organization in vivo help explain stromal deposition and growth
    • Bard J.B., Bansal M.K. The morphogenesis of the chick primary corneal stroma. I. New observations on collagen organization in vivo help explain stromal deposition and growth. Development 1987, 100:135-145.
    • (1987) Development , vol.100 , pp. 135-145
    • Bard, J.B.1    Bansal, M.K.2
  • 7
    • 0024021040 scopus 로고
    • Conformational flexibility: a new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans
    • Casu B., Petitou M., Provasoli M., Sinay P. Conformational flexibility: a new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans. Trends Biochem. Sci. 1988, 13:221-225.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 221-225
    • Casu, B.1    Petitou, M.2    Provasoli, M.3    Sinay, P.4
  • 8
    • 0032101311 scopus 로고    scopus 로고
    • Lumican regulates collagen fibril assembly: skin fragility and corneal opacity in the absence of lumican
    • Chakravarti S., Magnuson T., Lass J.H., Jepsen K.J., LaMantia C., Carroll H. Lumican regulates collagen fibril assembly: skin fragility and corneal opacity in the absence of lumican. J. Cell Biol. 1998, 141:1277-1286.
    • (1998) J. Cell Biol. , vol.141 , pp. 1277-1286
    • Chakravarti, S.1    Magnuson, T.2    Lass, J.H.3    Jepsen, K.J.4    LaMantia, C.5    Carroll, H.6
  • 9
    • 33748316797 scopus 로고    scopus 로고
    • Collagen fibril assembly during postnatal development and dysfunctional regulation in the lumican-deficient murine cornea
    • Chakravarti S., Zhang G., Chervoneva I., Roberts L., Birk D.E. Collagen fibril assembly during postnatal development and dysfunctional regulation in the lumican-deficient murine cornea. Dev. Dyn. 2006, 235:2493-2506.
    • (2006) Dev. Dyn. , vol.235 , pp. 2493-2506
    • Chakravarti, S.1    Zhang, G.2    Chervoneva, I.3    Roberts, L.4    Birk, D.E.5
  • 10
    • 84877691193 scopus 로고    scopus 로고
    • The regulatory roles of small leucine-rich proteoglycans in extracellular matrix assembly
    • Chen S., Birk D.E. The regulatory roles of small leucine-rich proteoglycans in extracellular matrix assembly. FEBS J. 2013, 280:2120-2137.
    • (2013) FEBS J. , vol.280 , pp. 2120-2137
    • Chen, S.1    Birk, D.E.2
  • 11
    • 33646714443 scopus 로고    scopus 로고
    • Observing growth steps of collagen self-assembly by time-lapse high-resolution atomic force microscopy
    • Cisneros D.A., Hung C., Franz C.M., Muller D.J. Observing growth steps of collagen self-assembly by time-lapse high-resolution atomic force microscopy. J. Struct. Biol. 2006, 154:232-245.
    • (2006) J. Struct. Biol. , vol.154 , pp. 232-245
    • Cisneros, D.A.1    Hung, C.2    Franz, C.M.3    Muller, D.J.4
  • 12
    • 34250352329 scopus 로고    scopus 로고
    • Creating ultrathin nanoscopic collagen matrices for biological and biotechnological applications
    • Cisneros D.A., Friedrichs J., Taubenberger A., Franz C.M., Muller D.J. Creating ultrathin nanoscopic collagen matrices for biological and biotechnological applications. Small 2007, 3:956-963.
    • (2007) Small , vol.3 , pp. 956-963
    • Cisneros, D.A.1    Friedrichs, J.2    Taubenberger, A.3    Franz, C.M.4    Muller, D.J.5
  • 13
    • 0022740621 scopus 로고
    • Preservation of corneal collagen fibril structure using low-temperature procedures for electron microscopy
    • Craig A.S., Robertson J.G., Parry D.A. Preservation of corneal collagen fibril structure using low-temperature procedures for electron microscopy. J. Ultrastruct. Mol. Struct. Res. 1986, 96:172-175.
    • (1986) J. Ultrastruct. Mol. Struct. Res. , vol.96 , pp. 172-175
    • Craig, A.S.1    Robertson, J.G.2    Parry, D.A.3
  • 14
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • Danielson K.G., Baribault H., Holmes D.F., Graham H., Kadler K.E., Iozzo R.V. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J. Cell Biol. 1997, 136:729-743.
    • (1997) J. Cell Biol. , vol.136 , pp. 729-743
    • Danielson, K.G.1    Baribault, H.2    Holmes, D.F.3    Graham, H.4    Kadler, K.E.5    Iozzo, R.V.6
  • 15
    • 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.A., Sweeney S.M., Korkko J., Ala-Kokko L., San Antonio J.D. Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. J. Biol. Chem. 2002, 277:4223-4231.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4223-4231
    • Di Lullo, G.A.1    Sweeney, S.M.2    Korkko, J.3    Ala-Kokko, L.4    San Antonio, J.D.5
  • 16
    • 33748366399 scopus 로고    scopus 로고
    • Fibrillogenesis of collagen types I, II, and III with small leucine-rich proteoglycans decorin and biglycan
    • Douglas T., Heinemann S., Bierbaum S., Scharnweber D., Worch H. Fibrillogenesis of collagen types I, II, and III with small leucine-rich proteoglycans decorin and biglycan. Biomacromolecules 2006, 7:2388-2393.
    • (2006) Biomacromolecules , vol.7 , pp. 2388-2393
    • Douglas, T.1    Heinemann, S.2    Bierbaum, S.3    Scharnweber, D.4    Worch, H.5
  • 17
    • 77649270954 scopus 로고    scopus 로고
    • Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy
    • Erickson H.P. Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biol. Proced. Online 2009, 11:32-51.
    • (2009) Biol. Proced. Online , vol.11 , pp. 32-51
    • Erickson, H.P.1
  • 18
    • 0035218925 scopus 로고    scopus 로고
    • Structural variations of collagen in normal and pathological tissues: role of electron microscopy
    • Eyden B., Tzaphlidou M. Structural variations of collagen in normal and pathological tissues: role of electron microscopy. Micron 2001, 32:287-300.
    • (2001) Micron , vol.32 , pp. 287-300
    • Eyden, B.1    Tzaphlidou, M.2
  • 19
    • 0034645039 scopus 로고    scopus 로고
    • Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons
    • Ezura Y., Chakravarti S., Oldberg A., Chervoneva I., Birk D.E. Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons. J. Cell Biol. 2000, 151:779-788.
    • (2000) J. Cell Biol. , vol.151 , pp. 779-788
    • Ezura, Y.1    Chakravarti, S.2    Oldberg, A.3    Chervoneva, I.4    Birk, D.E.5
  • 20
    • 77958064869 scopus 로고    scopus 로고
    • Equivalent stiffness after glycosaminoglycan depletion in tendon - an ultra-structural finite element model and corresponding experiments
    • Fessel G., Snedeker J.G. Equivalent stiffness after glycosaminoglycan depletion in tendon - an ultra-structural finite element model and corresponding experiments. J. Theor. Biol. 2011, 268:77-83.
    • (2011) J. Theor. Biol. , vol.268 , pp. 77-83
    • Fessel, G.1    Snedeker, J.G.2
  • 21
    • 80054831405 scopus 로고    scopus 로고
    • Studying collagen self-assembly by time-lapse high-resolution atomic force microscopy
    • Franz C.M., Muller D.J. Studying collagen self-assembly by time-lapse high-resolution atomic force microscopy. Methods Mol. Biol. 2011, 736:97-107.
    • (2011) Methods Mol. Biol. , vol.736 , pp. 97-107
    • Franz, C.M.1    Muller, D.J.2
  • 22
    • 34548501731 scopus 로고    scopus 로고
    • Nature's hierarchical materials
    • Fratzl P., Weinkamer R. Nature's hierarchical materials. Prog. Mater. Sci. 2007, 52:1263-1334.
    • (2007) Prog. Mater. Sci. , vol.52 , pp. 1263-1334
    • Fratzl, P.1    Weinkamer, R.2
  • 23
    • 4744352594 scopus 로고    scopus 로고
    • Bone morphogenetic protein-1/tolloid-related metalloproteinases process osteoglycin and enhance its ability to regulate collagen fibrillogenesis
    • Ge G., Seo N.S., Liang X., Hopkins D.R., Hook M., Greenspan D.S. Bone morphogenetic protein-1/tolloid-related metalloproteinases process osteoglycin and enhance its ability to regulate collagen fibrillogenesis. J. Biol. Chem. 2004, 279:41626-41633.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41626-41633
    • Ge, G.1    Seo, N.S.2    Liang, X.3    Hopkins, D.R.4    Hook, M.5    Greenspan, D.S.6
  • 24
    • 0016764743 scopus 로고
    • Statistical morphometric studies in normal human and rabbit corneal stroma
    • Giraud J.P., Pouliquen Y., Offret G., Payrau P. Statistical morphometric studies in normal human and rabbit corneal stroma. Exp. Eye Res. 1975, 21:221-229.
    • (1975) Exp. Eye Res. , vol.21 , pp. 221-229
    • Giraud, J.P.1    Pouliquen, Y.2    Offret, G.3    Payrau, P.4
  • 26
    • 0015892994 scopus 로고
    • Analysis of the primary structure of collagen for the origins of molecular packing
    • Hulmes D.J., Miller A., Parry D.A., Piez K.A., Woodhead-Galloway J. Analysis of the primary structure of collagen for the origins of molecular packing. J. Mol. Biol. 1973, 79:137-148.
    • (1973) J. Mol. Biol. , vol.79 , pp. 137-148
    • Hulmes, D.J.1    Miller, A.2    Parry, D.A.3    Piez, K.A.4    Woodhead-Galloway, J.5
  • 27
    • 0030010512 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function
    • Iozzo R.V., Murdoch A.D. Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J. 1996, 10:598-614.
    • (1996) FASEB J. , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 30
  • 32
    • 34848851981 scopus 로고    scopus 로고
    • Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11
    • Kalamajski S., Oldberg A. Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11. J. Biol. Chem. 2007, 282:26740-26745.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26740-26745
    • Kalamajski, S.1    Oldberg, A.2
  • 33
    • 58649096818 scopus 로고    scopus 로고
    • Homologous sequence in lumican and fibromodulin leucine-rich repeat 5-7 competes for collagen binding
    • Kalamajski S., Oldberg A. Homologous sequence in lumican and fibromodulin leucine-rich repeat 5-7 competes for collagen binding. J. Biol. Chem. 2009, 284:534-539.
    • (2009) J. Biol. Chem. , vol.284 , pp. 534-539
    • Kalamajski, S.1    Oldberg, A.2
  • 34
    • 77952550108 scopus 로고    scopus 로고
    • The role of small leucine-rich proteoglycans in collagen fibrillogenesis
    • Kalamajski S., Oldberg A. The role of small leucine-rich proteoglycans in collagen fibrillogenesis. Matrix Biol. 2010, 29:248-253.
    • (2010) Matrix Biol. , vol.29 , pp. 248-253
    • Kalamajski, S.1    Oldberg, A.2
  • 35
    • 79955591894 scopus 로고    scopus 로고
    • Incorporation of a decorin biomimetic enhances the mechanical properties of electrochemically aligned collagen threads
    • Kishore V., Paderi J.E., Akkus A., Smith K.M., Balachandran D., Beaudoin S., Panitch A., Akkus O. Incorporation of a decorin biomimetic enhances the mechanical properties of electrochemically aligned collagen threads. Acta Biomater. 2011, 7:2428-2436.
    • (2011) Acta Biomater. , vol.7 , pp. 2428-2436
    • Kishore, V.1    Paderi, J.E.2    Akkus, A.3    Smith, K.M.4    Balachandran, D.5    Beaudoin, S.6    Panitch, A.7    Akkus, O.8
  • 38
    • 0014345341 scopus 로고
    • The effect of acid mucopolysaccharides and acid mucopolysaccharide-proteins on fibril formation from collagen solutions
    • Mathews M.B., Decker L. The effect of acid mucopolysaccharides and acid mucopolysaccharide-proteins on fibril formation from collagen solutions. Biochem. J. 1968, 109:517-526.
    • (1968) Biochem. J. , vol.109 , pp. 517-526
    • Mathews, M.B.1    Decker, L.2
  • 39
    • 70449138788 scopus 로고
    • The structure and transparency of the cornea
    • Maurice D.M. The structure and transparency of the cornea. J. Physiol. 1957, 136:263-286.
    • (1957) J. Physiol. , vol.136 , pp. 263-286
    • Maurice, D.M.1
  • 41
    • 0015912131 scopus 로고
    • The influence of glycosaminoglycans on the formation of fibers from monomeric tropocollagen in vitro
    • Obrink B. The influence of glycosaminoglycans on the formation of fibers from monomeric tropocollagen in vitro. Eur. J. Biochem. 1973, 34:129-137.
    • (1973) Eur. J. Biochem. , vol.34 , pp. 129-137
    • Obrink, B.1
  • 42
    • 0347683486 scopus 로고    scopus 로고
    • Identification of tyrosine sulfation in extracellular leucine-rich repeat proteins using mass spectrometry
    • Onnerfjord P., Heathfield T.F., Heinegard D. Identification of tyrosine sulfation in extracellular leucine-rich repeat proteins using mass spectrometry. J. Biol. Chem. 2004, 279:26-33.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26-33
    • Onnerfjord, P.1    Heathfield, T.F.2    Heinegard, D.3
  • 43
    • 70349330118 scopus 로고    scopus 로고
    • Decorin core protein (decoron) shape complements collagen fibril surface structure and mediates its binding
    • Orgel J.P., Eid A., Antipova O., Bella J., Scott J.E. Decorin core protein (decoron) shape complements collagen fibril surface structure and mediates its binding. PLoS One 2009, 4:e7028.
    • (2009) PLoS One , vol.4
    • Orgel, J.P.1    Eid, A.2    Antipova, O.3    Bella, J.4    Scott, J.E.5
  • 44
    • 0034326762 scopus 로고    scopus 로고
    • A model for type II collagen fibrils: distinctive D-band patterns in native and reconstituted fibrils compared with sequence data for helix and telopeptide domains
    • Ortolani F., Giordano M., Marchini M. A model for type II collagen fibrils: distinctive D-band patterns in native and reconstituted fibrils compared with sequence data for helix and telopeptide domains. Biopolymers 2000, 54:448-463.
    • (2000) Biopolymers , vol.54 , pp. 448-463
    • Ortolani, F.1    Giordano, M.2    Marchini, M.3
  • 45
    • 73349125502 scopus 로고    scopus 로고
    • Collagen-binding peptidoglycans: a biomimetic approach to modulate collagen fibrillogenesis for tissue engineering applications
    • Paderi J.E., Sistiabudi R., Ivanisevic A., Panitch A. Collagen-binding peptidoglycans: a biomimetic approach to modulate collagen fibrillogenesis for tissue engineering applications. Tissue Eng. Part A 2009, 15:2991-2999.
    • (2009) Tissue Eng. Part A , vol.15 , pp. 2991-2999
    • Paderi, J.E.1    Sistiabudi, R.2    Ivanisevic, A.3    Panitch, A.4
  • 46
    • 0020405082 scopus 로고
    • A role for glycosaminoglycans in the development of collagen fibrils
    • Parry D.A., Flint M.H., Gillard G.C., Craig A.S. A role for glycosaminoglycans in the development of collagen fibrils. FEBS Lett. 1982, 149:1-7.
    • (1982) FEBS Lett. , vol.149 , pp. 1-7
    • Parry, D.A.1    Flint, M.H.2    Gillard, G.C.3    Craig, A.S.4
  • 47
    • 42949135530 scopus 로고    scopus 로고
    • Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis
    • Perumal S., Antipova O., Orgel J.P. Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:2824-2829.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 2824-2829
    • Perumal, S.1    Antipova, O.2    Orgel, J.P.3
  • 48
    • 3142725746 scopus 로고    scopus 로고
    • Quantitative analysis of fibronectin fibrillogenesis by endothelial cells on biomaterials
    • Pompe T., Mitdank C., Werner C. Quantitative analysis of fibronectin fibrillogenesis by endothelial cells on biomaterials. J. Phys. Condes Matter 2004, 16:S2421-S2426.
    • (2004) J. Phys. Condes Matter , vol.16
    • Pompe, T.1    Mitdank, C.2    Werner, C.3
  • 49
    • 27744560439 scopus 로고    scopus 로고
    • Fibronectin fibril pattern displays the force balance of cell-matrix adhesion
    • Pompe T., Keller K., Mitdank C., Werner C. Fibronectin fibril pattern displays the force balance of cell-matrix adhesion. Eur. Biophys. J. Biophys. Lett. 2005, 34:1049-1056.
    • (2005) Eur. Biophys. J. Biophys. Lett. , vol.34 , pp. 1049-1056
    • Pompe, T.1    Keller, K.2    Mitdank, C.3    Werner, C.4
  • 50
    • 18844409098 scopus 로고    scopus 로고
    • Molecular-scale topographic cues induce the orientation and directional movement of fibroblasts on two-dimensional collagen surfaces
    • Poole K., Khairy K., Friedrichs J., Franz C., Cisneros D.A., Howard J., Mueller D. Molecular-scale topographic cues induce the orientation and directional movement of fibroblasts on two-dimensional collagen surfaces. J. Mol. Biol. 2005, 349:380-386.
    • (2005) J. Mol. Biol. , vol.349 , pp. 380-386
    • Poole, K.1    Khairy, K.2    Friedrichs, J.3    Franz, C.4    Cisneros, D.A.5    Howard, J.6    Mueller, D.7
  • 51
    • 0027154689 scopus 로고
    • Regulation of corneal collagen fibrillogenesis in vitro by corneal proteoglycan (lumican and decorin) core proteins
    • Rada J.A., Cornuet P.K., Hassell J.R. Regulation of corneal collagen fibrillogenesis in vitro by corneal proteoglycan (lumican and decorin) core proteins. Exp. Eye Res. 1993, 56:635-648.
    • (1993) Exp. Eye Res. , vol.56 , pp. 635-648
    • Rada, J.A.1    Cornuet, P.K.2    Hassell, J.R.3
  • 52
    • 67649472791 scopus 로고    scopus 로고
    • Local strain measurement reveals a varied regional dependence of tensile tendon mechanics on glycosaminoglycan content
    • Rigozzi S., Muller R., Snedeker J.G. Local strain measurement reveals a varied regional dependence of tensile tendon mechanics on glycosaminoglycan content. J. Biomech. 2009, 42:1547-1552.
    • (2009) J. Biomech. , vol.42 , pp. 1547-1552
    • Rigozzi, S.1    Muller, R.2    Snedeker, J.G.3
  • 53
    • 84879883969 scopus 로고    scopus 로고
    • Tendon glycosaminoglycan proteoglycan sidechains promote collagen fibril sliding-AFM observations at the nanoscale
    • Rigozzi S., Muller R., Stemmer A., Snedeker J.G. Tendon glycosaminoglycan proteoglycan sidechains promote collagen fibril sliding-AFM observations at the nanoscale. J Biomech. 2013, 46:813-818.
    • (2013) J Biomech. , vol.46 , pp. 813-818
    • Rigozzi, S.1    Muller, R.2    Stemmer, A.3    Snedeker, J.G.4
  • 54
    • 0025851389 scopus 로고
    • Copolymerization of pNcollagen III and collagen I. pNcollagen III decreases the rate of incorporation of collagen I into fibrils, the amount of collagen I incorporated, and the diameter of the fibrils formed
    • Romanic A.M., Adachi E., Kadler K.E., Hojima Y., Prockop D.J. Copolymerization of pNcollagen III and collagen I. pNcollagen III decreases the rate of incorporation of collagen I into fibrils, the amount of collagen I incorporated, and the diameter of the fibrils formed. J. Biol. Chem. 1991, 266:12703-12709.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12703-12709
    • Romanic, A.M.1    Adachi, E.2    Kadler, K.E.3    Hojima, Y.4    Prockop, D.J.5
  • 55
    • 34547796856 scopus 로고    scopus 로고
    • The glycosaminoglycan chain of decorin plays an important role in collagen fibril formation at the early stages of fibrillogenesis
    • Ruhland C., Schonherr E., Robenek H., Hansen U., Iozzo R.V., Bruckner P., Seidler D.G. The glycosaminoglycan chain of decorin plays an important role in collagen fibril formation at the early stages of fibrillogenesis. FEBS J. 2007, 274:4246-4255.
    • (2007) FEBS J. , vol.274 , pp. 4246-4255
    • Ruhland, C.1    Schonherr, E.2    Robenek, H.3    Hansen, U.4    Iozzo, R.V.5    Bruckner, P.6    Seidler, D.G.7
  • 56
    • 52049122865 scopus 로고    scopus 로고
    • Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction
    • Schaefer L., Iozzo R.V. Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction. J. Biol. Chem. 2008, 283:21305-21309.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21305-21309
    • Schaefer, L.1    Iozzo, R.V.2
  • 58
    • 0030016013 scopus 로고    scopus 로고
    • Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen
    • Scott J.E. Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen. Biochemistry 1996, 35:8795-8799.
    • (1996) Biochemistry , vol.35 , pp. 8795-8799
    • Scott, J.E.1
  • 59
    • 0346242689 scopus 로고    scopus 로고
    • Elasticity in extracellular matrix 'shape modules' of tendon, cartilage, etc. A sliding proteoglycan-filament model
    • Scott J.E. Elasticity in extracellular matrix 'shape modules' of tendon, cartilage, etc. A sliding proteoglycan-filament model. J. Physiol. 2003, 553:335-343.
    • (2003) J. Physiol. , vol.553 , pp. 335-343
    • Scott, J.E.1
  • 60
    • 0019490438 scopus 로고
    • Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region
    • Scott J.E., Orford C.R. Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region. Biochem. J. 1981, 197:213-216.
    • (1981) Biochem. J. , vol.197 , pp. 213-216
    • Scott, J.E.1    Orford, C.R.2
  • 62
    • 8144221077 scopus 로고    scopus 로고
    • Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan
    • Scott P.G., McEwan P.A., Dodd C.M., Bergmann E.M., Bishop P.N., Bella J. Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:15633-15638.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 15633-15638
    • Scott, P.G.1    McEwan, P.A.2    Dodd, C.M.3    Bergmann, E.M.4    Bishop, P.N.5    Bella, J.6
  • 63
    • 33745616078 scopus 로고    scopus 로고
    • Defective glycosylation of decorin and biglycan, altered collagen structure, and abnormal phenotype of the skin fibroblasts of an Ehlers-Danlos syndrome patient carrying the novel Arg270Cys substitution in galactosyltransferase I (beta4GalT-7)
    • Seidler D.G., Faiyaz-Ul-Haque M., Hansen U., Yip G.W., Zaidi S.H., Teebi A.S., Kiesel L., Gotte M. Defective glycosylation of decorin and biglycan, altered collagen structure, and abnormal phenotype of the skin fibroblasts of an Ehlers-Danlos syndrome patient carrying the novel Arg270Cys substitution in galactosyltransferase I (beta4GalT-7). J. Mol. Med. (Ber.) 2006, 84:583-594.
    • (2006) J. Mol. Med. (Ber.) , vol.84 , pp. 583-594
    • Seidler, D.G.1    Faiyaz-Ul-Haque, M.2    Hansen, U.3    Yip, G.W.4    Zaidi, S.H.5    Teebi, A.S.6    Kiesel, L.7    Gotte, M.8
  • 64
    • 84867025824 scopus 로고    scopus 로고
    • Structure and function of ECM-inspired composite collagen type I scaffolds
    • Stamov D.R., Pompe T. Structure and function of ECM-inspired composite collagen type I scaffolds. Soft Matter 2012, 8:10200-10212.
    • (2012) Soft Matter , vol.8 , pp. 10200-10212
    • Stamov, D.R.1    Pompe, T.2
  • 65
    • 35348972929 scopus 로고    scopus 로고
    • Heparin intercalation into reconstituted collagen I fibrils: impact on growth kinetics and morphology
    • Stamov D., Grimmer M., Salchert K., Pompe T., Werner C. Heparin intercalation into reconstituted collagen I fibrils: impact on growth kinetics and morphology. Biomaterials 2008, 29:1-14.
    • (2008) Biomaterials , vol.29 , pp. 1-14
    • Stamov, D.1    Grimmer, M.2    Salchert, K.3    Pompe, T.4    Werner, C.5
  • 66
    • 70049114260 scopus 로고    scopus 로고
    • Structural polymorphism of collagen type I-heparin cofibrils
    • Stamov D., Salchert K., Springer A., Werner C., Pompe T. Structural polymorphism of collagen type I-heparin cofibrils. Soft Matter 2009, 5:3461-3468.
    • (2009) Soft Matter , vol.5 , pp. 3461-3468
    • Stamov, D.1    Salchert, K.2    Springer, A.3    Werner, C.4    Pompe, T.5
  • 67
    • 0040436000 scopus 로고    scopus 로고
    • Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon
    • Svensson L., Aszodi A., Reinholt F.P., Fassler R., Heinegard D., Oldberg A. Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon. J. Biol. Chem. 1999, 274:9636-9647.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9636-9647
    • Svensson, L.1    Aszodi, A.2    Reinholt, F.P.3    Fassler, R.4    Heinegard, D.5    Oldberg, A.6
  • 68
    • 0029778529 scopus 로고    scopus 로고
    • Model structure of decorin and implications for collagen fibrillogenesis
    • Weber I.T., Harrison R.W., Iozzo R.V. Model structure of decorin and implications for collagen fibrillogenesis. J. Biol. Chem. 1996, 271:31767-31770.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31767-31770
    • Weber, I.T.1    Harrison, R.W.2    Iozzo, R.V.3
  • 70
    • 0001358435 scopus 로고
    • The formation of fibrils from collagen solutions. 3. Effect of chondroitin sulphate and some other naturally occurring polyanions on the rate of formation
    • Wood G.C. The formation of fibrils from collagen solutions. 3. Effect of chondroitin sulphate and some other naturally occurring polyanions on the rate of formation. Biochem. J. 1960, 75:605-612.
    • (1960) Biochem. J. , vol.75 , pp. 605-612
    • Wood, G.C.1


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