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Volumn 43, Issue 2-3, 2012, Pages 205-214

Biochemical and anisotropical properties of tendons

Author keywords

Collagen; Extracellular matrix; Optical anisotropies; Organization; Tendons

Indexed keywords

ANISOTROPIC OPTICAL PROPERTIES; BIOMECHANICAL PROPERTIES; COLLAGEN MOLECULES; CONNECTIVE TISSUES; EXTRACELLULAR MATRICES; FIBER BUNDLES; LINEAR DICHROISM; MECHANICAL STRESS; ORGANIZATION; PROTEOGLYCANS; STRUCTURAL ORGANIZATION; SUPRAMOLECULAR ORGANIZATIONS;

EID: 84855215770     PISSN: 09684328     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micron.2011.07.015     Document Type: Article
Times cited : (51)

References (164)
  • 1
    • 0037383253 scopus 로고    scopus 로고
    • Synthesis and degradation of type IV collagen in rat skeletal muscle during immobilization in shortened and lengthened positions
    • Ahtikoski A.M., Koskinen S.O.A., Virtanen P., Kovanen V., Risteli J., Takala T.E.S. Synthesis and degradation of type IV collagen in rat skeletal muscle during immobilization in shortened and lengthened positions. Acta Physiol. Scand. 2003, 177:473-481.
    • (2003) Acta Physiol. Scand. , vol.177 , pp. 473-481
    • Ahtikoski, A.M.1    Koskinen, S.O.A.2    Virtanen, P.3    Kovanen, V.4    Risteli, J.5    Takala, T.E.S.6
  • 2
    • 36049045713 scopus 로고    scopus 로고
    • Optical anisotropies in corneal stroma collagen fibers from diabetic spontaneous mice
    • Aldrovani M., Guaraldo A.M., Vidal B.C. Optical anisotropies in corneal stroma collagen fibers from diabetic spontaneous mice. Vision Res. 2007, 47(26):3229-3237.
    • (2007) Vision Res. , vol.47 , Issue.26 , pp. 3229-3237
    • Aldrovani, M.1    Guaraldo, A.M.2    Vidal, B.C.3
  • 3
    • 0026234179 scopus 로고
    • Energy-saving mechanisms in walking and running
    • Alexander R.M. Energy-saving mechanisms in walking and running. J. Exp. Biol. 1991, 160:55-69.
    • (1991) J. Exp. Biol. , vol.160 , pp. 55-69
    • Alexander, R.M.1
  • 4
    • 0017338764 scopus 로고    scopus 로고
    • Storage of elastic strain energy in muscle and other tissues
    • Alexander R.M., Bennet-Clark H.C. Storage of elastic strain energy in muscle and other tissues. Nature 1997, 265:114-117.
    • (1997) Nature , vol.265 , pp. 114-117
    • Alexander, R.M.1    Bennet-Clark, H.C.2
  • 5
    • 2442677996 scopus 로고    scopus 로고
    • Detecting structural changes in early experimental osteoarthritis of tibial cartilage by microscopic magnetic resonance imaging and polarised light microscopy
    • Alhadlaq H., Xia Y., Moody J., Matyas J. Detecting structural changes in early experimental osteoarthritis of tibial cartilage by microscopic magnetic resonance imaging and polarised light microscopy. Ann. Rheum. Dis. 2004, 63(6):709-717.
    • (2004) Ann. Rheum. Dis. , vol.63 , Issue.6 , pp. 709-717
    • Alhadlaq, H.1    Xia, Y.2    Moody, J.3    Matyas, J.4
  • 7
    • 0033137092 scopus 로고    scopus 로고
    • Biomechanical, histological and immunohistological studies of patellar cartilage in an ovine model of osteoarthritis induced by lateral meniscectomy
    • Appleyard R.C., Ghosh P., Swain M.V. Biomechanical, histological and immunohistological studies of patellar cartilage in an ovine model of osteoarthritis induced by lateral meniscectomy. Osteoarthritis Cartilage 1999, 7:281-294.
    • (1999) Osteoarthritis Cartilage , vol.7 , pp. 281-294
    • Appleyard, R.C.1    Ghosh, P.2    Swain, M.V.3
  • 8
    • 57749102882 scopus 로고    scopus 로고
    • Biomechanical behavior and response of biological tissues to stress and immobilization
    • Aquino C.F., Viana S.O., Fonseca S.T. Biomechanical behavior and response of biological tissues to stress and immobilization. Physiother. Mov. 2005, 18(2):35-43.
    • (2005) Physiother. Mov. , vol.18 , Issue.2 , pp. 35-43
    • Aquino, C.F.1    Viana, S.O.2    Fonseca, S.T.3
  • 9
    • 57749100543 scopus 로고    scopus 로고
    • Structural and biochemical analysis of the effect of immobilization followed by stretching on the calcaneal tendon of rats
    • Aro A.A., Vidal B.C., Tomiosso T.C., Matiello-Rosa S.M.G., GOMES L., Pimentel E.R. Structural and biochemical analysis of the effect of immobilization followed by stretching on the calcaneal tendon of rats. Connect. Tissue Res. 2008, 49:443-454.
    • (2008) Connect. Tissue Res. , vol.49 , pp. 443-454
    • Aro, A.A.1    Vidal, B.C.2    Tomiosso, T.C.3    Matiello-Rosa, S.M.G.4    Gomes, L.5    Pimentel, E.R.6
  • 13
    • 0034014229 scopus 로고    scopus 로고
    • The cell and development biology of tendons and ligaments
    • Benjamim M., Ralphs J.R. The cell and development biology of tendons and ligaments. Int. Rev. Cytol. 2000, 196:85-130.
    • (2000) Int. Rev. Cytol. , vol.196 , pp. 85-130
    • Benjamim, M.1    Ralphs, J.R.2
  • 14
    • 0026326442 scopus 로고
    • Age-related changes in tendon fibrocartilage
    • Benjamin M., Tyers R.N.S., Ralphs J.R. Age-related changes in tendon fibrocartilage. J. Anat. 1991, 179:127-136.
    • (1991) J. Anat. , vol.179 , pp. 127-136
    • Benjamin, M.1    Tyers, R.N.S.2    Ralphs, J.R.3
  • 15
    • 0038165038 scopus 로고    scopus 로고
    • Linear dichroism of the retinal nerve fiber layer expressed with mueller matrices
    • Benoit A.M., Naoun K., Louis-Dorr V., Mala L., Naspiller A. Linear dichroism of the retinal nerve fiber layer expressed with mueller matrices. Appl. Opt. 2001, 40(4):565-569.
    • (2001) Appl. Opt. , vol.40 , Issue.4 , pp. 565-569
    • Benoit, A.M.1    Naoun, K.2    Louis-Dorr, V.3    Mala, L.4    Naspiller, A.5
  • 16
    • 77954681746 scopus 로고    scopus 로고
    • Obesity affects collagen fibril diameter and mechanical properties of tendons in zucker rats
    • Biancalana A., Velloso L.A., Gomes L. Obesity affects collagen fibril diameter and mechanical properties of tendons in zucker rats. Connect. Tissue Res. 2010, 51:171-178.
    • (2010) Connect. Tissue Res. , vol.51 , pp. 171-178
    • Biancalana, A.1    Velloso, L.A.2    Gomes, L.3
  • 18
    • 0030198753 scopus 로고    scopus 로고
    • Characterization of fibril segments from chicken embryo cornea, dermis and tendon
    • Birk D.E., Hahn R.A., Linsemayer C.Y., Zycband E.I. Characterization of fibril segments from chicken embryo cornea, dermis and tendon. Matrix Biol. 1996, 15:111-118.
    • (1996) Matrix Biol. , vol.15 , pp. 111-118
    • Birk, D.E.1    Hahn, R.A.2    Linsemayer, C.Y.3    Zycband, E.I.4
  • 20
    • 34247533278 scopus 로고    scopus 로고
    • Picrosirius-polarization staining method as an efficient histopathological tool for collagenolysis detection in vesical prolapse lesions
    • Borges L.F., Gutierrez P.S., Marana H.R.C., Taboga S.R. Picrosirius-polarization staining method as an efficient histopathological tool for collagenolysis detection in vesical prolapse lesions. Micron 2007, 38:580-583.
    • (2007) Micron , vol.38 , pp. 580-583
    • Borges, L.F.1    Gutierrez, P.S.2    Marana, H.R.C.3    Taboga, S.R.4
  • 21
    • 80051827463 scopus 로고    scopus 로고
    • The effect of platelet-rich plasma on the neovascularization of surgically created equine superficial digital flexor tendon lesions
    • March 10 [Epub ahead of print]
    • Bosch G., Moleman M., Barneveld A., van Weeren P.R., van Schie H.T. The effect of platelet-rich plasma on the neovascularization of surgically created equine superficial digital flexor tendon lesions. Scand. J. Med. Sci. Sports 2010, March 10 [Epub ahead of print].
    • (2010) Scand. J. Med. Sci. Sports
    • Bosch, G.1    Moleman, M.2    Barneveld, A.3    van Weeren, P.R.4    van Schie, H.T.5
  • 25
    • 0033229742 scopus 로고    scopus 로고
    • Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlate with cleavage of pp125FAK, paxillin and talin
    • Carragher N.O., Levkau B., Ross R., Raines E.W. Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlate with cleavage of pp125FAK, paxillin and talin. J. Cell. Biol. 1999, 147:619-629.
    • (1999) J. Cell. Biol. , vol.147 , pp. 619-629
    • Carragher, N.O.1    Levkau, B.2    Ross, R.3    Raines, E.W.4
  • 27
    • 0033963218 scopus 로고    scopus 로고
    • Integrin signaling potential for mediating gene expression in hypertrophying skeletal muscle
    • Carson J.A., Wei L. Integrin signaling potential for mediating gene expression in hypertrophying skeletal muscle. J. Appl. Physiol. 2000, 88:337-343.
    • (2000) J. Appl. Physiol. , vol.88 , pp. 337-343
    • Carson, J.A.1    Wei, L.2
  • 28
    • 0033928093 scopus 로고    scopus 로고
    • Structure and proteoglycan composition of specialized regions of the elastic tendon of the chicken wing
    • Carvalho H.F., Felisbino S.L., Covizi D.Z., Della Colleta H.H.M., Gomes L. Structure and proteoglycan composition of specialized regions of the elastic tendon of the chicken wing. Cell Tissue Res. 2000, 300:435-446.
    • (2000) Cell Tissue Res. , vol.300 , pp. 435-446
    • Carvalho, H.F.1    Felisbino, S.L.2    Covizi, D.Z.3    Della Colleta, H.H.M.4    Gomes, L.5
  • 29
    • 0028587552 scopus 로고
    • Cell types and evidence for traumatic cell death in a pressure-bearing tendon of Rana catesbeiana
    • Carvalho H.F., Vidal B.C. Cell types and evidence for traumatic cell death in a pressure-bearing tendon of Rana catesbeiana. Tissue Cell. 1994, 26(6):841-848.
    • (1994) Tissue Cell. , vol.26 , Issue.6 , pp. 841-848
    • Carvalho, H.F.1    Vidal, B.C.2
  • 30
    • 33745900253 scopus 로고    scopus 로고
    • Identification, content and distribution of type VI collagen in bovine tendons
    • Carvalho H.F., Felisbino S.L., Vogel K., Douglas K. Identification, content and distribution of type VI collagen in bovine tendons. Cell Tissue Res. 2006, 325(2):315-324.
    • (2006) Cell Tissue Res. , vol.325 , Issue.2 , pp. 315-324
    • Carvalho, H.F.1    Felisbino, S.L.2    Vogel, K.3    Douglas, K.4
  • 31
    • 0014402241 scopus 로고
    • Birefringence of muscle proteins and the problem of structural birefringence
    • Cassim J.Y., Tobias O.S. Birefringence of muscle proteins and the problem of structural birefringence. Biochem. Biophys. Acta 1968, 168:462-471.
    • (1968) Biochem. Biophys. Acta , vol.168 , pp. 462-471
    • Cassim, J.Y.1    Tobias, O.S.2
  • 33
    • 0032730185 scopus 로고    scopus 로고
    • Regulation of extracellular matrix gene expression by mechanical stress
    • Chiquet M. Regulation of extracellular matrix gene expression by mechanical stress. Matrix Biol. 1999, 18:417-426.
    • (1999) Matrix Biol. , vol.18 , pp. 417-426
    • Chiquet, M.1
  • 35
    • 0037360165 scopus 로고    scopus 로고
    • How do fibroblasts translate mechanical signals into changes in extracellular matrix production?
    • Chiquet M., Renedo A.S., Huber F., Flück M. How do fibroblasts translate mechanical signals into changes in extracellular matrix production?. Matrix Biol. 2003, 22:73-80.
    • (2003) Matrix Biol. , vol.22 , pp. 73-80
    • Chiquet, M.1    Renedo, A.S.2    Huber, F.3    Flück, M.4
  • 36
    • 0004178094 scopus 로고    scopus 로고
    • Extracellular matrix: tissue function
    • Harwood Academic, Amsterdam
    • Comper W.D. Extracellular matrix: tissue function. Tendon and Ligaments 1996, vol. 1:303-327. Harwood Academic, Amsterdam.
    • (1996) Tendon and Ligaments , vol.1 , pp. 303-327
    • Comper, W.D.1
  • 37
    • 33947256096 scopus 로고    scopus 로고
    • Hormone therapy is associated with smaller Achilles tendon diameter in active post-menopausal women
    • Cook J.L., Bass S.L., Black J.E. Hormone therapy is associated with smaller Achilles tendon diameter in active post-menopausal women. Scand. J. Med. Sci. Sports 2007, 17(2):128-132.
    • (2007) Scand. J. Med. Sci. Sports , vol.17 , Issue.2 , pp. 128-132
    • Cook, J.L.1    Bass, S.L.2    Black, J.E.3
  • 42
    • 0035058027 scopus 로고    scopus 로고
    • Proteoglycans and glycosaminoglycan fine structures in the mouse tail tendon fascicle
    • Derwin K.A., Soslowsky L.J., Kimura J.H., Plaas A.H. Proteoglycans and glycosaminoglycan fine structures in the mouse tail tendon fascicle. J. Orthop. Res. 2001, 19:269-277.
    • (2001) J. Orthop. Res. , vol.19 , pp. 269-277
    • Derwin, K.A.1    Soslowsky, L.J.2    Kimura, J.H.3    Plaas, A.H.4
  • 44
    • 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(8):2388-2393.
    • (2006) Biomacromolecules , vol.7 , Issue.8 , pp. 2388-2393
    • Douglas, T.1    Heinemann, S.2    Bierbaum, S.3    Scharnweber, D.4    Worch, H.5
  • 45
    • 0032884730 scopus 로고    scopus 로고
    • Involvement of long- and short-range signalling during early tendon development
    • D'Souza D., Patel K. Involvement of long- and short-range signalling during early tendon development. Anat. Embryol. 1999, 200:367-375.
    • (1999) Anat. Embryol. , vol.200 , pp. 367-375
    • D'Souza, D.1    Patel, K.2
  • 46
    • 34447626457 scopus 로고    scopus 로고
    • Aging enhances a mechanically-induced reduction in tendon strength by an active process involving matrix metalloproteinase activity
    • Dudhia J., Scott C.M., Draper E.R., Heinegård D., Pitsillides A.A., Smith R.K. Aging enhances a mechanically-induced reduction in tendon strength by an active process involving matrix metalloproteinase activity. Aging Cell. 2007, 6(4):547-556.
    • (2007) Aging Cell. , vol.6 , Issue.4 , pp. 547-556
    • Dudhia, J.1    Scott, C.M.2    Draper, E.R.3    Heinegård, D.4    Pitsillides, A.A.5    Smith, R.K.6
  • 47
    • 34247525444 scopus 로고    scopus 로고
    • Ultrastructural characteristics of tensional regions in tendons from rats of different ages
    • Esquisatto M.A.M., Joazeiro P.P., Pimentel E.R., Gomes L. Ultrastructural characteristics of tensional regions in tendons from rats of different ages. Braz. J. Morphol. Sci. 2003, 20(2):109-114.
    • (2003) Braz. J. Morphol. Sci. , vol.20 , Issue.2 , pp. 109-114
    • Esquisatto, M.A.M.1    Joazeiro, P.P.2    Pimentel, E.R.3    Gomes, L.4
  • 48
    • 34247484449 scopus 로고    scopus 로고
    • The effect of age on the structure and composition of rat tendon fibrocartilage
    • Esquisatto M.A.M., Joazeiro P.P., Pimentel E.R., Gomes L. The effect of age on the structure and composition of rat tendon fibrocartilage. Cell Biol. Int. 2007, 31:570-577.
    • (2007) Cell Biol. Int. , vol.31 , pp. 570-577
    • Esquisatto, M.A.M.1    Joazeiro, P.P.2    Pimentel, E.R.3    Gomes, L.4
  • 49
    • 0025674031 scopus 로고
    • Ultrastructure and proteoglycan composition in the developing fibrocartilaginous region of bovine tendon
    • Evanko S.P., Vogel K.G. Ultrastructure and proteoglycan composition in the developing fibrocartilaginous region of bovine tendon. Matrix 1990, 10(6):420-436.
    • (1990) Matrix , vol.10 , Issue.6 , pp. 420-436
    • Evanko, S.P.1    Vogel, K.G.2
  • 52
    • 0141500111 scopus 로고    scopus 로고
    • Variations in the glycosaminoglycans content, swelling properties and morphological aspects of different regions of the superficial digital flexor tendon of pigs
    • Feitosa V.L.C., Esquisatto M.A.M., Joazeiro P.P., Gomes L., Felisbino S.L., Pimentel E.R. Variations in the glycosaminoglycans content, swelling properties and morphological aspects of different regions of the superficial digital flexor tendon of pigs. Cell. Mol. Biol. 2002, 48:359-369.
    • (2002) Cell. Mol. Biol. , vol.48 , pp. 359-369
    • Feitosa, V.L.C.1    Esquisatto, M.A.M.2    Joazeiro, P.P.3    Gomes, L.4    Felisbino, S.L.5    Pimentel, E.R.6
  • 53
    • 0036205806 scopus 로고    scopus 로고
    • Optical anisitropy of a pig tendon under compression
    • Feitosa V.L.C., Vidal B.C., Pimentel E.R. Optical anisitropy of a pig tendon under compression. J. Anat. 2002, 200(1):105-110.
    • (2002) J. Anat. , vol.200 , Issue.1 , pp. 105-110
    • Feitosa, V.L.C.1    Vidal, B.C.2    Pimentel, E.R.3
  • 55
    • 33745831894 scopus 로고    scopus 로고
    • Comparative ultrastructural analysis of different regions of two digital flexor tendons of pigs
    • Feitosa V.L.C., Reis F.P., Esquisatto M.A.M., Joazeiro P.P., Vidal B.C., Pimentel E.R. Comparative ultrastructural analysis of different regions of two digital flexor tendons of pigs. Micron 2006, 37:518-525.
    • (2006) Micron , vol.37 , pp. 518-525
    • Feitosa, V.L.C.1    Reis, F.P.2    Esquisatto, M.A.M.3    Joazeiro, P.P.4    Vidal, B.C.5    Pimentel, E.R.6
  • 56
    • 0033112846 scopus 로고    scopus 로고
    • Identification na distribution type VI collagen in tendon fibrocartilages
    • Felisbino S.L., Carvalho H.F. Identification na distribution type VI collagen in tendon fibrocartilages. J. Submicrosc. Cytol. Pathol. 1999, 31(2):187-195.
    • (1999) J. Submicrosc. Cytol. Pathol. , vol.31 , Issue.2 , pp. 187-195
    • Felisbino, S.L.1    Carvalho, H.F.2
  • 57
    • 77949266012 scopus 로고    scopus 로고
    • Effect of high intensity aerobic exercise and mesterolone on remodeling of Achilles tendon of C57BL/6 transgenic mice
    • Fontana K., Almeida F.M., Tomiosso T.C., Pimentel E.R., Cruz Höfling M.A. Effect of high intensity aerobic exercise and mesterolone on remodeling of Achilles tendon of C57BL/6 transgenic mice. Cell Tissue Res. 2010, 339:411-420.
    • (2010) Cell Tissue Res. , vol.339 , pp. 411-420
    • Fontana, K.1    Almeida, F.M.2    Tomiosso, T.C.3    Pimentel, E.R.4    Cruz Höfling, M.A.5
  • 58
    • 79955464201 scopus 로고    scopus 로고
    • Diabetes mellitus alters the mechanical properties of the native tendon in an experimental rat model
    • Fox A.J., Bedi A., Deng X.H., Ying L., Harris P.E., Warren R.F., Rodeo S.A. Diabetes mellitus alters the mechanical properties of the native tendon in an experimental rat model. J. Orthop. Res. 2011, 29(6):880-885.
    • (2011) J. Orthop. Res. , vol.29 , Issue.6 , pp. 880-885
    • Fox, A.J.1    Bedi, A.2    Deng, X.H.3    Ying, L.4    Harris, P.E.5    Warren, R.F.6    Rodeo, S.A.7
  • 60
    • 34648843343 scopus 로고    scopus 로고
    • Ultrastructural immunolocalization of cartilage oligomeric matrix protein, thrombospondin-4, and collagen fibril size in rodent Achilles tendon in relation to exercise
    • Fredrick S., Stina E., Anja N., Frank Z., Dick H., Kjell H. Ultrastructural immunolocalization of cartilage oligomeric matrix protein, thrombospondin-4, and collagen fibril size in rodent Achilles tendon in relation to exercise. Connect. Tissue Res. 2007, 48:254-262.
    • (2007) Connect. Tissue Res. , vol.48 , pp. 254-262
    • Fredrick, S.1    Stina, E.2    Anja, N.3    Frank, Z.4    Dick, H.5    Kjell, H.6
  • 61
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch S.M., Vuori K., Ruoslahti E., Chan H.P. Control of adhesion-dependent cell survival by focal adhesion kinase. J. Cell. Biol. 1996, 134:793-799.
    • (1996) J. Cell. Biol. , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan, H.P.4
  • 62
    • 0025726552 scopus 로고
    • Crimp morphology in the fibre-forming collagens
    • Gathercole L.J., Keller A. Crimp morphology in the fibre-forming collagens. Matrix 1991, 11:214-234.
    • (1991) Matrix , vol.11 , pp. 214-234
    • Gathercole, L.J.1    Keller, A.2
  • 63
    • 0242710145 scopus 로고    scopus 로고
    • Collagens-structure, function, and biosynthesis
    • Gelse K., Pöschl E., Aigner T. Collagens-structure, function, and biosynthesis. Adv. Drug Deliv. Rev. 2003, 55(12):1531-1546.
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , Issue.12 , pp. 1531-1546
    • Gelse, K.1    Pöschl, E.2    Aigner, T.3
  • 64
    • 0035853388 scopus 로고    scopus 로고
    • Integrin-mediated mechanotransduction in vascular smooth muscle cells: frequency and force response characteristics
    • Goldschmidt M.E., McLeod K.J., Taylor W.R. Integrin-mediated mechanotransduction in vascular smooth muscle cells: frequency and force response characteristics. Circ. Res. 2001, 88:674-680.
    • (2001) Circ. Res. , vol.88 , pp. 674-680
    • Goldschmidt, M.E.1    McLeod, K.J.2    Taylor, W.R.3
  • 65
    • 77955422309 scopus 로고    scopus 로고
    • Protocol on induction of TMJ articular disc degeneration in rats by utilization of botulinum toxin
    • Guerra F.R., Pires I.L.S., Aro A.A., Camargo L.C., Pimentel E.R., Palomari E.T. Protocol on induction of TMJ articular disc degeneration in rats by utilization of botulinum toxin. Arch. Oral Biol. 2010, 55(7):530-534.
    • (2010) Arch. Oral Biol. , vol.55 , Issue.7 , pp. 530-534
    • Guerra, F.R.1    Pires, I.L.S.2    Aro, A.A.3    Camargo, L.C.4    Pimentel, E.R.5    Palomari, E.T.6
  • 67
    • 0035069134 scopus 로고    scopus 로고
    • Molecular basis of mechanotransduction in living cells
    • Hamill O.P., Martinac B. Molecular basis of mechanotransduction in living cells. Physiol. Rev. 2001, 81:685-740.
    • (2001) Physiol. Rev. , vol.81 , pp. 685-740
    • Hamill, O.P.1    Martinac, B.2
  • 68
    • 0020615381 scopus 로고
    • Quantitation of type I and type III collagen ratios in small samples of human tendon, blood vessels and atherosclerotic plaque
    • Hanson A.N., Bentley J.P. Quantitation of type I and type III collagen ratios in small samples of human tendon, blood vessels and atherosclerotic plaque. Anal. Biochem. 1983, 130:32-40.
    • (1983) Anal. Biochem. , vol.130 , pp. 32-40
    • Hanson, A.N.1    Bentley, J.P.2
  • 70
    • 22444441654 scopus 로고    scopus 로고
    • The ultrastructure of mouse articular cartilage: collagen orientation and implications for tissue functionality. A polarized light and scanning electron microscope study and review
    • Hughes L., Archer C., ap Gwynn I. The ultrastructure of mouse articular cartilage: collagen orientation and implications for tissue functionality. A polarized light and scanning electron microscope study and review. Eur. Cells Mater. 2005, 9:68-84.
    • (2005) Eur. Cells Mater. , vol.9 , pp. 68-84
    • Hughes, L.1    Archer, C.2    ap Gwynn, I.3
  • 71
    • 0028282547 scopus 로고
    • Cellular tensegrity: exploring how mechanical changes in the cytoskeleton regulate cell growth, migration and tissue pattern during morphogenesis
    • Ingber D.E., Dike L., Hansen L., Karp S., Liley H., Maniotis A., McNamee H., Mooney D., Plopper G., Sims J., Wang N. Cellular tensegrity: exploring how mechanical changes in the cytoskeleton regulate cell growth, migration and tissue pattern during morphogenesis. Int. Rev. Cytol. 1994, 150:173-224.
    • (1994) Int. Rev. Cytol. , vol.150 , pp. 173-224
    • Ingber, D.E.1    Dike, L.2    Hansen, L.3    Karp, S.4    Liley, H.5    Maniotis, A.6    McNamee, H.7    Mooney, D.8    Plopper, G.9    Sims, J.10    Wang, N.11
  • 72
    • 0032865578 scopus 로고    scopus 로고
    • Effect of tension on contraction-induced glucose transport in rat skeletal muscle
    • Ihlemann J., Ploug T., Hellsten Y., Galbo H. Effect of tension on contraction-induced glucose transport in rat skeletal muscle. Am. J. Physiol. Endocrinol. Metab. 1999, 277:208-214.
    • (1999) Am. J. Physiol. Endocrinol. Metab. , vol.277 , pp. 208-214
    • Ihlemann, J.1    Ploug, T.2    Hellsten, Y.3    Galbo, H.4
  • 73
    • 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
  • 74
    • 38849090654 scopus 로고    scopus 로고
    • Tendon: biology, biomechanics, repair, growth factors, and envolving treatment options
    • James R., Kesturu G., Balian G., Chhabra A.B. Tendon: biology, biomechanics, repair, growth factors, and envolving treatment options. J. Hand Surg. 2008, 33A:102-112.
    • (2008) J. Hand Surg. , vol.33 A , pp. 102-112
    • James, R.1    Kesturu, G.2    Balian, G.3    Chhabra, A.B.4
  • 75
    • 0141448766 scopus 로고    scopus 로고
    • Linear birefringence measurements of the in vitro human cornea
    • Jaronski J.W., Kasprzak H.T. Linear birefringence measurements of the in vitro human cornea. Ophthal. Physiol. Opt. 2003, 23(4):361-369.
    • (2003) Ophthal. Physiol. Opt. , vol.23 , Issue.4 , pp. 361-369
    • Jaronski, J.W.1    Kasprzak, H.T.2
  • 77
    • 84940618287 scopus 로고
    • Three-dimensional ultrastructure of human tendons
    • Józsa L., Kannus P., Balint B.J., Reffy A. Three-dimensional ultrastructure of human tendons. Acta Anat. 1991, 142:306-312.
    • (1991) Acta Anat. , vol.142 , pp. 306-312
    • Józsa, L.1    Kannus, P.2    Balint, B.J.3    Reffy, A.4
  • 78
    • 0026360247 scopus 로고
    • Sructure and macromolecular composition of the myotendineal junction. Histochemical immunohistochemical and electron microscopc study of the rat calt muscle
    • Józsa L., Kvist M., Kannus P., Vieno T., Järvinen M., Lehto M. Sructure and macromolecular composition of the myotendineal junction. Histochemical immunohistochemical and electron microscopc study of the rat calt muscle. Acta Morphol. Hung. 1991, 39(4):287-297.
    • (1991) Acta Morphol. Hung. , vol.39 , Issue.4 , pp. 287-297
    • Józsa, L.1    Kvist, M.2    Kannus, P.3    Vieno, T.4    Järvinen, M.5    Lehto, M.6
  • 79
    • 0001891919 scopus 로고    scopus 로고
    • Human tendons: anatomy, physiology and pathology
    • Human Kinetics, Champaign.
    • Józsa L.G., Kannus P. Human tendons: anatomy, physiology and pathology. Structure and Metabolism of Normal Tendons 1997, Human Kinetics, Champaign, pp. 46-97.
    • (1997) Structure and Metabolism of Normal Tendons , pp. 46-97
    • Józsa, L.G.1    Kannus, P.2
  • 80
    • 34247860597 scopus 로고    scopus 로고
    • Characterization of articular cartilage by combining microscopic analysis with a fibril-reinforced finite-element model
    • Julkunen P., Kiviranta P., Wilson W., Jurvelin J.S., Korhonen R.K. Characterization of articular cartilage by combining microscopic analysis with a fibril-reinforced finite-element model. J. Biomech. 2007, 40(8):1862-1870.
    • (2007) J. Biomech. , vol.40 , Issue.8 , pp. 1862-1870
    • Julkunen, P.1    Kiviranta, P.2    Wilson, W.3    Jurvelin, J.S.4    Korhonen, R.K.5
  • 82
    • 0034577312 scopus 로고    scopus 로고
    • Structure of the tendon connective tissue
    • Kannus P. Structure of the tendon connective tissue. Scand. J. Med. Sci. Sports 2000, 10:312-320.
    • (2000) Scand. J. Med. Sci. Sports , vol.10 , pp. 312-320
    • Kannus, P.1
  • 85
    • 1642313674 scopus 로고    scopus 로고
    • Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading
    • Kjaer M. Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading. Physiol. Rev. 2004, 84:649-698.
    • (2004) Physiol. Rev. , vol.84 , pp. 649-698
    • Kjaer, M.1
  • 87
    • 39749116324 scopus 로고    scopus 로고
    • Effect of uncompensated corneal polarization on the detection of localized retinal nerve fiber layer defects
    • Kogure S., Kohwa H., Tsukahara S. Effect of uncompensated corneal polarization on the detection of localized retinal nerve fiber layer defects. Ophthal. Res. 2008, 40(2):61-68.
    • (2008) Ophthal. Res. , vol.40 , Issue.2 , pp. 61-68
    • Kogure, S.1    Kohwa, H.2    Tsukahara, S.3
  • 88
    • 0026655518 scopus 로고
    • Biomechanical loading of Achilles tendon during normal locomotion
    • Komi P.V., Fukashiro S., Jarvinen M. Biomechanical loading of Achilles tendon during normal locomotion. Clin. Sports Med. 1992, 11:521-531.
    • (1992) Clin. Sports Med. , vol.11 , pp. 521-531
    • Komi, P.V.1    Fukashiro, S.2    Jarvinen, M.3
  • 89
    • 34250622360 scopus 로고    scopus 로고
    • Fluorescence spectroscopy and birefringence of molecular changes in maturing rat tail tendon
    • Korol R.M., Finlay H.M., Josseau M.J., Lucas A.R., Canham P.B. Fluorescence spectroscopy and birefringence of molecular changes in maturing rat tail tendon. J. Biomed. Opt. 2007, 12(2):024011.
    • (2007) J. Biomed. Opt. , vol.12 , Issue.2 , pp. 024011
    • Korol, R.M.1    Finlay, H.M.2    Josseau, M.J.3    Lucas, A.R.4    Canham, P.B.5
  • 90
    • 84855217767 scopus 로고    scopus 로고
    • Type-1 collagen turnover in peritendinous connective tissue after exercise determined by microdialysis
    • Langberg H., Skovgaard D., Petersen L.J., Bulow J., Kjaer M. Type-1 collagen turnover in peritendinous connective tissue after exercise determined by microdialysis. J. Physiol. 1999, 52:299-306.
    • (1999) J. Physiol. , vol.52 , pp. 299-306
    • Langberg, H.1    Skovgaard, D.2    Petersen, L.J.3    Bulow, J.4    Kjaer, M.5
  • 92
    • 2342532523 scopus 로고    scopus 로고
    • Disorders of the Achilles tendon
    • Lesic A., Bumbasirevic M. Disorders of the Achilles tendon. Curr. Orthop. 2004, 18:63-75.
    • (2004) Curr. Orthop. , vol.18 , pp. 63-75
    • Lesic, A.1    Bumbasirevic, M.2
  • 94
    • 0032856628 scopus 로고    scopus 로고
    • Rupture of the Achilles tendon
    • Maffulli N. Rupture of the Achilles tendon. J. Bone Joint Surg. Am. 1999, 81(7):1019-1036.
    • (1999) J. Bone Joint Surg. Am. , vol.81 , Issue.7 , pp. 1019-1036
    • Maffulli, N.1
  • 95
    • 0344873751 scopus 로고    scopus 로고
    • Tendon properties in relation to muscular activity and physical training
    • Magnusson S.P., Hansen P., Kjaer M. Tendon properties in relation to muscular activity and physical training. Scand. J. Med. Sci. Sports 2003, 13:211-223.
    • (2003) Scand. J. Med. Sci. Sports , vol.13 , pp. 211-223
    • Magnusson, S.P.1    Hansen, P.2    Kjaer, M.3
  • 96
    • 2142708564 scopus 로고    scopus 로고
    • Experimental tendon repair: glycosaminoglycan arrangement in newly synthesized collagen fibers
    • Mello M.L.S., Vidal B.C. Experimental tendon repair: glycosaminoglycan arrangement in newly synthesized collagen fibers. Cell. Mol. Biol. 2003, 49(4):579-585.
    • (2003) Cell. Mol. Biol. , vol.49 , Issue.4 , pp. 579-585
    • Mello, M.L.S.1    Vidal, B.C.2
  • 97
    • 0031657982 scopus 로고    scopus 로고
    • Fibrocartilages in the extensor tendons of the interphalangeal joints of human toes
    • Milz S., McNeilly C., Putz R., Ralphs J., Benjamin M. Fibrocartilages in the extensor tendons of the interphalangeal joints of human toes. Anat. Rec. 1998, 252:264-270.
    • (1998) Anat. Rec. , vol.252 , pp. 264-270
    • Milz, S.1    McNeilly, C.2    Putz, R.3    Ralphs, J.4    Benjamin, M.5
  • 98
    • 0036242693 scopus 로고    scopus 로고
    • Expression of a wide range of extracellular matrix molecules in the tendon and trochlea of the human superior oblique muscle
    • Milz S., Regner F., Putz R., Benjamin M. Expression of a wide range of extracellular matrix molecules in the tendon and trochlea of the human superior oblique muscle. Invest. Ophthalmol. Vis. Sci. 2002, 43(5):1330-1334.
    • (2002) Invest. Ophthalmol. Vis. Sci. , vol.43 , Issue.5 , pp. 1330-1334
    • Milz, S.1    Regner, F.2    Putz, R.3    Benjamin, M.4
  • 99
    • 0032456952 scopus 로고    scopus 로고
    • Comp (cartilage oligomeric matrix protein) is synthesized in ligament, tendon, meniscus, and cartilage
    • Muller G., Michel A., Altenburg E. Comp (cartilage oligomeric matrix protein) is synthesized in ligament, tendon, meniscus, and cartilage. Connect. Tissue Res. 1998, 39:233-244.
    • (1998) Connect. Tissue Res. , vol.39 , pp. 233-244
    • Muller, G.1    Michel, A.2    Altenburg, E.3
  • 101
    • 34648813848 scopus 로고    scopus 로고
    • Biomechanical and biochemical properties of chicken calcaneal tendon under effect of age and nonforced active exercise
    • Nakagaki W.R., Biancalana A., Benevides G.P., Gomes L. Biomechanical and biochemical properties of chicken calcaneal tendon under effect of age and nonforced active exercise. Connect. Tissue Res. 2007, 48:219-228.
    • (2007) Connect. Tissue Res. , vol.48 , pp. 219-228
    • Nakagaki, W.R.1    Biancalana, A.2    Benevides, G.P.3    Gomes, L.4
  • 102
    • 77954409662 scopus 로고    scopus 로고
    • The effect of age and spontaneous exercise on the biomechanical and biochemical properties of chicken superficial digital flexor tendon
    • Nakagaki W.R., Pimentel E.R., Benevides G.P., Gomes L. The effect of age and spontaneous exercise on the biomechanical and biochemical properties of chicken superficial digital flexor tendon. Connect. Tissue Res. 2010, 51:265-273.
    • (2010) Connect. Tissue Res. , vol.51 , pp. 265-273
    • Nakagaki, W.R.1    Pimentel, E.R.2    Benevides, G.P.3    Gomes, L.4
  • 103
    • 29244439951 scopus 로고    scopus 로고
    • Exploration of the retinal nerve fiber layer thickness by measurement of the linear dichroism
    • Naoun O.K., Dorr V.L., Allé P., Sablon J.C., Benoit A.M. Exploration of the retinal nerve fiber layer thickness by measurement of the linear dichroism. Appl. Opt. 2005, 44(33):7074-7082.
    • (2005) Appl. Opt. , vol.44 , Issue.33 , pp. 7074-7082
    • Naoun, O.K.1    Dorr, V.L.2    Allé, P.3    Sablon, J.C.4    Benoit, A.M.5
  • 104
    • 21844467550 scopus 로고    scopus 로고
    • All-optical control of microfluidic components using from birefringence
    • Neale S.L., MacDonald M.P., Dholakia K., Krauss T.F. All-optical control of microfluidic components using from birefringence. Nat. Mater. 2005, 4:530-533.
    • (2005) Nat. Mater. , vol.4 , pp. 530-533
    • Neale, S.L.1    MacDonald, M.P.2    Dholakia, K.3    Krauss, T.F.4
  • 105
    • 0031113402 scopus 로고    scopus 로고
    • Structure and metabolism of tendons
    • O'Brien M. Structure and metabolism of tendons. Scand. J. Med. Sci. Sports 1997, 7:55-61.
    • (1997) Scand. J. Med. Sci. Sports , vol.7 , pp. 55-61
    • O'Brien, M.1
  • 106
    • 79954431108 scopus 로고    scopus 로고
    • Metrenperone enhances collagen turnover and remodeling in the early stages of healing of tendon injury in rabbit
    • Oryan A., Silver I.A., Goodship A.E. Metrenperone enhances collagen turnover and remodeling in the early stages of healing of tendon injury in rabbit. Arch. Orthop. Trauma Surg. 2010, 130(12):1451-1457.
    • (2010) Arch. Orthop. Trauma Surg. , vol.130 , Issue.12 , pp. 1451-1457
    • Oryan, A.1    Silver, I.A.2    Goodship, A.E.3
  • 108
    • 0019776120 scopus 로고
    • Photometric studies on xylidine ponceau-collagen interaction
    • Pimentel R., Recco S.M., Graccho M. Photometric studies on xylidine ponceau-collagen interaction. Cell. Mol. Biol. 1981, 27(4):347-352.
    • (1981) Cell. Mol. Biol. , vol.27 , Issue.4 , pp. 347-352
    • Pimentel, R.1    Recco, S.M.2    Graccho, M.3
  • 109
    • 0037709393 scopus 로고    scopus 로고
    • Cellular aspects of elastogonesis in the elastic tendon of the chicken wing
    • Pimentel S.B., Carvalho H.F. Cellular aspects of elastogonesis in the elastic tendon of the chicken wing. Cell Biol. Int. 2003, 27:579-586.
    • (2003) Cell Biol. Int. , vol.27 , pp. 579-586
    • Pimentel, S.B.1    Carvalho, H.F.2
  • 111
    • 65849384082 scopus 로고    scopus 로고
    • The role of cartilage oligomeric matrix protein (COMP) in skeletal disease
    • Posey K.L., Hecht J.T. The role of cartilage oligomeric matrix protein (COMP) in skeletal disease. Curr. Drug Targets 2008, 9(10):869-877.
    • (2008) Curr. Drug Targets , vol.9 , Issue.10 , pp. 869-877
    • Posey, K.L.1    Hecht, J.T.2
  • 112
    • 79955372815 scopus 로고    scopus 로고
    • Inflammation, neovascularization and intra-plaque hemorrhage are associated with increased reparative collagen content: implication for plaque progression in diabetic atherosclerosis
    • Purushothaman K.R., Purushothaman M., Muntner P., Lento P.A., O'Connor W.N., Sharma S.K., Fuster V., Moreno P.R. Inflammation, neovascularization and intra-plaque hemorrhage are associated with increased reparative collagen content: implication for plaque progression in diabetic atherosclerosis. Vasc. Med. 2011, 16(2):103-108.
    • (2011) Vasc. Med. , vol.16 , Issue.2 , pp. 103-108
    • Purushothaman, K.R.1    Purushothaman, M.2    Muntner, P.3    Lento, P.A.4    O'Connor, W.N.5    Sharma, S.K.6    Fuster, V.7    Moreno, P.R.8
  • 113
    • 33845382338 scopus 로고    scopus 로고
    • Microstructural modeling of collagen network mechanics and interactions with the proteoglycan gel in articular cartilage
    • Quinn T.M., Morel V. Microstructural modeling of collagen network mechanics and interactions with the proteoglycan gel in articular cartilage. Biomech. Model Mechanobiol. 2007, 6(1-2):73-82.
    • (2007) Biomech. Model Mechanobiol. , vol.6 , Issue.1-2 , pp. 73-82
    • Quinn, T.M.1    Morel, V.2
  • 114
    • 4544276100 scopus 로고    scopus 로고
    • Flow linear dichroism to probe binding of aromatic molecules and DNA to single-walled carbon nanotubes
    • Rajendra J., Baxendale M., Dil Rap L.G., Rodger A. Flow linear dichroism to probe binding of aromatic molecules and DNA to single-walled carbon nanotubes. J. Am. Chem. Soc. 2004, 126(36):11182-11188.
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.36 , pp. 11182-11188
    • Rajendra, J.1    Baxendale, M.2    Dil Rap, L.G.3    Rodger, A.4
  • 115
    • 0038362684 scopus 로고    scopus 로고
    • Cell signalling events: a view from the matrix
    • Ramirez F., Rifkin D.B. Cell signalling events: a view from the matrix. Matrix Biol. 2003, 22:101-107.
    • (2003) Matrix Biol. , vol.22 , pp. 101-107
    • Ramirez, F.1    Rifkin, D.B.2
  • 116
    • 0141788733 scopus 로고    scopus 로고
    • Possible role decorin glycosaminoglycans in fibril force transfer in relative mature tendons - a computational study from molecular to microstructural level
    • Redaelli A., Vesentini S., Soncini M., Vena P., Mantero S., Montevecchi F.M. Possible role decorin glycosaminoglycans in fibril force transfer in relative mature tendons - a computational study from molecular to microstructural level. J. Biomech. 2003, 36:1555-1569.
    • (2003) J. Biomech. , vol.36 , pp. 1555-1569
    • Redaelli, A.1    Vesentini, S.2    Soncini, M.3    Vena, P.4    Mantero, S.5    Montevecchi, F.M.6
  • 118
    • 0034192751 scopus 로고    scopus 로고
    • Developmental expression of dermatan sulfate proteoglycans in the elastic bovine nuchal ligament
    • Reinbotha B.J., Finnisa M.L., Gibsona M.A., Sandbergb L.B., Cleary E.G. Developmental expression of dermatan sulfate proteoglycans in the elastic bovine nuchal ligament. Matrix Biol. 2000, 19:149-162.
    • (2000) Matrix Biol. , vol.19 , pp. 149-162
    • Reinbotha, B.J.1    Finnisa, M.L.2    Gibsona, M.A.3    Sandbergb, L.B.4    Cleary, E.G.5
  • 119
    • 0028128027 scopus 로고
    • Diaphragm injury and myofibrillar structure induced by resistive loading
    • Ried W., Huang J., Bryson S. Diaphragm injury and myofibrillar structure induced by resistive loading. J. Appl. Physiol. 1994, 76:176-184.
    • (1994) J. Appl. Physiol. , vol.76 , pp. 176-184
    • Ried, W.1    Huang, J.2    Bryson, S.3
  • 120
    • 42049114290 scopus 로고    scopus 로고
    • Practical considerations in the use of polarized light microscopy in the analysis of the collagen network in articular cartilage
    • Rieppo J., Hallikainen J., Jurvelin J.S., Kiviranta I., Helminen H.J., Hyttinen M.M. Practical considerations in the use of polarized light microscopy in the analysis of the collagen network in articular cartilage. Microsc. Res. Tech. 2007, 71(4):279-287.
    • (2007) Microsc. Res. Tech. , vol.71 , Issue.4 , pp. 279-287
    • Rieppo, J.1    Hallikainen, J.2    Jurvelin, J.S.3    Kiviranta, I.4    Helminen, H.J.5    Hyttinen, M.M.6
  • 121
    • 0030959386 scopus 로고    scopus 로고
    • Stretching is good for a cell
    • Rouslahti E. Stretching is good for a cell. Science 1997, 276:1345-1346.
    • (1997) Science , vol.276 , pp. 1345-1346
    • Rouslahti, E.1
  • 122
    • 0027049229 scopus 로고
    • Development and aging of phenotypically distinct fibrocartilage associated with the rat Achilles tendon
    • Rufai A., Benjamin M., Ralphs J.R. Development and aging of phenotypically distinct fibrocartilage associated with the rat Achilles tendon. Anat. Embryol. 1992, 186:611-618.
    • (1992) Anat. Embryol. , vol.186 , pp. 611-618
    • Rufai, A.1    Benjamin, M.2    Ralphs, J.R.3
  • 123
    • 70349192852 scopus 로고    scopus 로고
    • Mesenchymal stem cells and insulin-like growth factor-I gene-enhanced mesenchymal stem cells improve structural aspects of healing in equine flexor digitorum superficialis tendons
    • Schnabel L.V., Lynch M.E., van der Meulen M.C., Yeager A.E., Kornatowski M.A., Nixon A.J. Mesenchymal stem cells and insulin-like growth factor-I gene-enhanced mesenchymal stem cells improve structural aspects of healing in equine flexor digitorum superficialis tendons. J. Orthop. Res. 2009, 27(10):1392-1398.
    • (2009) J. Orthop. Res. , vol.27 , Issue.10 , pp. 1392-1398
    • Schnabel, L.V.1    Lynch, M.E.2    van der Meulen, M.C.3    Yeager, A.E.4    Kornatowski, M.A.5    Nixon, A.J.6
  • 124
    • 0028845761 scopus 로고
    • Extracellular matrix, supramolecular organization and shape
    • Scott J.E. Extracellular matrix, supramolecular organization and shape. J. Anat. 1995, 187:259-269.
    • (1995) J. Anat. , vol.187 , pp. 259-269
    • Scott, J.E.1
  • 125
    • 0023927040 scopus 로고    scopus 로고
    • Proteoglycan-fibrillar collagen interactions
    • Scott J.E. Proteoglycan-fibrillar collagen interactions. Biochem. J. 1998, 252:313-323.
    • (1998) Biochem. J. , vol.252 , pp. 313-323
    • Scott, J.E.1
  • 126
    • 0030856986 scopus 로고    scopus 로고
    • Isolation and characterization of small proteoglycans from different zones of the porcine knee meniscus
    • Scott P.G., Nakano T., Dodd C.M. Isolation and characterization of small proteoglycans from different zones of the porcine knee meniscus. Biochim. Biophys. Acta 1997, 1336:254-262.
    • (1997) Biochim. Biophys. Acta , vol.1336 , pp. 254-262
    • Scott, P.G.1    Nakano, T.2    Dodd, C.M.3
  • 127
    • 0000353211 scopus 로고
    • Aging of long-lived proteins: extracellular matrix (collagens, elastins and proteoglycans)
    • Oxford University Press, New York, E.J. Masoro (Ed.)
    • Sell D.R., Monnier V.M. Aging of long-lived proteins: extracellular matrix (collagens, elastins and proteoglycans). Handbook of Physiology Section 11: Aging 1995, 1106-1128. Oxford University Press, New York. E.J. Masoro (Ed.).
    • (1995) Handbook of Physiology Section 11: Aging , pp. 1106-1128
    • Sell, D.R.1    Monnier, V.M.2
  • 128
    • 0025215287 scopus 로고
    • Elastic energy storage in tendons: mechanical differences related to function and age
    • Shadwick R.E. Elastic energy storage in tendons: mechanical differences related to function and age. J. Appl. Physiol. 1990, 68:1033-1040.
    • (1990) J. Appl. Physiol. , vol.68 , pp. 1033-1040
    • Shadwick, R.E.1
  • 129
    • 0030760119 scopus 로고    scopus 로고
    • Role of integrins in cellular responses to mechanical stress and adhesion
    • Shyy J.Y., Chien S. Role of integrins in cellular responses to mechanical stress and adhesion. Curr. Opin. Cell. Biol. 1997, 9(5):707-713.
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , Issue.5 , pp. 707-713
    • Shyy, J.Y.1    Chien, S.2
  • 131
    • 0031893071 scopus 로고    scopus 로고
    • Lysyl oxidase: properties, regulation and multiple functions in biology
    • Smith-Mungo L.I., Kagan H.M. Lysyl oxidase: properties, regulation and multiple functions in biology. Matrix Biol. 1997, 16:387-398.
    • (1997) Matrix Biol. , vol.16 , pp. 387-398
    • Smith-Mungo, L.I.1    Kagan, H.M.2
  • 132
    • 0033628325 scopus 로고    scopus 로고
    • Cartilage oligomeric matrix protein (COMP) levels in digital sheath synovial fluid and serum with tendon injury
    • Smith R.K.W., Heinegård D. Cartilage oligomeric matrix protein (COMP) levels in digital sheath synovial fluid and serum with tendon injury. Equine Vet. J. 2000, 32:52-58.
    • (2000) Equine Vet. J. , vol.32 , pp. 52-58
    • Smith, R.K.W.1    Heinegård, D.2
  • 133
    • 79951990521 scopus 로고    scopus 로고
    • Sequential rupture of triceps and quadriceps tendons in a dialysis patient using hormone supplements. Relaxin affects the in vivo mechanical properties of some but not all tendons in normally menstruating young females
    • Soo I., Christiansen J., Marion D., Courtney M., Luyckx V.A. Sequential rupture of triceps and quadriceps tendons in a dialysis patient using hormone supplements. Relaxin affects the in vivo mechanical properties of some but not all tendons in normally menstruating young females. Clin. Nephrol. 2011, 75(1):20-23.
    • (2011) Clin. Nephrol. , vol.75 , Issue.1 , pp. 20-23
    • Soo, I.1    Christiansen, J.2    Marion, D.3    Courtney, M.4    Luyckx, V.A.5
  • 134
    • 0035213312 scopus 로고    scopus 로고
    • Ruptured Achilles tendons are significantly more degenerated than tendinopathic tendons
    • Tallon C., Maffulli N., Ewen S.N. Ruptured Achilles tendons are significantly more degenerated than tendinopathic tendons. Med. Sci. Sports Exerc. 2001, 33:1983-1990.
    • (2001) Med. Sci. Sports Exerc. , vol.33 , pp. 1983-1990
    • Tallon, C.1    Maffulli, N.2    Ewen, S.N.3
  • 135
    • 0033567291 scopus 로고    scopus 로고
    • The stress-activated protein kinase pathways
    • Tibbles L.A., Woodgett J.R. The stress-activated protein kinase pathways. Cell. Mol. Life Sci. 1999, 55:1230-1254.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 1230-1254
    • Tibbles, L.A.1    Woodgett, J.R.2
  • 136
    • 68449087492 scopus 로고    scopus 로고
    • Organization of collagen bundles during tendon healing in rats treated with L-NAME
    • Tomiosso T.C., Nakagaki W.R., Gomes L., Hyslop S., Pimentel E.R. Organization of collagen bundles during tendon healing in rats treated with L-NAME. Cell Tissue Res. 2009, 337:235-242.
    • (2009) Cell Tissue Res. , vol.337 , pp. 235-242
    • Tomiosso, T.C.1    Nakagaki, W.R.2    Gomes, L.3    Hyslop, S.4    Pimentel, E.R.5
  • 137
    • 0027355493 scopus 로고
    • Tendon collagens: extracellular matrix composition in shear stress and tensile components of flexor tendons
    • Tsuzaki M., Yamauchi M., Banes A.J. Tendon collagens: extracellular matrix composition in shear stress and tensile components of flexor tendons. Connect. Tissue Res. 1993, 29(2):141-152.
    • (1993) Connect. Tissue Res. , vol.29 , Issue.2 , pp. 141-152
    • Tsuzaki, M.1    Yamauchi, M.2    Banes, A.J.3
  • 139
    • 74049158684 scopus 로고    scopus 로고
    • Modeling optical behavior of birefringent biological tissues for evaluation of quantitative polarized light microscopy
    • van Turnhout M.C., Kranenbarg S., van Leeuwen J.L. Modeling optical behavior of birefringent biological tissues for evaluation of quantitative polarized light microscopy. J. Biomed Opt. 2009, 14(5):054018.
    • (2009) J. Biomed Opt. , vol.14 , Issue.5 , pp. 054018
    • van Turnhout, M.C.1    Kranenbarg, S.2    van Leeuwen, J.L.3
  • 140
    • 22744437655 scopus 로고    scopus 로고
    • Determination of molecular orientation of uniaxially stretched polyamide fibers by polarized infrared spectroscopy: comparison of X-ray diffraction and birefringence methods
    • Vasanthan N. Determination of molecular orientation of uniaxially stretched polyamide fibers by polarized infrared spectroscopy: comparison of X-ray diffraction and birefringence methods. Appl. Spectrosc. 2005, 59(7):897-903.
    • (2005) Appl. Spectrosc. , vol.59 , Issue.7 , pp. 897-903
    • Vasanthan, N.1
  • 141
    • 84855242192 scopus 로고
    • Feixes de colágeno: detecção e quantificação de ordem macromolecular I. Dicroísmo com corantes azóicos sulfatados (Orange G, Xylidine Ponceau e Sirius Red)
    • Vidal B.C. Feixes de colágeno: detecção e quantificação de ordem macromolecular I. Dicroísmo com corantes azóicos sulfatados (Orange G, Xylidine Ponceau e Sirius Red). Ciência e Cultura 1980, 32(5):603-611.
    • (1980) Ciência e Cultura , vol.32 , Issue.5 , pp. 603-611
    • Vidal, B.C.1
  • 142
    • 0023027976 scopus 로고
    • Evaluation of carbohydrate role in the molecular order of collagen bundles: microphotometric measurements of textural birefringence
    • Vidal B.C. Evaluation of carbohydrate role in the molecular order of collagen bundles: microphotometric measurements of textural birefringence. Cell. Mol. Biol. 1986, 32:527-535.
    • (1986) Cell. Mol. Biol. , vol.32 , pp. 527-535
    • Vidal, B.C.1
  • 143
    • 14744271474 scopus 로고
    • Métodos em Biologia Celular
    • Atheneu, Rio de Janeiro, B.C. Vidal, M.L.S. Mello (Eds.)
    • Vidal B.C. Métodos em Biologia Celular. Biologia Celular 1987, 5-34. Atheneu, Rio de Janeiro. B.C. Vidal, M.L.S. Mello (Eds.).
    • (1987) Biologia Celular , pp. 5-34
    • Vidal, B.C.1
  • 144
    • 2442687461 scopus 로고
    • Cell and extracellular matrix interaction: a feedback theory based on molecular order recognition-adhesion events
    • Vidal B.C. Cell and extracellular matrix interaction: a feedback theory based on molecular order recognition-adhesion events. Rev. Fac. Ciên. Med. Unicamp. 1994, 4:11-14.
    • (1994) Rev. Fac. Ciên. Med. Unicamp. , vol.4 , pp. 11-14
    • Vidal, B.C.1
  • 146
    • 0242709860 scopus 로고    scopus 로고
    • Image analysis of tendon helical superstructure using interference and polarized light microscopy
    • Vidal B.C. Image analysis of tendon helical superstructure using interference and polarized light microscopy. Micron 2003, 34:423-432.
    • (2003) Micron , vol.34 , pp. 423-432
    • Vidal, B.C.1
  • 147
    • 78649484405 scopus 로고    scopus 로고
    • Form birefringence as applied to biopolymer and inorganic material supraorganization
    • Vidal B.C. Form birefringence as applied to biopolymer and inorganic material supraorganization. Biotech. Histochem. 2010, 85:365-378.
    • (2010) Biotech. Histochem. , vol.85 , pp. 365-378
    • Vidal, B.C.1
  • 148
    • 0025218977 scopus 로고
    • Aggregational state and molecular order of tendons as a function of age
    • Vidal B.C., Carvalho H.F. Aggregational state and molecular order of tendons as a function of age. Matrix 1990, 10:48-57.
    • (1990) Matrix , vol.10 , pp. 48-57
    • Vidal, B.C.1    Carvalho, H.F.2
  • 149
    • 0020403474 scopus 로고
    • Polarization microscopy and microspectrophotometry of Sirius Red, Picrosirius and Chlorantine Fast Red aggregates and of their complexes with collagen
    • Vidal B.C., Mello M.L., Pimentel E.R. Polarization microscopy and microspectrophotometry of Sirius Red, Picrosirius and Chlorantine Fast Red aggregates and of their complexes with collagen. Histochem. J. 1982, 14(6):857-878.
    • (1982) Histochem. J. , vol.14 , Issue.6 , pp. 857-878
    • Vidal, B.C.1    Mello, M.L.2    Pimentel, E.R.3
  • 150
    • 0021118692 scopus 로고
    • Proteoglycan arrangement in tendon collagen bundles
    • Vidal B.C., Mello M.L.S. Proteoglycan arrangement in tendon collagen bundles. Cell. Mol. Biol. 1984, 30:195-204.
    • (1984) Cell. Mol. Biol. , vol.30 , pp. 195-204
    • Vidal, B.C.1    Mello, M.L.S.2
  • 151
    • 21244492354 scopus 로고    scopus 로고
    • Supramolecular order following binding of the dichroic birefringent sulfonic dye ponceau SS to collagen fibers
    • Vidal B.C., Mello M.L.S. Supramolecular order following binding of the dichroic birefringent sulfonic dye ponceau SS to collagen fibers. Biopolymers 2005, 78(3):121-128.
    • (2005) Biopolymers , vol.78 , Issue.3 , pp. 121-128
    • Vidal, B.C.1    Mello, M.L.S.2
  • 152
    • 67649846307 scopus 로고    scopus 로고
    • Structural organization of collagen fibers in chordae tendineae as assessed by optical anisotropic properties and Fast Fourier Transform
    • Vidal B.C., Mello M.L.S. Structural organization of collagen fibers in chordae tendineae as assessed by optical anisotropic properties and Fast Fourier Transform. J. Struct. Biol. 2009, 167:66-75.
    • (2009) J. Struct. Biol. , vol.167 , pp. 66-75
    • Vidal, B.C.1    Mello, M.L.S.2
  • 153
    • 73749083518 scopus 로고    scopus 로고
    • Optical anisotropy of collagen fibers of rat calcaneal tendons: an approach to spatially resolved supramolecular organization
    • Vidal B.C., Mello M.L.S. Optical anisotropy of collagen fibers of rat calcaneal tendons: an approach to spatially resolved supramolecular organization. Acta Histochem. 2010, 112:53-61.
    • (2010) Acta Histochem. , vol.112 , pp. 53-61
    • Vidal, B.C.1    Mello, M.L.S.2
  • 154
    • 78650755968 scopus 로고    scopus 로고
    • Collagen type I amide I band infrared spectroscopy
    • Vidal B.C., Mello M.L.S. Collagen type I amide I band infrared spectroscopy. Micron 2011, 42:283-289.
    • (2011) Micron , vol.42 , pp. 283-289
    • Vidal, B.C.1    Mello, M.L.S.2
  • 155
    • 0020403474 scopus 로고
    • Polarization microscopy and microspectrophotometry of sirius red, picro sirius and chlorantine fast red aggregates and their complexes with collagen
    • Vidal B.C., Mello M.L.S., Pimentel E.R. Polarization microscopy and microspectrophotometry of sirius red, picro sirius and chlorantine fast red aggregates and their complexes with collagen. Histochem. J. 1982, 14:857-978.
    • (1982) Histochem. J. , vol.14 , pp. 857-978
    • Vidal, B.C.1    Mello, M.L.S.2    Pimentel, E.R.3
  • 156
    • 0023910436 scopus 로고
    • Articular cartilage: collagen II-proteoglycan interactions. Availability of reative groups. Variation in birefringence and differences as compared to collagen I
    • Vidal B.C., Vilarta R. Articular cartilage: collagen II-proteoglycan interactions. Availability of reative groups. Variation in birefringence and differences as compared to collagen I. Acta Histochem. 1988, 83:189-205.
    • (1988) Acta Histochem. , vol.83 , pp. 189-205
    • Vidal, B.C.1    Vilarta, R.2
  • 157
    • 0024493670 scopus 로고
    • Anisotropic and biochemical properties of tendons modified by exercise and denervation: aggregational state and macromolecular order
    • Vilarta R., Vidal B.C. Anisotropic and biochemical properties of tendons modified by exercise and denervation: aggregational state and macromolecular order. Matrix Biol. 1989, 9(1):55-61.
    • (1989) Matrix Biol. , vol.9 , Issue.1 , pp. 55-61
    • Vilarta, R.1    Vidal, B.C.2
  • 158
    • 0022389596 scopus 로고
    • Characterization of proteoglycans from adult bovine tendon
    • Vogel K.G., Heinegård D. Characterization of proteoglycans from adult bovine tendon. J. Biol. Chem. 1985, 260:298-306.
    • (1985) J. Biol. Chem. , vol.260 , pp. 298-306
    • Vogel, K.G.1    Heinegård, D.2
  • 159
    • 0024392956 scopus 로고
    • Structural specialization in tendon under compression
    • Vogel K.J., Koob T.J. Structural specialization in tendon under compression. Int. Rev. Cytol. 1989, 115:267-293.
    • (1989) Int. Rev. Cytol. , vol.115 , pp. 267-293
    • Vogel, K.J.1    Koob, T.J.2
  • 160
    • 0032752746 scopus 로고    scopus 로고
    • Proteins in the tensile region of adult bovine deep flexor tendon
    • Vogel K.G., Meyers A.B. Proteins in the tensile region of adult bovine deep flexor tendon. Clin. Orthop. Relat. Res. 1999, 367:344-355.
    • (1999) Clin. Orthop. Relat. Res. , vol.367 , pp. 344-355
    • Vogel, K.G.1    Meyers, A.B.2
  • 161
    • 0023121507 scopus 로고
    • Quantitative structural analysis of collagen in chordae tendinae and its relation to floppy mitral valves and proteoglycans infiltration
    • Whittaker P., Bouhner D.R., Perkins D.G., Cnham P.B. Quantitative structural analysis of collagen in chordae tendinae and its relation to floppy mitral valves and proteoglycans infiltration. Br. Heart 1987, 57:264-269.
    • (1987) Br. Heart , vol.57 , pp. 264-269
    • Whittaker, P.1    Bouhner, D.R.2    Perkins, D.G.3    Cnham, P.B.4
  • 162
    • 0000042564 scopus 로고
    • Die Theorie des Mischkorper fur das Feld der stationaren Stromung erste Abhandlung. Die Mittelwerstaze fur Kraft, Polarization und Energie
    • Wiener O. Die Theorie des Mischkorper fur das Feld der stationaren Stromung erste Abhandlung. Die Mittelwerstaze fur Kraft, Polarization und Energie. Ab. Math. Klas. Kongl. Sach. Gesel. Wiss. 1912, 23:509-604.
    • (1912) Ab. Math. Klas. Kongl. Sach. Gesel. Wiss. , vol.23 , pp. 509-604
    • Wiener, O.1


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