메뉴 건너뛰기




Volumn 7, Issue , 2007, Pages 404-420

Collagen structure of tendon relates to function

Author keywords

Collagen; Crimps; Electron microscopy; Fibrils; Tendon; Ultrastructure

Indexed keywords

COLLAGEN; COLLAGEN FIBER; COLLAGEN TYPE 1; DECORIN; HYALURONIC ACID; PROTEOGLYCAN;

EID: 34047242983     PISSN: None     EISSN: 1537744X     Source Type: Journal    
DOI: 10.1100/tsw.2007.92     Document Type: Review
Times cited : (233)

References (132)
  • 1
    • 0034577312 scopus 로고    scopus 로고
    • Structure of the tendon connective tissue
    • Kannus, P. (2000) Structure of the tendon connective tissue. Scand. J. Med. Sci. Sports 10, 312-20.
    • (2000) Scand. J. Med. Sci. Sports , vol.10 , pp. 312-320
    • Kannus, P.1
  • 4
    • 0036901713 scopus 로고    scopus 로고
    • Effects of exercise on the biomechanical, biochemical and structural properties of tendons
    • Buchanan, C.I., and Marsh, R.L. (2002) Effects of exercise on the biomechanical, biochemical and structural properties of tendons. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 133, 1101-1107.
    • (2002) Comp. Biochem. Physiol. A Mol. Integr. Physiol , vol.133 , pp. 1101-1107
    • Buchanan, C.I.1    Marsh, R.L.2
  • 6
    • 0344873751 scopus 로고    scopus 로고
    • Tendon properties in relation to muscular activity and physical training
    • Magnusson, S.P., Hansen, P., and Kjaer, M. (2003) Tendon properties in relation to muscular activity and physical training. Scand. J. Med. Sci. Sports 13, 211-223.
    • (2003) Scand. J. Med. Sci. Sports , vol.13 , pp. 211-223
    • Magnusson, S.P.1    Hansen, P.2    Kjaer, M.3
  • 7
    • 78651192479 scopus 로고
    • Structure and function of mammalian tendon
    • Elliott, D.H. (1965) Structure and function of mammalian tendon. Biol. Rev. 40, 392-421.
    • (1965) Biol. Rev , vol.40 , pp. 392-421
    • Elliott, D.H.1
  • 8
    • 0141453852 scopus 로고    scopus 로고
    • Collagen self-assembly and the development of tendon mechanical properties
    • Silver, F.H., Freeman, J.W., and Seehra, G.P. (2003) Collagen self-assembly and the development of tendon mechanical properties. J. Biomech. 36, 1529-1553.
    • (2003) J. Biomech , vol.36 , pp. 1529-1553
    • Silver, F.H.1    Freeman, J.W.2    Seehra, G.P.3
  • 9
    • 17844373840 scopus 로고    scopus 로고
    • Procollagen trafficking, processing and fibrillogenesis
    • Canty, E.G., and Kadler, K.E. (2005) Procollagen trafficking, processing and fibrillogenesis. J. Cell Sci. 118, 1341-1353
    • (2005) J. Cell Sci , vol.118 , pp. 1341-1353
    • Canty, E.G.1    Kadler, K.E.2
  • 10
    • 0018425484 scopus 로고
    • The limiting collagen microfibril. The minimum structure demonstrating native axial periodicity
    • Veis, A., Miller, A., Leibovich, S.J., and Traub, W. (1979) The limiting collagen microfibril. The minimum structure demonstrating native axial periodicity. Bioch. Biophis. Acta 576, 88-98.
    • (1979) Bioch. Biophis. Acta , vol.576 , pp. 88-98
    • Veis, A.1    Miller, A.2    Leibovich, S.J.3    Traub, W.4
  • 11
    • 0019334167 scopus 로고
    • Direct observation of a transverse periodicity in collagen fibrils
    • Squire, J.M., and Freundlich, A. (1980) Direct observation of a transverse periodicity in collagen fibrils. Nature 288, 410-413.
    • (1980) Nature , vol.288 , pp. 410-413
    • Squire, J.M.1    Freundlich, A.2
  • 12
    • 0019448805 scopus 로고
    • Differences in the microfibrillar arrangement of collagen fibrils. Distribution and possible significance
    • Reale, E., Benazzo, F., and Ruggeri, A. (1981) Differences in the microfibrillar arrangement of collagen fibrils. Distribution and possible significance. J. Sub. Cytol. 13, 135-143.
    • (1981) J. Sub. Cytol , vol.13 , pp. 135-143
    • Reale, E.1    Benazzo, F.2    Ruggeri, A.3
  • 13
    • 0025066885 scopus 로고
    • Subfibrillar architecture and functional properties of collagen: A comparative study in rat tendons
    • Raspanti, M., Ottani, V., and Ruggeri, A. (1990) Subfibrillar architecture and functional properties of collagen: a comparative study in rat tendons. J. Anat. 172, 157-164.
    • (1990) J. Anat , vol.172 , pp. 157-164
    • Raspanti, M.1    Ottani, V.2    Ruggeri, A.3
  • 14
    • 0035218932 scopus 로고    scopus 로고
    • Collagen structure and functional implications
    • Ottani, V., Raspanti, M., and Ruggeri A. (2001) Collagen structure and functional implications. Micron 32, 251-260.
    • (2001) Micron , vol.32 , pp. 251-260
    • Ottani, V.1    Raspanti, M.2    Ruggeri, A.3
  • 15
    • 0003096350 scopus 로고
    • Molecular structure and function of collagen
    • Nimni, M.E, ed, CRC Press. Boca Raton, FL
    • Nimni, M.E., and Harkness, R.D. (1988) Molecular structure and function of collagen. In: Nimni, M.E. (ed.) Collagen, vol. 1. CRC Press. Boca Raton, FL, 1-77.
    • (1988) Collagen , vol.1 , pp. 1-77
    • Nimni, M.E.1    Harkness, R.D.2
  • 16
    • 0036905451 scopus 로고    scopus 로고
    • Collagen fibril biosynthesis in tendon: A review and recent insights
    • Canty, E.G., and Kadler, K.E. (2002) Collagen fibril biosynthesis in tendon: a review and recent insights. Comp. Biochem. Physiol. A Mol. Integr. Physiol 133, 979-985.
    • (2002) Comp. Biochem. Physiol. A Mol. Integr. Physiol , vol.133 , pp. 979-985
    • Canty, E.G.1    Kadler, K.E.2
  • 17
    • 32544452057 scopus 로고    scopus 로고
    • Collagen fibril morphology and organization: Implications for force transmission in ligament and tendon
    • Provenzano, P.P., and Vanderby, R., Jr. (2006) Collagen fibril morphology and organization: implications for force transmission in ligament and tendon. Matrix Biol. 25,71-84.
    • (2006) Matrix Biol , vol.25 , pp. 71-84
    • Provenzano, P.P.1    Vanderby Jr., R.2
  • 18
    • 0023077343 scopus 로고
    • Histology and ultrastructure of the human flexor tendon sheath
    • Cohen, M.J., and Kaplan, L. (1987) Histology and ultrastructure of the human flexor tendon sheath. J. Hand Surg. [Am] 12, 25-29.
    • (1987) J. Hand Surg. [Am] , vol.12 , pp. 25-29
    • Cohen, M.J.1    Kaplan, L.2
  • 21
    • 0030744791 scopus 로고    scopus 로고
    • Ultrastructural observations on the tendon sheath of the rat tail
    • Gotoh, T., Murashige, N., and Yamashita, K. (1997) Ultrastructural observations on the tendon sheath of the rat tail. J. Electron Microsc. (Tokyo) 46, 247-252.
    • (1997) J. Electron Microsc. (Tokyo) , vol.46 , pp. 247-252
    • Gotoh, T.1    Murashige, N.2    Yamashita, K.3
  • 22
    • 0030945384 scopus 로고    scopus 로고
    • Localization of collagen types I, III and V during tendon development. Changes in collagen types I and III are correlated with changes in fibril diameter
    • Birk, D.E., and Mayne, R. (1997) Localization of collagen types I, III and V during tendon development. Changes in collagen types I and III are correlated with changes in fibril diameter. Eur. J. Cell. Biol. 72, 352-361.
    • (1997) Eur. J. Cell. Biol , vol.72 , pp. 352-361
    • Birk, D.E.1    Mayne, R.2
  • 23
    • 0022346449 scopus 로고
    • Fine structural alterations in chronic Achilles paratenonitis in athletes
    • Kvist, M., Jozsa, L., Järvinen, M., and Kvist, H. (1985) Fine structural alterations in chronic Achilles paratenonitis in athletes. Pathol. Res. Pract. 180, 416-423.
    • (1985) Pathol. Res. Pract , vol.180 , pp. 416-423
    • Kvist, M.1    Jozsa, L.2    Järvinen, M.3    Kvist, H.4
  • 24
    • 0345845171 scopus 로고
    • The architecture of human tendons. II. The peritenonium and so-called surface phenomenon
    • Jozsa, L., and Balint, B.J. (1978) The architecture of human tendons. II. The peritenonium and so-called surface phenomenon. Traumatologia 21, 293-297.
    • (1978) Traumatologia , vol.21 , pp. 293-297
    • Jozsa, L.1    Balint, B.J.2
  • 25
    • 0022639818 scopus 로고
    • Achilles tendon lesions in sport
    • Williams, J.G.P. (1986) Achilles tendon lesions in sport. Sports Med. 3, 114-135.
    • (1986) Sports Med , vol.3 , pp. 114-135
    • Williams, J.G.P.1
  • 26
    • 0024848824 scopus 로고
    • Prevention and treatment of overuse tendon injuries
    • Hess, G.P., Cappiello, W.L, Poole, R.M., and Hunter, S.C. (1989) Prevention and treatment of overuse tendon injuries. Sports Med. 8, 371-384.
    • (1989) Sports Med , vol.8 , pp. 371-384
    • Hess, G.P.1    Cappiello, W.L.2    Poole, R.M.3    Hunter, S.C.4
  • 27
    • 0026247301 scopus 로고
    • Equine synovial tendon sheaths and bursae: A transmission electron microscope study
    • Hago, B.E., Vaughan, L.C., and Plummer, J.M. (1991) Equine synovial tendon sheaths and bursae: a transmission electron microscope study. Equine Vet. J. 23, 475-478.
    • (1991) Equine Vet. J , vol.23 , pp. 475-478
    • Hago, B.E.1    Vaughan, L.C.2    Plummer, J.M.3
  • 28
    • 0014658332 scopus 로고
    • Intravital observations on the microvascular anatomy and microcirculation of the tendon
    • Schatzker, J., and Branemark, P.I. (1969) Intravital observations on the microvascular anatomy and microcirculation of the tendon. Acta Orthop. Scand. 126, Suppl. 1-23.
    • (1969) Acta Orthop. Scand , vol.126 , Issue.SUPPL. , pp. 1-23
    • Schatzker, J.1    Branemark, P.I.2
  • 29
    • 0022310556 scopus 로고
    • The structure of rat tail tendon
    • Rowe, R.W.D. (1985) The structure of rat tail tendon. Conn. Tiss. Res. 14, 9-20.
    • (1985) Conn. Tiss. Res , vol.14 , pp. 9-20
    • Rowe, R.W.D.1
  • 30
    • 0022293482 scopus 로고
    • The structure of rat tail tendon fascicles
    • Rowe, R.W.D. (1985) The structure of rat tail tendon fascicles. Conn. Tiss. Res. 14, 21-30.
    • (1985) Conn. Tiss. Res , vol.14 , pp. 21-30
    • Rowe, R.W.D.1
  • 31
    • 0018869426 scopus 로고
    • Morphological, immunochemical and biochemical study of rabbit Achilles tendon at various ages
    • Ippolito, E., Natali, P.G., Postacchini, F., Accinni, L., and Demartino, C. (1980) Morphological, immunochemical and biochemical study of rabbit Achilles tendon at various ages. J. Bone Joint Surg. (Am) 62, 583-592.
    • (1980) J. Bone Joint Surg. (Am) , vol.62 , pp. 583-592
    • Ippolito, E.1    Natali, P.G.2    Postacchini, F.3    Accinni, L.4    Demartino, C.5
  • 32
    • 0012452589 scopus 로고
    • Basic concepts in inflammation
    • Leadbetter, W, Buckwalter, J.A. and Gordon, S.L. eds, American Academy of Orthopedic Surgeons, Park Ridge
    • Martinez-Hernandez, A., and Amenta, P.S. (1990) Basic concepts in inflammation. In: Leadbetter, W., Buckwalter, J.A. and Gordon, S.L. eds. Sport-Induced Inflammation. American Academy of Orthopedic Surgeons, Park Ridge, 55-102.
    • (1990) Sport-Induced Inflammation , pp. 55-102
    • Martinez-Hernandez, A.1    Amenta, P.S.2
  • 33
    • 2542439729 scopus 로고    scopus 로고
    • Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon
    • Canty, E.G., Lu, Y., Meadows, R.S., Shaw, M.K., Holmes, D.F., and Kadler, K.E. (2004) Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon. J. Cell Biol. 165, 553-563.
    • (2004) J. Cell Biol , vol.165 , pp. 553-563
    • Canty, E.G.1    Lu, Y.2    Meadows, R.S.3    Shaw, M.K.4    Holmes, D.F.5    Kadler, K.E.6
  • 34
    • 0034038922 scopus 로고    scopus 로고
    • Role of mechanical factors in modulating cardiac fibroblasts function and extracellular matrix synthesis
    • MacKenna, D., Summerour, S.R., and Villarreal, F.J. (2000) Role of mechanical factors in modulating cardiac fibroblasts function and extracellular matrix synthesis. Cardiovasc. Res. 46, 257-263.
    • (2000) Cardiovasc. Res , vol.46 , pp. 257-263
    • MacKenna, D.1    Summerour, S.R.2    Villarreal, F.J.3
  • 35
    • 0026245524 scopus 로고
    • Integrins as mechanochemical transducers
    • Ingber, D. (1991) Integrins as mechanochemical transducers. Curr. Op. Cell Biol. 3, 841-848.
    • (1991) Curr. Op. Cell Biol , vol.3 , pp. 841-848
    • Ingber, D.1
  • 36
    • 0032730185 scopus 로고    scopus 로고
    • Regulation of extracellular matrix gene expression by mechanical stress
    • Chiquet, M. (1999) Regulation of extracellular matrix gene expression by mechanical stress. Matrix Biol. 18, 417-426.
    • (1999) Matrix Biol , vol.18 , pp. 417-426
    • Chiquet, M.1
  • 37
    • 0028282547 scopus 로고
    • Cellular tensegrity: Exploring how mechanical changes in the cytoskeleton regulate cell growth, migration, and tissue pattern during morphognesis
    • Ingber, D. (1994) Cellular tensegrity: exploring how mechanical changes in the cytoskeleton regulate cell growth, migration, and tissue pattern during morphognesis. Int. Rev. Cytol. 150, 173-224.
    • (1994) Int. Rev. Cytol , vol.150 , pp. 173-224
    • Ingber, D.1
  • 38
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmatic domain-binding proteins
    • Liu, S., Calderwood, D.A., and Ginsberg, M.H. (2000) Integrin cytoplasmatic domain-binding proteins. J. Cell. Sci. 113, 3563-3571.
    • (2000) J. Cell. Sci , vol.113 , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2    Ginsberg, M.H.3
  • 39
    • 0032952039 scopus 로고    scopus 로고
    • Ingber, D. (1999) How cells (might) sense microgravity. FASEB J. 13, Suppl. S3-S15.
    • Ingber, D. (1999) How cells (might) sense microgravity. FASEB J. 13, Suppl. S3-S15.
  • 40
    • 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., and Murdoch, A.D. (1996) Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J. 10, 598-614.
    • (1996) FASEB J , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 41
    • 0035058027 scopus 로고    scopus 로고
    • Proteoglycans and glycosaminoglycan fine structure in the mouse tail tendon fascicle
    • Derwin, K.A., Soslowsky, L.J., Kimura, J.H., and Plaas, A.H. (2001) Proteoglycans and glycosaminoglycan fine structure in the mouse tail tendon fascicle. J.Orthop. Res. 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
  • 42
    • 0019490438 scopus 로고
    • Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region
    • Scott., J.E., and Oxford, C.R. (1981) Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region. Biochem. J. 197, 213-216.
    • (1981) Biochem. J , vol.197 , pp. 213-216
    • Scott, J.E.1    Oxford, C.R.2
  • 43
    • 0028892860 scopus 로고
    • Tendon response to tensile stress: An ultrastructural investigation of collagen: proteoglycan interactions in stressed tendon
    • Cribb, A.M., and Scott, J.E. (1995) Tendon response to tensile stress: an ultrastructural investigation of collagen: proteoglycan interactions in stressed tendon. J. Anat. 187, 423-428.
    • (1995) J. Anat , vol.187 , pp. 423-428
    • Cribb, A.M.1    Scott, J.E.2
  • 44
    • 0029560104 scopus 로고
    • Fibrocartilage associated with human tendons and their pulleys
    • Benjamin, M., Qin, S., and Ralphs, J.R. (1995) Fibrocartilage associated with human tendons and their pulleys. J. Anat. 187, 625-633.
    • (1995) J. Anat , vol.187 , pp. 625-633
    • Benjamin, M.1    Qin, S.2    Ralphs, J.R.3
  • 45
    • 0019862889 scopus 로고
    • Proteoglycan-collagen arrangements in developing rat tail tendon: An electron microscopical and biochemical investigation
    • Scott, J.E., Oxford, C.R., and Hughes, E.W. (1981) Proteoglycan-collagen arrangements in developing rat tail tendon: an electron microscopical and biochemical investigation. Biochem. J. 195, 573-581.
    • (1981) Biochem. J , vol.195 , pp. 573-581
    • Scott, J.E.1    Oxford, C.R.2    Hughes, E.W.3
  • 47
    • 0021362952 scopus 로고
    • The periphery of the developing collagen fibrils
    • Scott, J.E. (1984) The periphery of the developing collagen fibrils. Biochem. J. 218, 229-233.
    • (1984) Biochem. J , vol.218 , pp. 229-233
    • Scott, J.E.1
  • 48
    • 3042772972 scopus 로고    scopus 로고
    • What happens when tendons bend and twist? Proteoglycans
    • Vogel, K.G. (2004) What happens when tendons bend and twist? Proteoglycans. J. Musculoskelet. Neuronal Interact. 4, 202-203.
    • (2004) J. Musculoskelet. Neuronal Interact , vol.4 , pp. 202-203
    • Vogel, K.G.1
  • 49
    • 0030016013 scopus 로고    scopus 로고
    • Proteodermatan and proteokeratan sulphate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagens
    • Scott., J.E. (1996) Proteodermatan and proteokeratan sulphate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagens. Biochemistry (Mosc.) 35, 8795-8799.
    • (1996) Biochemistry (Mosc.) , vol.35 , pp. 8795-8799
    • Scott, J.E.1
  • 50
    • 0030875449 scopus 로고    scopus 로고
    • Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties
    • Pins, G.D., Christiansen, D.L., Patel, R., and Silver F.H. (1997) Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties. Biophys. J. 73, 2164-2172.
    • (1997) Biophys. J , vol.73 , pp. 2164-2172
    • Pins, G.D.1    Christiansen, D.L.2    Patel, R.3    Silver, F.H.4
  • 51
    • 0028923480 scopus 로고
    • Collagen fibrillogenesis in situ: Fibril segments undergo post-depositional mofidications resulting in linear and lateral growth during matrix development
    • Birk, D.E., Nurminskaya, M.V., and Zycband, E.I. (1995) Collagen fibrillogenesis in situ: fibril segments undergo post-depositional mofidications resulting in linear and lateral growth during matrix development. Dev. Dyn. 202, 229-243.
    • (1995) Dev. Dyn , vol.202 , pp. 229-243
    • Birk, D.E.1    Nurminskaya, M.V.2    Zycband, E.I.3
  • 52
    • 0032101311 scopus 로고    scopus 로고
    • Lumican regulates collagen fibril assembly: Skin fragility and corneal opacity in the absence of lumican
    • Chakravarti, S., Magnusson, T., Lass, J.H., Jepsen, K.J., LaMantia, C., and Carroll, H. (1998) Lumican regulates collagen fibril assembly: skin fragility and corneal opacity in the absence of lumican. J. Cell. Biol. 141, 1277-1286.
    • (1998) J. Cell. Biol , vol.141 , pp. 1277-1286
    • Chakravarti, S.1    Magnusson, T.2    Lass, J.H.3    Jepsen, K.J.4    LaMantia, C.5    Carroll, H.6
  • 56
    • 0141651913 scopus 로고    scopus 로고
    • Functions of lumican and fibromodulin: Lessons from knockout mice
    • Chakravarti, S. (2003) Functions of lumican and fibromodulin: lessons from knockout mice. Glycoconj. J. 19, 287-293.
    • (2003) Glycoconj. J , vol.19 , pp. 287-293
    • Chakravarti, S.1
  • 58
    • 1542752970 scopus 로고    scopus 로고
    • Molecular packing in network-forming collagens
    • Knupp, C., and Squire, J. M. (2003) Molecular packing in network-forming collagens. TheScientificWorldJournal 3, 558-577.
    • (2003) TheScientificWorldJournal , vol.3 , pp. 558-577
    • Knupp, C.1    Squire, J.M.2
  • 59
    • 0027006916 scopus 로고
    • Analysis of mammalian connective tissue: Relationship between hierarchical structures and mechanical properties
    • Silver, F.H., Kato, Y.P., Ohno, M., and Wasserman, A.J. (1992) Analysis of mammalian connective tissue: relationship between hierarchical structures and mechanical properties. J. Long Term Eff. Med. Implants 2, 165-198.
    • (1992) J. Long Term Eff. Med. Implants , vol.2 , pp. 165-198
    • Silver, F.H.1    Kato, Y.P.2    Ohno, M.3    Wasserman, A.J.4
  • 61
    • 0018762445 scopus 로고
    • Tendon collagen fibrillogenesis: Intracellular subassemblies and cell surface changes associated with fibril growth
    • Trelstad, R.L., and Hayashi, K. (1979) Tendon collagen fibrillogenesis: intracellular subassemblies and cell surface changes associated with fibril growth. Dev. Biol. 71, 228-242.
    • (1979) Dev. Biol , vol.71 , pp. 228-242
    • Trelstad, R.L.1    Hayashi, K.2
  • 62
    • 0141857158 scopus 로고
    • Partial purification and characterization of a neutral protease which cleaves the N-terminal propeptides from procollagen
    • Tuderman, L., Kivirik, K.I., and Prockop, D.J. (1977) Partial purification and characterization of a neutral protease which cleaves the N-terminal propeptides from procollagen. Biochem. 16, 3421-3429.
    • (1977) Biochem , vol.16 , pp. 3421-3429
    • Tuderman, L.1    Kivirik, K.I.2    Prockop, D.J.3
  • 63
    • 0344636656 scopus 로고    scopus 로고
    • Biomechanics of tendon and the effects of immobilization
    • Curwin, S. (1997) Biomechanics of tendon and the effects of immobilization. Foot Ankle Clin. 2, 371-389.
    • (1997) Foot Ankle Clin , vol.2 , pp. 371-389
    • Curwin, S.1
  • 64
    • 0031113402 scopus 로고    scopus 로고
    • Structure and metabolism of tendons
    • O'Brien, M. (1997) Structure and metabolism of tendons. Scand. J. Med. Sci. Sports 7, 55-61.
    • (1997) Scand. J. Med. Sci. Sports , vol.7 , pp. 55-61
    • O'Brien, M.1
  • 66
    • 0020320305 scopus 로고
    • Organization of collagen fibers in rat tail tendon at the optical microscope level
    • Niven, H., Baer, E., and Hiltner, A. (1982) Organization of collagen fibers in rat tail tendon at the optical microscope level. Coll. Relat.. Res. 2, 131-142.
    • (1982) Coll. Relat.. Res , vol.2 , pp. 131-142
    • Niven, H.1    Baer, E.2    Hiltner, A.3
  • 67
    • 0021982815 scopus 로고
    • Interferometric evaluation of collagen concentration in tendon fibers
    • Angel, G., and George, V. (1985) Interferometric evaluation of collagen concentration in tendon fibers. Conn. Tissue Res. 13, 323-337.
    • (1985) Conn. Tissue Res , vol.13 , pp. 323-337
    • Angel, G.1    George, V.2
  • 68
    • 0018876157 scopus 로고
    • The biomechanical and biochemical properties of swine tendons: Long-term effects of exercise on the digital extensors
    • Woo, S.L., Ritter, M.A., Amiel, D., Sanders, T.M., Gomez, M.A., Kuei, S.C., Garfin, S.R., and Akeson, W.H. (1980) The biomechanical and biochemical properties of swine tendons: Long-term effects of exercise on the digital extensors. Conn. Tiss. Res. 7, 177-183.
    • (1980) Conn. Tiss. Res , vol.7 , pp. 177-183
    • Woo, S.L.1    Ritter, M.A.2    Amiel, D.3    Sanders, T.M.4    Gomez, M.A.5    Kuei, S.C.6    Garfin, S.R.7    Akeson, W.H.8
  • 69
    • 0019531550 scopus 로고
    • The effects of exercise on the biomechanical and biochemical properties of swine digital flexor tendons
    • Woo, S.L.-Y., Gomez, M.A., Amiel, D., Ritter, M.A., Gelberman, R.H., and Akeson, W.H. (1981) The effects of exercise on the biomechanical and biochemical properties of swine digital flexor tendons. J. Biomech. Eng. 103, 51-56.
    • (1981) J. Biomech. Eng , vol.103 , pp. 51-56
    • Woo, S.L.-Y.1    Gomez, M.A.2    Amiel, D.3    Ritter, M.A.4    Gelberman, R.H.5    Akeson, W.H.6
  • 70
    • 0033155064 scopus 로고    scopus 로고
    • Treadmill exercise induced tendon hypertrophy: Assessment of tendons with different mechanical functions
    • Birch, H.L., McLaughlin, L., Smith, R.K.W., and Goodship, A.E. (1999) Treadmill exercise induced tendon hypertrophy: assessment of tendons with different mechanical functions. Equine Vet. J. Suppl. 30, 222-226.
    • (1999) Equine Vet. J. Suppl , vol.30 , pp. 222-226
    • Birch, H.L.1    McLaughlin, L.2    Smith, R.K.W.3    Goodship, A.E.4
  • 71
    • 0035164481 scopus 로고    scopus 로고
    • Effects of long-term exercise on the biomechanical properties of the Achilles tendon of Guinea Fowl
    • Buchanan, C.I., and Marsh, R.L. (2001) Effects of long-term exercise on the biomechanical properties of the Achilles tendon of Guinea Fowl. J. Appl. Physiol. 90, 164-171.
    • (2001) J. Appl. Physiol , vol.90 , pp. 164-171
    • Buchanan, C.I.1    Marsh, R.L.2
  • 73
    • 33645896138 scopus 로고    scopus 로고
    • Adaptability of elderly human muscles and tendons to increased loading
    • Narici, M., and Maganaris, C.N. (2006) Adaptability of elderly human muscles and tendons to increased loading. J.Anat. 208, 433-443.
    • (2006) J.Anat , vol.208 , pp. 433-443
    • Narici, M.1    Maganaris, C.N.2
  • 74
    • 0037320115 scopus 로고    scopus 로고
    • Increased crosssectional area and reduced tensile stress of the Achilles tendon in elderly compared with young women
    • Magnusson, S.P., Beyer, N., Abrahamsen, H., Aagaard, P., Neergaard, K., and Kajer, M. (2003) Increased crosssectional area and reduced tensile stress of the Achilles tendon in elderly compared with young women. J. Gerontol. A. Biol. Sci. Med. Sci. 58, 123-127.
    • (2003) J. Gerontol. A. Biol. Sci. Med. Sci , vol.58 , pp. 123-127
    • Magnusson, S.P.1    Beyer, N.2    Abrahamsen, H.3    Aagaard, P.4    Neergaard, K.5    Kajer, M.6
  • 75
    • 0026045037 scopus 로고
    • The vascularity of the rotator cuff
    • Chansky, H.A., and Iannotti, I.P. (1991) The vascularity of the rotator cuff. Clin. Sports Med. 10, 807-822.
    • (1991) Clin. Sports Med , vol.10 , pp. 807-822
    • Chansky, H.A.1    Iannotti, I.P.2
  • 76
    • 84940618287 scopus 로고
    • Three-dimensional ultrastructure of human tendons
    • Jozsa, L., Kannus. P., Balint, B.J., and Reffy, A. (1991) Three-dimensional ultrastructure of human tendons. Acta Anat. 142, 306-312.
    • (1991) Acta Anat , vol.142 , pp. 306-312
    • Jozsa, L.1    Kannus, P.2    Balint, B.J.3    Reffy, A.4
  • 77
    • 0025218977 scopus 로고
    • Aggregational state and molecular order of tendons as function of age
    • de Campos Vidal, B., and de Carvalho, H.F. (1990) Aggregational state and molecular order of tendons as function of age. Matrix 10, 48-57.
    • (1990) Matrix , vol.10 , pp. 48-57
    • de Campos Vidal, B.1    de Carvalho, H.F.2
  • 78
    • 0023198987 scopus 로고
    • Chemistry of the collagen cross-links. Origin and partial characterization of a putative mature cross-link of collagen
    • Barnard, K., Light, N.D., Sims, T.J., and Bailey, A.J. (1987) Chemistry of the collagen cross-links. Origin and partial characterization of a putative mature cross-link of collagen. Biochem. J. 244, 303-309.
    • (1987) Biochem. J , vol.244 , pp. 303-309
    • Barnard, K.1    Light, N.D.2    Sims, T.J.3    Bailey, A.J.4
  • 79
    • 0035978878 scopus 로고    scopus 로고
    • Molecular mechanisms of ageing in connective tissues
    • Bailey, A.J. (2001) Molecular mechanisms of ageing in connective tissues. Mech. Ageing Dev. 122, 735-755.
    • (2001) Mech. Ageing Dev , vol.122 , pp. 735-755
    • Bailey, A.J.1
  • 80
    • 0031687318 scopus 로고    scopus 로고
    • Effect of exercise training on passive stiffness in locomotor skeletal muscle: Role of extracellular matrix
    • Gosselin, L.E., Adams, C., Cotter, T.A., McCormick, R.J., and Thomas D.P. (1998) Effect of exercise training on passive stiffness in locomotor skeletal muscle: role of extracellular matrix. J. Appl. Physiol. 85, 1011-1016.
    • (1998) J. Appl. Physiol , vol.85 , pp. 1011-1016
    • Gosselin, L.E.1    Adams, C.2    Cotter, T.A.3    McCormick, R.J.4    Thomas, D.P.5
  • 81
    • 0015063391 scopus 로고
    • The tridimensional structure of native collagenous fibrils, their proteinaceous filaments
    • Bouteille, M., and Pease, D.C. (1971) The tridimensional structure of native collagenous fibrils, their proteinaceous filaments. J. Ultrastruct. Res. 35, 314-338.
    • (1971) J. Ultrastruct. Res , vol.35 , pp. 314-338
    • Bouteille, M.1    Pease, D.C.2
  • 82
    • 0031658373 scopus 로고
    • A consensus model for molecular packing of type I collagen
    • Wess, T.J., Hammersley, A.P., Wess, L., and Miller, A. (1988) A consensus model for molecular packing of type I collagen. J. Struct. Biol. 122, 92-100.
    • (1988) J. Struct. Biol , vol.122 , pp. 92-100
    • Wess, T.J.1    Hammersley, A.P.2    Wess, L.3    Miller, A.4
  • 83
    • 0022653567 scopus 로고
    • Cryosection of X-ray monitored collagen fibrils provide support for quasihexagonal packing
    • Chew, M.W.K., and Squire, J.M. (1986) Cryosection of X-ray monitored collagen fibrils provide support for quasihexagonal packing. Int. J. Biol. Macromol. 8, 27-36.
    • (1986) Int. J. Biol. Macromol , vol.8 , pp. 27-36
    • Chew, M.W.K.1    Squire, J.M.2
  • 84
    • 0028910961 scopus 로고
    • Radial packing, order, and disorder in collagen fibrils
    • Hulmes, D.J.S., Wess, T.J., Prockop, D.J., and Fartzl, 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.J.S.1    Wess, T.J.2    Prockop, D.J.3    Fartzl, P.4
  • 87
    • 0018219823 scopus 로고
    • A comparison of the size distribution of collagen fibrils in connective tissue as a function of age and a possible relation between fibril size distribution and mechanical properties
    • Parry, D.A., Barnes, G.R.G., and Craig, A.S. (1978) A comparison of the size distribution of collagen fibrils in connective tissue as a function of age and a possible relation between fibril size distribution and mechanical properties. Proc. R. Soc. Lond. B Biol. Sci. 203, 305-321.
    • (1978) Proc. R. Soc. Lond. B Biol. Sci , vol.203 , pp. 305-321
    • Parry, D.A.1    Barnes, G.R.G.2    Craig, A.S.3
  • 88
    • 0023387265 scopus 로고
    • A quantitative ultrastructural study of rat tail tendon from birth to maturity
    • Moore, M.J., and De Beaux, A. (1987) A quantitative ultrastructural study of rat tail tendon from birth to maturity. J. Anat. 153, 163-169.
    • (1987) J. Anat , vol.153 , pp. 163-169
    • Moore, M.J.1    De Beaux, A.2
  • 89
    • 0028019009 scopus 로고
    • Effect of ageing on ultrastructure of slow and fast skeletal muscle tendon in rabbit Achilles tendon
    • Nakagawa, Y., Majima, T., and Nagashima K. (1994) Effect of ageing on ultrastructure of slow and fast skeletal muscle tendon in rabbit Achilles tendon. Acta Physiol. Scand. 152, 307-313.
    • (1994) Acta Physiol. Scand , vol.152 , pp. 307-313
    • Nakagawa, Y.1    Majima, T.2    Nagashima, K.3
  • 90
    • 0024465294 scopus 로고
    • Effect of disuse on the ultrastructure of the Achilles tendon in rats
    • Nakagawa, Y., Totsuka, M., Sato, T., Fukuda, Y., and Hirota, K. (1989) Effect of disuse on the ultrastructure of the Achilles tendon in rats. Eur. J. Appl. Physiol. 59, 239-242.
    • (1989) Eur. J. Appl. Physiol , vol.59 , pp. 239-242
    • Nakagawa, Y.1    Totsuka, M.2    Sato, T.3    Fukuda, Y.4    Hirota, K.5
  • 91
    • 0017116224 scopus 로고
    • Ultrastructural features of adult human tendon
    • Dyer, R.F., and Enna, C.D. (1976) Ultrastructural features of adult human tendon. Cell Tissue Res. 168, 247-259.
    • (1976) Cell Tissue Res , vol.168 , pp. 247-259
    • Dyer, R.F.1    Enna, C.D.2
  • 92
    • 0021174766 scopus 로고
    • Polarization and electron microscopic studies on the collagen of intact and ruptured human tendons
    • Jozsa, L., Reffy, A., and Balint, B.J. (1984) Polarization and electron microscopic studies on the collagen of intact and ruptured human tendons. Acta Histochem. 74, 209-215.
    • (1984) Acta Histochem , vol.74 , pp. 209-215
    • Jozsa, L.1    Reffy, A.2    Balint, B.J.3
  • 93
    • 0033870607 scopus 로고    scopus 로고
    • Role of storage on charges in the mechanical properties of tendon and self-assembled collagen fibers
    • Silver, F.H., Christiansen, D.L., Snowhill, P.B., and Chen, Y. (2000) Role of storage on charges in the mechanical properties of tendon and self-assembled collagen fibers. Conn. Tiss. Res. 42, 155-164.
    • (2000) Conn. Tiss. Res , vol.42 , pp. 155-164
    • Silver, F.H.1    Christiansen, D.L.2    Snowhill, P.B.3    Chen, Y.4
  • 95
    • 0023034390 scopus 로고
    • Differences in the fibril structure of corneal and tendon collagen. An electron microscopy and X-ray diffraction investigation
    • Marchini, M., Morocutti, M., Ruggeri, A., Koch, M.H.J., Bigi, A., and Roveri, N. (1986) Differences in the fibril structure of corneal and tendon collagen. An electron microscopy and X-ray diffraction investigation. Conn. Tiss. Res. 15, 269-281.
    • (1986) Conn. Tiss. Res , vol.15 , pp. 269-281
    • Marchini, M.1    Morocutti, M.2    Ruggeri, A.3    Koch, M.H.J.4    Bigi, A.5    Roveri, N.6
  • 96
    • 26644442130 scopus 로고    scopus 로고
    • The 3D structure of crimps in the rat Achilles tendon
    • Raspanti, M., Manelli, A., Franchi, M., and Ruggeri, A. (2005) The 3D structure of crimps in the rat Achilles tendon. Matrix Biol. 24, 503-507.
    • (2005) Matrix Biol , vol.24 , pp. 503-507
    • Raspanti, M.1    Manelli, A.2    Franchi, M.3    Ruggeri, A.4
  • 98
    • 0035155477 scopus 로고    scopus 로고
    • Transition from viscous to elastic-dependency of mechanical properties of self-assembled collagen fibers
    • Silver, F.H., Christiansen, D.L., Snowhill, P.B., and Chen, Y. (2001) Transition from viscous to elastic-dependency of mechanical properties of self-assembled collagen fibers. J. Pol. Sci. 7, 134-142.
    • (2001) J. Pol. Sci , vol.7 , pp. 134-142
    • Silver, F.H.1    Christiansen, D.L.2    Snowhill, P.B.3    Chen, Y.4
  • 99
    • 0036308986 scopus 로고    scopus 로고
    • Mechanical implications of the domain structure of fibril forming collagens: Comparison of the molecular and fibrillar flexibilities of the alpha1-chains found in types I-III collagen
    • Silver., F.H., Horvath, I., and Foran, D.J. (2002) Mechanical implications of the domain structure of fibril forming collagens: comparison of the molecular and fibrillar flexibilities of the alpha1-chains found in types I-III collagen. J. Theor. Biol. 216, 243-254.
    • (2002) J. Theor. Biol , vol.216 , pp. 243-254
    • Silver, F.H.1    Horvath, I.2    Foran, D.J.3
  • 100
    • 0035145015 scopus 로고    scopus 로고
    • Influence of static stretching on viscoelastic properties of human tendon structures in vivo
    • Kubo, K., Kanehisa, H., Kawakami, Y., and Fukunaga, T. (2001) Influence of static stretching on viscoelastic properties of human tendon structures in vivo. J. Appl. Physiol. 90, 520-527.
    • (2001) J. Appl. Physiol , vol.90 , pp. 520-527
    • Kubo, K.1    Kanehisa, H.2    Kawakami, Y.3    Fukunaga, T.4
  • 101
    • 0036096319 scopus 로고    scopus 로고
    • Effects of transient muscle contractions and stretching on the tendon structures in vivo
    • Kubo, K., Kanehisa, H., and Fukunaga, T. (2002) Effects of transient muscle contractions and stretching on the tendon structures in vivo. Acta Physiol. Scand. 175, 157-164.
    • (2002) Acta Physiol. Scand , vol.175 , pp. 157-164
    • Kubo, K.1    Kanehisa, H.2    Fukunaga, T.3
  • 102
    • 0036402664 scopus 로고    scopus 로고
    • Effects of resistance and stretching training programmes on the viscoelastic properties of human tendon structures in vivo
    • Kubo, K., Kanehisa H., and Fukunaga, T. (2002) Effects of resistance and stretching training programmes on the viscoelastic properties of human tendon structures in vivo. J. Physiol. 538, 219-226.
    • (2002) J. Physiol , vol.538 , pp. 219-226
    • Kubo, K.1    Kanehisa, H.2    Fukunaga, T.3
  • 104
    • 0030246115 scopus 로고    scopus 로고
    • Elongation mechanism of collagen fibrils and force-strain relationships of tendon at each level of structural hierarchy
    • Sasaki, N., and Odajima, S. (1996) Elongation mechanism of collagen fibrils and force-strain relationships of tendon at each level of structural hierarchy. J. Biomech. 9, 1131-1136.
    • (1996) J. Biomech , vol.9 , pp. 1131-1136
    • Sasaki, N.1    Odajima, S.2
  • 105
    • 0000658473 scopus 로고    scopus 로고
    • Folkard, W., Mosler, E., Geercken, E., Knorzer, H., Nemetschek-Gansler, Nemetschek Th., and Koch, J. (1987) Quantitative analysis of the molecular sliding mechanism in native tendon collagen-time-resolved dynamic studies using synchrotron radiation. Int. J. Biol. Macromolec. 9, 169-175.
    • Folkard, W., Mosler, E., Geercken, E., Knorzer, H., Nemetschek-Gansler, Nemetschek Th., and Koch, J. (1987) Quantitative analysis of the molecular sliding mechanism in native tendon collagen-time-resolved dynamic studies using synchrotron radiation. Int. J. Biol. Macromolec. 9, 169-175.
  • 106
    • 0024493670 scopus 로고
    • Anisotropic and biomechanical properties of tendon modified by exercise and denervation: Aggregation and macromolecular order in collagen bundles
    • Vilarta, R., and deCampos Vidal B. (1989) Anisotropic and biomechanical properties of tendon modified by exercise and denervation: aggregation and macromolecular order in collagen bundles. Matrix 9, 55-61.
    • (1989) Matrix , vol.9 , pp. 55-61
    • Vilarta, R.1    deCampos Vidal, B.2
  • 107
    • 0026940450 scopus 로고
    • Control of collagen fibril diameters in tissues
    • Scott, J.E., and Parry, A.D. (1992) Control of collagen fibril diameters in tissues. Int. J. Biol. Macromolec. 14, 292-293.
    • (1992) Int. J. Biol. Macromolec , vol.14 , pp. 292-293
    • Scott, J.E.1    Parry, A.D.2
  • 108
    • 0021905789 scopus 로고
    • Proteoglycan-type I collagen fibril interactions in bone and non-calcifying connective tissues
    • Scott, J.E., and Haigh, M. (1985) Proteoglycan-type I collagen fibril interactions in bone and non-calcifying connective tissues. Biosci. Rep. 5, 71-81.
    • (1985) Biosci. Rep , vol.5 , pp. 71-81
    • Scott, J.E.1    Haigh, M.2
  • 109
    • 2442517329 scopus 로고    scopus 로고
    • Strain-sensitive mechanical properties of tendon fascicles from mice with genetically engineered alterations in collagen and decorin
    • Robinson, P.S., Lin, T.W., Reynolds, P.R., Derwin, K.A., Iozzo, R.V., and Soslowsky, L.J. (2004) Strain-sensitive mechanical properties of tendon fascicles from mice with genetically engineered alterations in collagen and decorin. J. Biomech. Eng. 126, 252-257.
    • (2004) J. Biomech. Eng , vol.126 , pp. 252-257
    • Robinson, P.S.1    Lin, T.W.2    Reynolds, P.R.3    Derwin, K.A.4    Iozzo, R.V.5    Soslowsky, L.J.6
  • 110
    • 0346242689 scopus 로고    scopus 로고
    • Elasticity in extracellular matrix shape modules of tendon, cartilage, etc. A sliding proteoglycan-filament model
    • Scott, J.E. (2003) Elasticity in extracellular matrix shape modules of tendon, cartilage, etc. A sliding proteoglycan-filament model. J. Physiol. 553, 335-343.
    • (2003) J. Physiol , vol.553 , pp. 335-343
    • Scott, J.E.1
  • 111
    • 34047203177 scopus 로고    scopus 로고
    • An investigation into the effects of the hierarchical structure of tendon fascicles on micromechanical properties
    • Screen, H.R.C., Lee, D.A., Bader, D.L., and Shelton, J.C. (2004) An investigation into the effects of the hierarchical structure of tendon fascicles on micromechanical properties. J. Biomech. Eng. 126, 252-257.
    • (2004) J. Biomech. Eng , vol.126 , pp. 252-257
    • Screen, H.R.C.1    Lee, D.A.2    Bader, D.L.3    Shelton, J.C.4
  • 112
    • 0024313452 scopus 로고
    • An estimate of the mean length of collagen fibrils in rat tailtendon as a function of age
    • Craig, A., Birtles, M., Conway, J., and Parry, D. (1989). An estimate of the mean length of collagen fibrils in rat tailtendon as a function of age. Connect. Tissue Res. 19, 51-62.
    • (1989) Connect. Tissue Res , vol.19 , pp. 51-62
    • Craig, A.1    Birtles, M.2    Conway, J.3    Parry, D.4
  • 113
  • 114
    • 0015274766 scopus 로고
    • Simultaneous mechanical and light microscopic studies of collagen fibers
    • Viidik, A. (1972) Simultaneous mechanical and light microscopic studies of collagen fibers. Anat. Entwickl. Gesch. 136, 204-212.
    • (1972) Anat. Entwickl. Gesch , vol.136 , pp. 204-212
    • Viidik, A.1
  • 115
    • 0015505561 scopus 로고
    • Collagen ultrastrucuture and its relation to mechanical properties as a function of aging
    • Diamant, J., Keller, A., Baer, E., Litt, M., and Arridge, G.C. (1972) Collagen ultrastrucuture and its relation to mechanical properties as a function of aging. Proc. R. Soc. Lond. B. Biol. Sci. 180, 293-315.
    • (1972) Proc. R. Soc. Lond. B. Biol. Sci , vol.180 , pp. 293-315
    • Diamant, J.1    Keller, A.2    Baer, E.3    Litt, M.4    Arridge, G.C.5
  • 116
    • 0018950212 scopus 로고
    • A structural model for tendon crimping
    • Kastelic, J., Palley, I., and Baer, E. (1980) A structural model for tendon crimping. J. Biomech. 13, 887-893.
    • (1980) J. Biomech , vol.13 , pp. 887-893
    • Kastelic, J.1    Palley, I.2    Baer, E.3
  • 117
    • 0025726552 scopus 로고
    • Crimp morphology in the fibre-forming collagens
    • Gathercole, L.J., and Keller, A. (1991) Crimp morphology in the fibre-forming collagens. Matrix 11, 214-234.
    • (1991) Matrix , vol.11 , pp. 214-234
    • Gathercole, L.J.1    Keller, A.2
  • 118
    • 0028937275 scopus 로고
    • Crimps as part of a helical structure
    • de Campos Vidal, B. (1995) Crimps as part of a helical structure. C.R. Acad. Sci. Ser. III 318, 173-178.
    • (1995) C.R. Acad. Sci. Ser. III , vol.318 , pp. 173-178
    • de Campos Vidal, B.1
  • 119
    • 0010463247 scopus 로고    scopus 로고
    • Tendons and ligaments
    • Comper, W.D, ed, Harwood Academic Publishes, Amsterdam
    • Viidik, A. (1996) Tendons and ligaments. In: Comper, W.D. (ed.), Extracellular Matrix, vol. I. Tissue function. Harwood Academic Publishes, Amsterdam, 303-327.
    • (1996) Extracellular Matrix. Tissue function , vol.1 , pp. 303-327
    • Viidik, A.1
  • 120
    • 0036176293 scopus 로고    scopus 로고
    • Recruitment of tendon crimp with applied tensile strain
    • Hansen, K.A., Weiss, J.A., and Barton, J.K. (2002) Recruitment of tendon crimp with applied tensile strain. J. Biomech. Eng. 124, 72-77.
    • (2002) J. Biomech. Eng , vol.124 , pp. 72-77
    • Hansen, K.A.1    Weiss, J.A.2    Barton, J.K.3
  • 121
    • 0242709860 scopus 로고    scopus 로고
    • Image analysis of tendon helical superstructure using interference and polarized light microscopy
    • de Campos Vidal, B. (2003) Image analysis of tendon helical superstructure using interference and polarized light microscopy. Micron 34, 423-432.
    • (2003) Micron , vol.34 , pp. 423-432
    • de Campos Vidal, B.1
  • 122
    • 0032801772 scopus 로고    scopus 로고
    • The tensile and stress relaxation responses of human patellar tendon varies with specimen cross-sectional area
    • Atkinson, T.S., Ewers, B., and Haut, R.C. (1999) The tensile and stress relaxation responses of human patellar tendon varies with specimen cross-sectional area. J. Biomech. 32, 907-914.
    • (1999) J. Biomech , vol.32 , pp. 907-914
    • Atkinson, T.S.1    Ewers, B.2    Haut, R.C.3
  • 123
    • 0030865343 scopus 로고    scopus 로고
    • Versatile collagens in invertebrates
    • Engel, J. (1997) Versatile collagens in invertebrates. Science 277,1785-1786.
    • (1997) Science , vol.277 , pp. 1785-1786
    • Engel, J.1
  • 124
    • 0021126710 scopus 로고    scopus 로고
    • Silver, F.H., and Birk, D.E. (1984) Molecular structure of collagen in solution: comparison of types I, II, III and V. Int. J. Biol. Macromol. 6, 125-132.
    • Silver, F.H., and Birk, D.E. (1984) Molecular structure of collagen in solution: comparison of types I, II, III and V. Int. J. Biol. Macromol. 6, 125-132.
  • 126
    • 0030152813 scopus 로고    scopus 로고
    • Stress-strain curve and Young's modulus of a collagen molecule as determined by the X-ray diffraction technique
    • Sasakai, N., and Odajima, S. (1996) Stress-strain curve and Young's modulus of a collagen molecule as determined by the X-ray diffraction technique. J. Biomech. 29, 655-658.
    • (1996) J. Biomech , vol.29 , pp. 655-658
    • Sasakai, N.1    Odajima, S.2
  • 127
    • 0025800074 scopus 로고
    • Two type XII-like collagens localize to the surface of banded collagen fibrils
    • Keene, D.R., Lunstrum, G.P., Morris, N.P., Stoddard, D.W., and Burgeson, R.E. (1991) Two type XII-like collagens localize to the surface of banded collagen fibrils. J. Cell Biol. 113, 971-978.
    • (1991) J. Cell Biol , vol.113 , pp. 971-978
    • Keene, D.R.1    Lunstrum, G.P.2    Morris, N.P.3    Stoddard, D.W.4    Burgeson, R.E.5
  • 128
    • 0033558813 scopus 로고    scopus 로고
    • Rapid and reversible regulation of collagen XII expression by mechanical stress
    • Trachslin, J., Koch, M., and Chiquet, M. (1999) Rapid and reversible regulation of collagen XII expression by mechanical stress. Exp. Cell. Res. 247, 320-328.
    • (1999) Exp. Cell. Res , vol.247 , pp. 320-328
    • Trachslin, J.1    Koch, M.2    Chiquet, M.3
  • 129
    • 0027971943 scopus 로고
    • Type XII and XIV collagens mediated interactions between banded collagen fibers in vitro and may modulate extracellular matrix deformability
    • Nishiyama, T., McDonough, A.M., Bruns, P.R., and Burgeson, R.E. (1994) Type XII and XIV collagens mediated interactions between banded collagen fibers in vitro and may modulate extracellular matrix deformability. J. Biol. Chem. 269, 28193-28199.
    • (1994) J. Biol. Chem , vol.269 , pp. 28193-28199
    • Nishiyama, T.1    McDonough, A.M.2    Bruns, P.R.3    Burgeson, R.E.4
  • 130
    • 0000501039 scopus 로고
    • Age-related changes in connective tissues
    • ed. Viidik A, London: Academic Press
    • Viidik, A. (1982) Age-related changes in connective tissues. In: Lectures on Gerontology (ed. Viidik A.), London: Academic Press. 173-211.
    • (1982) Lectures on Gerontology , pp. 173-211
    • Viidik, A.1
  • 132
    • 1642313674 scopus 로고    scopus 로고
    • Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading
    • Kjaer, M. (2004) Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading. Physiol. Rev. 84, 649-698.
    • (2004) Physiol. Rev , vol.84 , pp. 649-698
    • Kjaer, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.