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Volumn 94, Issue 4, 2013, Pages 248-259

The role of the non-collagenous matrix in tendon function

Author keywords

Ageing; Glycoprotein; Interfascicular matrix; Proteoglycan; Structure function

Indexed keywords

COLLAGEN TYPE 1; GLYCOPROTEIN; PROTEOGLYCAN;

EID: 84880269257     PISSN: 09599673     EISSN: 13652613     Source Type: Journal    
DOI: 10.1111/iep.12027     Document Type: Review
Times cited : (159)

References (121)
  • 1
    • 0019490755 scopus 로고
    • Elastin as a random-network elastomer: a mechanical and optical analysis of single elastin fibers
    • Aaron B.B. & Gosline J.M. (1981) Elastin as a random-network elastomer: a mechanical and optical analysis of single elastin fibers. Biopolymers 20, 1247-1260.
    • (1981) Biopolymers , vol.20 , pp. 1247-1260
    • Aaron, B.B.1    Gosline, J.M.2
  • 2
    • 0036148897 scopus 로고    scopus 로고
    • In situ cell nucleus deformation in tendons under tensile load; a morphological analysis using confocal laser microscopy
    • Arnoczky S.P., Lavagnino M., Whallon J.H., Hoonjan A. (2002) In situ cell nucleus deformation in tendons under tensile load; a morphological analysis using confocal laser microscopy. J. Orthop. Res. 20, 29-35.
    • (2002) J. Orthop. Res. , vol.20 , pp. 29-35
    • Arnoczky, S.P.1    Lavagnino, M.2    Whallon, J.H.3    Hoonjan, A.4
  • 4
    • 79952721821 scopus 로고    scopus 로고
    • Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity
    • Baldock C., Oberhauser A.F., Ma L. et al. (2011) Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity. Proc. Natl Acad. Sci. USA 108, 4322-4327.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 4322-4327
    • Baldock, C.1    Oberhauser, A.F.2    Ma, L.3
  • 5
    • 51949094410 scopus 로고    scopus 로고
    • Collagen fibrillogenesis in tendon development: current models and regulation of fibril assembly
    • Banos C.C., Thomas A.H., Kuo C.K. (2008) Collagen fibrillogenesis in tendon development: current models and regulation of fibril assembly. Birth Defects Res. C Embryo Today 84, 228-244.
    • (2008) Birth Defects Res. C Embryo Today , vol.84 , pp. 228-244
    • Banos, C.C.1    Thomas, A.H.2    Kuo, C.K.3
  • 6
    • 0141958551 scopus 로고    scopus 로고
    • Are the material properties and matrix composition of equine flexor and extensor tendons determined by their functions?
    • Batson E.L., Paramour R.J., Smith T.J., Birch H.L., Patterson-Kane J.C., Goodship A.E. (2003) Are the material properties and matrix composition of equine flexor and extensor tendons determined by their functions? Equine Vet. J. 35, 314-318.
    • (2003) Equine Vet. J. , vol.35 , pp. 314-318
    • Batson, E.L.1    Paramour, R.J.2    Smith, T.J.3    Birch, H.L.4    Patterson-Kane, J.C.5    Goodship, A.E.6
  • 7
    • 0031827973 scopus 로고    scopus 로고
    • Muscle-tendon stresses and elastic energy storage during locomotion in the horse
    • Biewener A.A. (1998) Muscle-tendon stresses and elastic energy storage during locomotion in the horse. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 120, 73-87.
    • (1998) Comp. Biochem. Physiol. B, Biochem. Mol. Biol. , vol.120 , pp. 73-87
    • Biewener, A.A.1
  • 8
    • 34547879628 scopus 로고    scopus 로고
    • Tendon matrix composition and turnover in relation to functional requirements
    • Birch H.L. (2007) Tendon matrix composition and turnover in relation to functional requirements. Int. J. Exp. Pathol. 88, 241-248.
    • (2007) Int. J. Exp. Pathol. , vol.88 , pp. 241-248
    • Birch, H.L.1
  • 9
    • 0032198563 scopus 로고    scopus 로고
    • Macroscopic 'degeneration' of equine superficial digital flexor tendon is accompanied by a change in extracellular matrix composition
    • Birch H.L., Bailey A.J., Goodship A.E. (1998) Macroscopic 'degeneration' of equine superficial digital flexor tendon is accompanied by a change in extracellular matrix composition. Equine Vet. J. 30, 534-539.
    • (1998) Equine Vet. J. , vol.30 , pp. 534-539
    • Birch, H.L.1    Bailey, A.J.2    Goodship, A.E.3
  • 10
    • 0033194907 scopus 로고    scopus 로고
    • Age-related changes to the molecular and cellular components of equine flexor tendons
    • Birch H.L., Bailey J.V., Bailey A.J., Goodship A.E. (1999) Age-related changes to the molecular and cellular components of equine flexor tendons. Equine Vet. J. 31, 391-396.
    • (1999) Equine Vet. J. , vol.31 , pp. 391-396
    • Birch, H.L.1    Bailey, J.V.2    Bailey, A.J.3    Goodship, A.E.4
  • 12
    • 0028923480 scopus 로고
    • Collagen fibrillogenesis in situ: fibril segments undergo post-depositional modifications resulting in linear and lateral growth during matrix development
    • Birk D.E., Nurminskaya M.V., Zycband E.I. (1995) Collagen fibrillogenesis in situ: fibril segments undergo post-depositional modifications 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
  • 13
    • 0035034042 scopus 로고    scopus 로고
    • A novel gene, tendin, is strongly expressed in tendons and ligaments and shows high homology with chondromodulin-I
    • Brandau O., Meindl A., Fassler R., Aszodi A. (2001) A novel gene, tendin, is strongly expressed in tendons and ligaments and shows high homology with chondromodulin-I. Dev. Dyn. 221, 72-80.
    • (2001) Dev. Dyn. , vol.221 , pp. 72-80
    • Brandau, O.1    Meindl, A.2    Fassler, R.3    Aszodi, A.4
  • 15
    • 34548454116 scopus 로고    scopus 로고
    • The micro-structural strain response of tendon
    • Cheng V.W.T. & Screen H.R.C. (2007) The micro-structural strain response of tendon. J. Mater. Sci. 42, 8957-8965.
    • (2007) J. Mater. Sci. , vol.42 , pp. 8957-8965
    • Cheng, V.W.T.1    Screen, H.R.C.2
  • 16
    • 0035991242 scopus 로고    scopus 로고
    • Phenotypic effects of biglycan deficiency are linked to collagen fibril abnormalities, are synergized by decorin deficiency, and mimic Ehlers-Danlos-like changes in bone and other connective tissues
    • Corsi A., Xu T., Chen X.D. et al. (2002) Phenotypic effects of biglycan deficiency are linked to collagen fibril abnormalities, are synergized by decorin deficiency, and mimic Ehlers-Danlos-like changes in bone and other connective tissues. J. Bone Miner. Res. 17, 1180-1189.
    • (2002) J. Bone Miner. Res. , vol.17 , pp. 1180-1189
    • Corsi, A.1    Xu, T.2    Chen, X.D.3
  • 18
    • 11844286305 scopus 로고    scopus 로고
    • Tenomodulin is necessary for tenocyte proliferation and tendon maturation
    • Docheva D., Hunziker E.B., Fassler R., Brandau O. (2005) Tenomodulin is necessary for tenocyte proliferation and tendon maturation. Mol. Cell. Biol. 25, 699-705.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 699-705
    • Docheva, D.1    Hunziker, E.B.2    Fassler, R.3    Brandau, O.4
  • 19
    • 84859882811 scopus 로고    scopus 로고
    • Influence of decorin on the mechanical, compositional, and structural properties of the mouse patellar tendon
    • Dourte L.M., Pathmanathan L., Jawad A.F. et al. (2012) Influence of decorin on the mechanical, compositional, and structural properties of the mouse patellar tendon. J. Biomech. Eng. 134, 031005.
    • (2012) J. Biomech. Eng. , vol.134 , pp. 031005
    • Dourte, L.M.1    Pathmanathan, L.2    Jawad, A.F.3
  • 20
    • 67651172893 scopus 로고    scopus 로고
    • Descriptive epidemiology of fracture, tendon and suspensory ligament injuries in National Hunt racehorses in training
    • Ely E.R., Avella C.S., Price J.S., Smith R.K., Wood J.L., Verheyen K.L. (2009) Descriptive epidemiology of fracture, tendon and suspensory ligament injuries in National Hunt racehorses in training. Equine Vet. J. 41, 372-378.
    • (2009) Equine Vet. J. , vol.41 , pp. 372-378
    • Ely, E.R.1    Avella, C.S.2    Price, J.S.3    Smith, R.K.4    Wood, J.L.5    Verheyen, K.L.6
  • 21
    • 46449105265 scopus 로고    scopus 로고
    • Effect of NKISK on tendon lengthening: an in vivo model for various clinically applicable dosing regimens
    • Esther R.J., Creighton R.A., Draeger R.W., Weinhold P.S., Dahners L.E. (2008) Effect of NKISK on tendon lengthening: an in vivo model for various clinically applicable dosing regimens. J. Orthop. Res. 26, 971-976.
    • (2008) J. Orthop. Res. , vol.26 , pp. 971-976
    • Esther, R.J.1    Creighton, R.A.2    Draeger, R.W.3    Weinhold, P.S.4    Dahners, L.E.5
  • 22
    • 0034645039 scopus 로고    scopus 로고
    • Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons
    • Ezura Y., Chakravarti S., Oldberg A., Chervoneva I., Birk D.E. (2000) Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons. J. Cell Biol. 151, 779-788.
    • (2000) J. Cell Biol. , vol.151 , pp. 779-788
    • Ezura, Y.1    Chakravarti, S.2    Oldberg, A.3    Chervoneva, I.4    Birk, D.E.5
  • 24
    • 70450228394 scopus 로고    scopus 로고
    • Evidence against proteoglycan mediated collagen fibril load transmission and dynamic viscoelasticity in tendon
    • Fessel G. & Snedeker J.G. (2009) Evidence against proteoglycan mediated collagen fibril load transmission and dynamic viscoelasticity in tendon. Matrix Biol. 28, 503-510.
    • (2009) Matrix Biol. , vol.28 , pp. 503-510
    • Fessel, G.1    Snedeker, J.G.2
  • 25
    • 77958064869 scopus 로고    scopus 로고
    • Equivalent stiffness after glycosaminoglycan depletion in tendon-an ultra-structural finite element model and corresponding experiments
    • Fessel G. & Snedeker J.G. (2011) Equivalent stiffness after glycosaminoglycan depletion in tendon-an ultra-structural finite element model and corresponding experiments. J. Theor. Biol. 268, 77-83.
    • (2011) J. Theor. Biol. , vol.268 , pp. 77-83
    • Fessel, G.1    Snedeker, J.G.2
  • 26
    • 0033608160 scopus 로고    scopus 로고
    • Articular Cartilage Superficial Zone Protein (SZP) Is Homologous to Megakaryocyte Stimulating Factor Precursor and Is a Multifunctional Proteoglycan with Potential Growth-Promoting, Cytoprotective, and Lubricating Properties in Cartilage Metabolism
    • Flannery C.R., Hughes C.E., Schumacher B.L. et al. (1999) Articular Cartilage Superficial Zone Protein (SZP) Is Homologous to Megakaryocyte Stimulating Factor Precursor and Is a Multifunctional Proteoglycan with Potential Growth-Promoting, Cytoprotective, and Lubricating Properties in Cartilage Metabolism. Biochem. Biophys. Res. Commun. 254, 535-541.
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 535-541
    • Flannery, C.R.1    Hughes, C.E.2    Schumacher, B.L.3
  • 27
    • 43249103731 scopus 로고    scopus 로고
    • Different crimp patterns in collagen fibrils relate to the subfibrillar arrangement
    • Franchi M., Raspanti M., Dell'Orbo C. et al. (2008) Different crimp patterns in collagen fibrils relate to the subfibrillar arrangement. Connect. Tissue Res. 49, 85-91.
    • (2008) Connect. Tissue Res. , vol.49 , pp. 85-91
    • Franchi, M.1    Raspanti, M.2    Dell'Orbo, C.3
  • 28
    • 41849141223 scopus 로고    scopus 로고
    • Lubricin distribution in the goat infraspinatus tendon: a basis for interfascicular lubrication
    • Funakoshi T., Schmid T., Hsu H., Spector M. (2008) Lubricin distribution in the goat infraspinatus tendon: a basis for interfascicular lubrication. J. Bone Joint Surg. Am. 90, 803-814.
    • (2008) J. Bone Joint Surg. Am. , vol.90 , pp. 803-814
    • Funakoshi, T.1    Schmid, T.2    Hsu, H.3    Spector, M.4
  • 29
    • 77952485221 scopus 로고    scopus 로고
    • Distribution of lubricin in the ruptured human rotator cuff and biceps tendon: a pilot study
    • Funakoshi T., Martin S.D., Schmid T.M., Spector M. (2009) Distribution of lubricin in the ruptured human rotator cuff and biceps tendon: a pilot study. Clin. Orthop. Relat. Res. 468, 1588-1599.
    • (2009) Clin. Orthop. Relat. Res. , vol.468 , pp. 1588-1599
    • Funakoshi, T.1    Martin, S.D.2    Schmid, T.M.3    Spector, M.4
  • 31
    • 79960281031 scopus 로고    scopus 로고
    • Monitoring micrometer-scale collagen organization in rat-tail tendon upon mechanical strain using second harmonic microscopy
    • Goulam Houssen Y., Gusachenko I., Schanne-Klein M.C., Allain J.M. (2011) Monitoring micrometer-scale collagen organization in rat-tail tendon upon mechanical strain using second harmonic microscopy. J. Biomech. 44, 2047-2052.
    • (2011) J. Biomech. , vol.44 , pp. 2047-2052
    • Goulam Houssen, Y.1    Gusachenko, I.2    Schanne-Klein, M.C.3    Allain, J.M.4
  • 32
    • 35748950738 scopus 로고    scopus 로고
    • COMP acts as a catalyst in collagen fibrillogenesis
    • Halasz K., Kassner A., Morgelin M., Heinegard D. (2007) COMP acts as a catalyst in collagen fibrillogenesis. J. Biol. Chem. 282, 31166-31173.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31166-31173
    • Halasz, K.1    Kassner, A.2    Morgelin, M.3    Heinegard, D.4
  • 33
    • 38949112122 scopus 로고    scopus 로고
    • Lateral force transmission between human tendon fascicles
    • Haraldsson B.T., Aagaard P., Qvortrup K. et al. (2008) Lateral force transmission between human tendon fascicles. Matrix Biol. 27, 86-95.
    • (2008) Matrix Biol. , vol.27 , pp. 86-95
    • Haraldsson, B.T.1    Aagaard, P.2    Qvortrup, K.3
  • 34
    • 0024533495 scopus 로고
    • Interaction of a 59-kDa connective tissue matrix protein with collagen I and collagen II
    • Hedbom E. & Heinegard D. (1989) Interaction of a 59-kDa connective tissue matrix protein with collagen I and collagen II. J. Biol. Chem. 264, 6898-6905.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6898-6905
    • Hedbom, E.1    Heinegard, D.2
  • 35
    • 0018037777 scopus 로고
    • A study of the normal range of strain, strain rate, and stiffness of tendon
    • Herrick W.C., Kingsbury H.B., Lou D.Y. (1978) A study of the normal range of strain, strain rate, and stiffness of tendon. J. Biomed. Mater. Res. 12, 877-894.
    • (1978) J. Biomed. Mater. Res. , vol.12 , pp. 877-894
    • Herrick, W.C.1    Kingsbury, H.B.2    Lou, D.Y.3
  • 36
    • 77955886129 scopus 로고    scopus 로고
    • Achilles tendon rupture: a review of etiology, population, anatomy, risk factors, and injury prevention
    • Hess G.W. (2010) Achilles tendon rupture: a review of etiology, population, anatomy, risk factors, and injury prevention. Foot Ankle Spec. 3, 29-32.
    • (2010) Foot Ankle Spec. , vol.3 , pp. 29-32
    • Hess, G.W.1
  • 37
    • 0037040276 scopus 로고    scopus 로고
    • Versican Interacts with Fibrillin-1 and Links Extracellular Microfibrils to Other Connective Tissue Networks
    • Isogai Z., Aspberg A., Keene D.R., Ono R.N., Reinhardt D.P., Sakai L.Y. (2002) Versican Interacts with Fibrillin-1 and Links Extracellular Microfibrils to Other Connective Tissue Networks. J. Biol. Chem. 277, 4565-4572.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4565-4572
    • Isogai, Z.1    Aspberg, A.2    Keene, D.R.3    Ono, R.N.4    Reinhardt, D.P.5    Sakai, L.Y.6
  • 39
    • 0037348805 scopus 로고    scopus 로고
    • Mechanical loading regulates the expression of tenascin-C in the myotendinous junction and tendon but does not induce de novo synthesis in the skeletal muscle
    • Jarvinen T.A., Jozsa L., Kannus P. et al. (2003) Mechanical loading regulates the expression of tenascin-C in the myotendinous junction and tendon but does not induce de novo synthesis in the skeletal muscle. J. Cell Sci. 116, 857-866.
    • (2003) J. Cell Sci. , vol.116 , pp. 857-866
    • Jarvinen, T.A.1    Jozsa, L.2    Kannus, P.3
  • 40
    • 21644449866 scopus 로고    scopus 로고
    • ADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis
    • Jones G.C. & Riley G.P. (2005) ADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis. Arthritis Res. Ther. 7, 160-169.
    • (2005) Arthritis Res. Ther. , vol.7 , pp. 160-169
    • Jones, G.C.1    Riley, G.P.2
  • 41
    • 58649096818 scopus 로고    scopus 로고
    • Homologous sequence in lumican and fibromodulin leucine-rich repeat 5-7 competes for collagen binding
    • Kalamajski S. & Oldberg A. (2009) Homologous sequence in lumican and fibromodulin leucine-rich repeat 5-7 competes for collagen binding. J. Biol. Chem. 284, 534-539.
    • (2009) J. Biol. Chem. , vol.284 , pp. 534-539
    • Kalamajski, S.1    Oldberg, A.2
  • 42
    • 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, 312-320.
    • (2000) Scand. J. Med. Sci. Sports , vol.10 , pp. 312-320
    • Kannus, P.1
  • 43
    • 2542572389 scopus 로고    scopus 로고
    • Prevalence of superficial digital flexor tendonitis and suspensory desmitis in Japanese Thoroughbred flat racehorses in 1999
    • Kasashima Y., Takahashi T., Smith R.K. et al. (2004) Prevalence of superficial digital flexor tendonitis and suspensory desmitis in Japanese Thoroughbred flat racehorses in 1999. Equine Vet. J. 36, 346-350.
    • (2004) Equine Vet. J. , vol.36 , pp. 346-350
    • Kasashima, Y.1    Takahashi, T.2    Smith, R.K.3
  • 46
    • 69149095063 scopus 로고    scopus 로고
    • Potential roles for the small leucine-rich proteoglycans biglycan and fibromodulin in ectopic ossification of tendon induced by exercise and in modulating rotarod performance
    • Kilts T., Ameye L., Syed-Picard F. et al. (2009) Potential roles for the small leucine-rich proteoglycans biglycan and fibromodulin in ectopic ossification of tendon induced by exercise and in modulating rotarod performance. Scand. J. Med. Sci. Sports 19, 536-546.
    • (2009) Scand. J. Med. Sci. Sports , vol.19 , pp. 536-546
    • Kilts, T.1    Ameye, L.2    Syed-Picard, F.3
  • 47
    • 77956176666 scopus 로고    scopus 로고
    • Glycan profiling of a defect in decorin glycosylation in equine systemic proteoglycan accumulation, a potential model of progeroid form of Ehlers-Danlos syndrome
    • Kim B., Yoon J.H., Zhang J., Eric Mueller P.O., Halper J. (2010) Glycan profiling of a defect in decorin glycosylation in equine systemic proteoglycan accumulation, a potential model of progeroid form of Ehlers-Danlos syndrome. Arch. Biochem. Biophys. 501, 221-231.
    • (2010) Arch. Biochem. Biophys. , vol.501 , pp. 221-231
    • Kim, B.1    Yoon, J.H.2    Zhang, J.3    Eric Mueller, P.O.4    Halper, J.5
  • 48
    • 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
  • 49
    • 69149106086 scopus 로고    scopus 로고
    • From mechanical loading to collagen synthesis, structural changes and function in human tendon
    • Kjaer M., Langberg H., Heinemeier K. et al. (2009) From mechanical loading to collagen synthesis, structural changes and function in human tendon. Scand. J. Med. Sci. Sports 19, 500-510.
    • (2009) Scand. J. Med. Sci. Sports , vol.19 , pp. 500-510
    • Kjaer, M.1    Langberg, H.2    Heinemeier, K.3
  • 50
    • 46849085994 scopus 로고    scopus 로고
    • Acute and overuse injuries correlated to hours of training in master running athletes
    • Knobloch K., Yoon U., Vogt P.M. (2008) Acute and overuse injuries correlated to hours of training in master running athletes. Foot Ankle Int. 29, 671-676.
    • (2008) Foot Ankle Int. , vol.29 , pp. 671-676
    • Knobloch, K.1    Yoon, U.2    Vogt, P.M.3
  • 51
    • 79251535940 scopus 로고    scopus 로고
    • Tendon fascicle gliding in wild type, heterozygous, and lubricin knockout mice
    • Kohrs R.T., Zhao C., Sun Y.-L. et al. (2011) Tendon fascicle gliding in wild type, heterozygous, and lubricin knockout mice. J. Orthop. Res. 29, 384-389.
    • (2011) J. Orthop. Res. , vol.29 , pp. 384-389
    • Kohrs, R.T.1    Zhao, C.2    Sun, Y.-L.3
  • 52
    • 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. (2007) Fluorescence spectroscopy and birefringence of molecular changes in maturing rat tail tendon. J. Biomed. Opt. 12, 024011-024011.
    • (2007) J. Biomed. Opt. , vol.12 , pp. 024011-024011
    • Korol, R.M.1    Finlay, H.M.2    Josseau, M.J.3    Lucas, A.R.4    Canham, P.B.5
  • 53
    • 79954504506 scopus 로고    scopus 로고
    • Altered synthesis of cartilage-specific proteoglycans by mutant human cartilage oligomeric matrix protein
    • Kwak Y.H., Roh J.Y., Lee K.S., Park H.W., Kim H.W. (2009) Altered synthesis of cartilage-specific proteoglycans by mutant human cartilage oligomeric matrix protein. Clin. Orthop. Surg. 1, 181-187.
    • (2009) Clin. Orthop. Surg. , vol.1 , pp. 181-187
    • Kwak, Y.H.1    Roh, J.Y.2    Lee, K.S.3    Park, H.W.4    Kim, H.W.5
  • 54
    • 84877719555 scopus 로고    scopus 로고
    • GAG depletion increases the stress relaxation response of tendon fascicles, but does not influence recovery
    • doi: 10.1016/j.actbio.2013.02.028. [Epub ahead of print].
    • Legerlotz K., Riley G.P., Screen H.R.C. (2013) GAG depletion increases the stress relaxation response of tendon fascicles, but does not influence recovery. Acta Biomater. doi: 10.1016/j.actbio.2013.02.028. [Epub ahead of print].
    • (2013) Acta Biomater.
    • Legerlotz, K.1    Riley, G.P.2    Screen, H.R.C.3
  • 55
    • 31044455698 scopus 로고    scopus 로고
    • In vivo mechanical properties of the human Achilles tendon during one-legged hopping
    • Lichtwark G.A. & Wilson A.M. (2005) In vivo mechanical properties of the human Achilles tendon during one-legged hopping. J. Exp. Biol. 208, 4715-4725.
    • (2005) J. Exp. Biol. , vol.208 , pp. 4715-4725
    • Lichtwark, G.A.1    Wilson, A.M.2
  • 56
    • 34247869558 scopus 로고    scopus 로고
    • Is Achilles tendon compliance optimised for maximum muscle efficiency during locomotion?
    • Lichtwark G.A. & Wilson A.M. (2007) Is Achilles tendon compliance optimised for maximum muscle efficiency during locomotion? J. Biomech. 40, 1768-1775.
    • (2007) J. Biomech. , vol.40 , pp. 1768-1775
    • Lichtwark, G.A.1    Wilson, A.M.2
  • 57
    • 0037041218 scopus 로고    scopus 로고
    • The viscoelastic basis for the tensile strength of elastin
    • Lillie M.A. & Gosline J.M. (2002) The viscoelastic basis for the tensile strength of elastin. Int. J. Biol. Macromol. 30, 119-127.
    • (2002) Int. J. Biol. Macromol. , vol.30 , pp. 119-127
    • Lillie, M.A.1    Gosline, J.M.2
  • 58
    • 0034646705 scopus 로고    scopus 로고
    • A cartilage oligomeric matrix protein mutation associated with pseudoachondroplasia changes the structural and functional properties of the type 3 domain
    • Maddox B.K., Mokashi A., Keene D.R., Bachinger H.P. (2000) A cartilage oligomeric matrix protein mutation associated with pseudoachondroplasia changes the structural and functional properties of the type 3 domain. J. Biol. Chem. 275, 11412-11417.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11412-11417
    • Maddox, B.K.1    Mokashi, A.2    Keene, D.R.3    Bachinger, H.P.4
  • 59
    • 20444493586 scopus 로고    scopus 로고
    • Risk factors for injury to the superficial digital flexor tendon and suspensory apparatus in Thoroughbred racehorses in New Zealand
    • Perkins N.R., Reid S.W.J., Morris R.S. (2005) Risk factors for injury to the superficial digital flexor tendon and suspensory apparatus in Thoroughbred racehorses in New Zealand. NZ Vet. J. 53, 184-192.
    • (2005) NZ Vet. J. , vol.53 , pp. 184-192
    • Perkins, N.R.1    Reid, S.W.J.2    Morris, R.S.3
  • 60
    • 77649322497 scopus 로고    scopus 로고
    • A mouse model offers novel insights into the myopathy and tendinopathy often associated with pseudoachondroplasia and multiple epiphyseal dysplasia
    • Pirog K.A., Jaka O., Katakura Y. et al. (2010) A mouse model offers novel insights into the myopathy and tendinopathy often associated with pseudoachondroplasia and multiple epiphyseal dysplasia. Hum. Mol. Genet. 19, 52-64.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 52-64
    • Pirog, K.A.1    Jaka, O.2    Katakura, Y.3
  • 61
    • 32544452057 scopus 로고    scopus 로고
    • Collagen fibril morphology and organization: implications for force transmission in ligament and tendon
    • Provenzano P.P. & Vanderby R. (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, R.2
  • 62
    • 77952690559 scopus 로고    scopus 로고
    • The shear modulus of connections between tendon fascicles. Proceedings of the Science and Technology for Humanity (TIC-STH), IEEE Toronto International Conference
    • Purslow P.P. (2009) The shear modulus of connections between tendon fascicles. Proceedings of the Science and Technology for Humanity (TIC-STH), IEEE Toronto International Conference, pp. 134-136.
    • (2009) , pp. 134-136
    • Purslow, P.P.1
  • 63
    • 0141788733 scopus 로고    scopus 로고
    • Possible role of decorin glycosaminoglycans in fibril to 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. (2003) Possible role of decorin glycosaminoglycans in fibril to fibril force transfer in relative mature tendons-a computational study from molecular to microstructural level. J. Biomech. 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
  • 65
    • 0036860501 scopus 로고    scopus 로고
    • Immunolocalisation and expression of proteoglycan 4 (cartilage superficial zone proteoglycan) in tendon
    • Rees S.G., Davies J.R., Tudor D. et al. (2002) Immunolocalisation and expression of proteoglycan 4 (cartilage superficial zone proteoglycan) in tendon. Matrix Biol. 21, 593-602.
    • (2002) Matrix Biol. , vol.21 , pp. 593-602
    • Rees, S.G.1    Davies, J.R.2    Tudor, D.3
  • 66
    • 67649472791 scopus 로고    scopus 로고
    • Local strain measurement reveals a varied regional dependence of tensile tendon mechanics on glycosaminoglycan content
    • Rigozzi S., Muller R., Snedeker J.G. (2009) Local strain measurement reveals a varied regional dependence of tensile tendon mechanics on glycosaminoglycan content. J. Biomech. 42, 1547-1552.
    • (2009) J. Biomech. , vol.42 , pp. 1547-1552
    • Rigozzi, S.1    Muller, R.2    Snedeker, J.G.3
  • 67
    • 84879883969 scopus 로고    scopus 로고
    • Tendon glycosaminoglycan proteoglycan sidechains promote collagen fibril sliding-AFM observations at the nanoscale
    • Rigozzi S., Müller R., Stemmer A., Snedeker J.G. (2013) Tendon glycosaminoglycan proteoglycan sidechains promote collagen fibril sliding-AFM observations at the nanoscale. J. Biomech., 46, 813-818.
    • (2013) J. Biomech. , vol.46 , pp. 813-818
    • Rigozzi, S.1    Müller, R.2    Stemmer, A.3    Snedeker, J.G.4
  • 68
    • 1242274622 scopus 로고    scopus 로고
    • The pathogenesis of tendinopathy. A molecular perspective
    • Riley G. (2004) The pathogenesis of tendinopathy. A molecular perspective. Rheumatology (Oxford) 43, 131-142.
    • (2004) Rheumatology (Oxford) , vol.43 , pp. 131-142
    • Riley, G.1
  • 69
    • 0028278497 scopus 로고
    • Glycosaminoglycans of human rotator cuff tendons: changes with age and in chronic rotator cuff tendinitis
    • Riley G.P., Harrall R.L., Constant C.R., Chard M.D., Cawston T.E., Hazleman B.L. (1994a) Glycosaminoglycans of human rotator cuff tendons: changes with age and in chronic rotator cuff tendinitis. Ann. Rheum. Dis. 53, 367-376.
    • (1994) Ann. Rheum. Dis. , vol.53 , pp. 367-376
    • Riley, G.P.1    Harrall, R.L.2    Constant, C.R.3    Chard, M.D.4    Cawston, T.E.5    Hazleman, B.L.6
  • 70
    • 0028243182 scopus 로고
    • Tendon degeneration and chronic shoulder pain: changes in the collagen composition of the human rotator cuff tendons in rotator cuff tendinitis
    • Riley G.P., Harrall R.L., Constant C.R., Chard M.D., Cawston T.E., Hazleman B.L. (1994b) Tendon degeneration and chronic shoulder pain: changes in the collagen composition of the human rotator cuff tendons in rotator cuff tendinitis. Ann. Rheum. Dis. 53, 359-366.
    • (1994) Ann. Rheum. Dis. , vol.53 , pp. 359-366
    • Riley, G.P.1    Harrall, R.L.2    Constant, C.R.3    Chard, M.D.4    Cawston, T.E.5    Hazleman, B.L.6
  • 72
    • 0036892222 scopus 로고    scopus 로고
    • Distribution of the elastic fiber and associated proteins in flexor tendon reflects function
    • Ritty T.M., Ditsios K., Starcher B.C. (2002) Distribution of the elastic fiber and associated proteins in flexor tendon reflects function. Anat. Rec. 268, 430-440.
    • (2002) Anat. Rec. , vol.268 , pp. 430-440
    • Ritty, T.M.1    Ditsios, K.2    Starcher, B.C.3
  • 73
    • 0041833720 scopus 로고    scopus 로고
    • Tendon cell array isolation reveals a previously unknown fibrillin-2-containing macromolecular assembly
    • Ritty T.M., Roth R., Heuser J.E. (2003) Tendon cell array isolation reveals a previously unknown fibrillin-2-containing macromolecular assembly. Structure 11, 1179-1188.
    • (2003) Structure , vol.11 , pp. 1179-1188
    • Ritty, T.M.1    Roth, R.2    Heuser, J.E.3
  • 74
    • 79251502375 scopus 로고    scopus 로고
    • Flexible mechanisms: the diverse roles of biological springs in vertebrate movement
    • Roberts T.J. & Azizi E. (2011) Flexible mechanisms: the diverse roles of biological springs in vertebrate movement. J. Exp. Biol. 214, 353-361.
    • (2011) J. Exp. Biol. , vol.214 , pp. 353-361
    • Roberts, T.J.1    Azizi, E.2
  • 75
    • 2442517329 scopus 로고    scopus 로고
    • Strain-rate 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., Soslowsky L.J. (2004) Strain-rate 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
  • 76
    • 16244403925 scopus 로고    scopus 로고
    • Influence of decorin and biglycan on mechanical properties of multiple tendons in knockout mice
    • Robinson P.S., Huang T.F., Kazam E., Iozzo R.V., Birk D.E., Soslowsky L.J. (2005) Influence of decorin and biglycan on mechanical properties of multiple tendons in knockout mice. J. Biomech. Eng. 127, 181-185.
    • (2005) J. Biomech. Eng. , vol.127 , pp. 181-185
    • Robinson, P.S.1    Huang, T.F.2    Kazam, E.3    Iozzo, R.V.4    Birk, D.E.5    Soslowsky, L.J.6
  • 77
    • 0032493665 scopus 로고    scopus 로고
    • Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen
    • Rosenberg K., Olsson H., Morgelin M., Heinegard D. (1998) Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen. J. Biol. Chem. 273, 20397-20403.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20397-20403
    • Rosenberg, K.1    Olsson, H.2    Morgelin, M.3    Heinegard, D.4
  • 78
    • 3042713511 scopus 로고    scopus 로고
    • Characterisation of proteoglycans and their catabolic products in tendon and explant cultures of tendon
    • Samiric T., Ilic M.Z., Handley C.J. (2004) Characterisation of proteoglycans and their catabolic products in tendon and explant cultures of tendon. Matrix Biol. 23, 127-140.
    • (2004) Matrix Biol. , vol.23 , pp. 127-140
    • Samiric, T.1    Ilic, M.Z.2    Handley, C.J.3
  • 80
    • 0030016013 scopus 로고    scopus 로고
    • Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen
    • Scott J.E. (1996) Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen. Biochemistry 35, 8795-8799.
    • (1996) Biochemistry , vol.35 , pp. 8795-8799
    • Scott, J.E.1
  • 82
    • 24644492943 scopus 로고    scopus 로고
    • Cyclic tensile strain upregulates collagen synthesis in isolated tendon fascicles
    • Screen H.R.C., Shelton J.C., Bader D.L., Lee D.A. (2005) Cyclic tensile strain upregulates collagen synthesis in isolated tendon fascicles. Biochem. Biophys. Res. Commun. 336, 424-429.
    • (2005) Biochem. Biophys. Res. Commun. , vol.336 , pp. 424-429
    • Screen, H.R.C.1    Shelton, J.C.2    Bader, D.L.3    Lee, D.A.4
  • 83
    • 0028875704 scopus 로고
    • Type VI collagen in mouse masseter tendon, from osseous attachment to myotendinous junction
    • Senga K., Kobayashi M., Hattori H. et al. (1995) Type VI collagen in mouse masseter tendon, from osseous attachment to myotendinous junction. Anat. Rec. 243, 294-302.
    • (1995) Anat. Rec. , vol.243 , pp. 294-302
    • Senga, K.1    Kobayashi, M.2    Hattori, H.3
  • 84
    • 84987486560 scopus 로고
    • IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN). Nomenclature of glycoproteins, glycopeptides and peptidoglycans. Recommendations 1985
    • Sharon N. (1986) IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN). Nomenclature of glycoproteins, glycopeptides and peptidoglycans. Recommendations 1985. Eur. J. Biochem. 159, 1-6.
    • (1986) Eur. J. Biochem. , vol.159 , pp. 1-6
    • Sharon, N.1
  • 85
    • 33748765254 scopus 로고    scopus 로고
    • Scleraxis positively regulates the expression of tenomodulin, a differentiation marker of tenocytes
    • Shukunami C., Takimoto A., Oro M., Hiraki Y. (2006) Scleraxis positively regulates the expression of tenomodulin, a differentiation marker of tenocytes. Dev. Biol. 298, 234-247.
    • (2006) Dev. Biol. , vol.298 , pp. 234-247
    • Shukunami, C.1    Takimoto, A.2    Oro, M.3    Hiraki, Y.4
  • 86
    • 0141453852 scopus 로고    scopus 로고
    • Collagen self-assembly and the development of tendon mechanical properties
    • Silver F.H., Freeman J.W., 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
  • 87
    • 0031282595 scopus 로고    scopus 로고
    • The distribution of cartilage oligomeric matrix protein (COMP) in tendon and its variation with tendon site, age and load
    • Smith R.K., Zunino L., Webbon P.M., Heinegard D. (1997) The distribution of cartilage oligomeric matrix protein (COMP) in tendon and its variation with tendon site, age and load. Matrix Biol. 16, 255-271.
    • (1997) Matrix Biol. , vol.16 , pp. 255-271
    • Smith, R.K.1    Zunino, L.2    Webbon, P.M.3    Heinegard, D.4
  • 88
    • 6444245091 scopus 로고    scopus 로고
    • The influence of ageing and exercise on tendon growth and degeneration-hypotheses for the initiation and prevention of strain-induced tendinopathies
    • Smith R.K., Birch H.L., Goodman S., Heinegard D., Goodship A.E. (2002a) The influence of ageing and exercise on tendon growth and degeneration-hypotheses for the initiation and prevention of strain-induced tendinopathies. Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. 133, 1039-1050.
    • (2002) Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. , vol.133 , pp. 1039-1050
    • Smith, R.K.1    Birch, H.L.2    Goodman, S.3    Heinegard, D.4    Goodship, A.E.5
  • 89
    • 0036728312 scopus 로고    scopus 로고
    • Correlation of cartilage oligomeric matrix protein (COMP) levels in equine tendon with mechanical properties: a proposed role for COMP in determining function-specific mechanical characteristics of locomotor tendons
    • Smith R.K., Gerard M., Dowling B., Dart A.J., Birch H.L., Goodship A.E. (2002b) Correlation of cartilage oligomeric matrix protein (COMP) levels in equine tendon with mechanical properties: a proposed role for COMP in determining function-specific mechanical characteristics of locomotor tendons. Equine Vet. J. Suppl. 241-244.
    • (2002) Equine Vet. J. Suppl. , pp. 241-244
    • Smith, R.K.1    Gerard, M.2    Dowling, B.3    Dart, A.J.4    Birch, H.L.5    Goodship, A.E.6
  • 91
    • 70449713611 scopus 로고    scopus 로고
    • Functional fibered confocal microscopy: a promising tool for assessing tendon regeneration
    • Snedeker J.G., Ben Arav A., Zilberman Y., Pelled G., Gazit D. (2009a) Functional fibered confocal microscopy: a promising tool for assessing tendon regeneration. Tissue Eng. Part C Methods 15, 485-491.
    • (2009) Tissue Eng. Part C Methods , vol.15 , pp. 485-491
    • Snedeker, J.G.1    Ben Arav, A.2    Zilberman, Y.3    Pelled, G.4    Gazit, D.5
  • 92
    • 67651102589 scopus 로고    scopus 로고
    • An analytical model for elucidating tendon tissue structure and biomechanical function from in vivo cellular confocal microscopy images
    • Snedeker J.G., Pelled G., Zilberman Y. et al. (2009b) An analytical model for elucidating tendon tissue structure and biomechanical function from in vivo cellular confocal microscopy images. Cells Tissues Organs 190, 111-119.
    • (2009) Cells Tissues Organs , vol.190 , pp. 111-119
    • Snedeker, J.G.1    Pelled, G.2    Zilberman, Y.3
  • 93
    • 22544435541 scopus 로고    scopus 로고
    • Ultrastructural immunolocalization of cartilage oligomeric matrix protein (COMP) in relation to collagen fibrils in the equine tendon
    • Sodersten F., Ekman S., Eloranta M.L., Heinegard D., Dudhia J., Hultenby K. (2005) Ultrastructural immunolocalization of cartilage oligomeric matrix protein (COMP) in relation to collagen fibrils in the equine tendon. Matrix Biol. 24, 376-385.
    • (2005) Matrix Biol. , vol.24 , pp. 376-385
    • Sodersten, F.1    Ekman, S.2    Eloranta, M.L.3    Heinegard, D.4    Dudhia, J.5    Hultenby, K.6
  • 94
    • 84872136816 scopus 로고    scopus 로고
    • Immunolocalization of collagens (I and III) and cartilage oligomeric matrix protein (COMP) in the normal and injured equine superficial digital flexor tendon
    • Sodersten F., Hultenby K., Heinegard D., Johnston C., Ekman S. (2013) Immunolocalization of collagens (I and III) and cartilage oligomeric matrix protein (COMP) in the normal and injured equine superficial digital flexor tendon. Connect. Tissue Res. 54, 62-69.
    • (2013) Connect. Tissue Res. , vol.54 , pp. 62-69
    • Sodersten, F.1    Hultenby, K.2    Heinegard, D.3    Johnston, C.4    Ekman, S.5
  • 95
    • 46249124038 scopus 로고    scopus 로고
    • Electron microscopy of collagen fibril structure in vitro and in vivo including three-dimensional reconstruction
    • Starborg T., Lu Y., Kadler K.E., Holmes D.F. (2008) Electron microscopy of collagen fibril structure in vitro and in vivo including three-dimensional reconstruction. Methods Cell Biol. 88, 319-345.
    • (2008) Methods Cell Biol. , vol.88 , pp. 319-345
    • Starborg, T.1    Lu, Y.2    Kadler, K.E.3    Holmes, D.F.4
  • 96
    • 0024697022 scopus 로고
    • Application of a Hall-effect transducer for measurement of tendon strains in horses
    • Stephens P.R., Nunamaker D.M., Butterweck D.M. (1989) Application of a Hall-effect transducer for measurement of tendon strains in horses. Am. J. Vet. Res. 50, 1089-1095.
    • (1989) Am. J. Vet. Res. , vol.50 , pp. 1089-1095
    • Stephens, P.R.1    Nunamaker, D.M.2    Butterweck, D.M.3
  • 98
  • 99
    • 0036264997 scopus 로고    scopus 로고
    • Cartilage oligomeric matrix protein-deficient mice have normal skeletal development
    • Svensson L., Aszodi A., Heinegard D. et al. (2002) Cartilage oligomeric matrix protein-deficient mice have normal skeletal development. Mol. Cell. Biol. 22, 4366-4371.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4366-4371
    • Svensson, L.1    Aszodi, A.2    Heinegard, D.3
  • 100
    • 80052742678 scopus 로고    scopus 로고
    • Tensile force transmission in human patellar tendon fascicles is not mediated by glycosaminoglycans
    • Svensson R.B., Hassenkam T., Hansen P., Kjaer M., Magnusson S.P. (2011) Tensile force transmission in human patellar tendon fascicles is not mediated by glycosaminoglycans. Connect. Tissue Res. 52, 415-421.
    • (2011) Connect. Tissue Res. , vol.52 , pp. 415-421
    • Svensson, R.B.1    Hassenkam, T.2    Hansen, P.3    Kjaer, M.4    Magnusson, S.P.5
  • 101
    • 0019796599 scopus 로고
    • The molecular structure of lubricating glycoprotein-I, the boundary lubricant for articular cartilage
    • Swann D.A., Slayter H.S., Silver F.H. (1981) The molecular structure of lubricating glycoprotein-I, the boundary lubricant for articular cartilage. J. Biol. Chem. 256, 5921-5925.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5921-5925
    • Swann, D.A.1    Slayter, H.S.2    Silver, F.H.3
  • 102
    • 51049121850 scopus 로고    scopus 로고
    • Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates
    • Sweeney S.M., Orgel J.P., Fertala A. et al. (2008) Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates. J. Biol. Chem. 283, 21187-21197.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21187-21197
    • Sweeney, S.M.1    Orgel, J.P.2    Fertala, A.3
  • 103
    • 37849003847 scopus 로고    scopus 로고
    • Lubricin surface modification improves extrasynovial tendon gliding in a Canine model in vitro
    • Taguchi M., Sun Y.-L., Zhao C. et al. (2008) Lubricin surface modification improves extrasynovial tendon gliding in a Canine model in vitro. J. Bone Joint Surg. Am. 90, 129-135.
    • (2008) J. Bone Joint Surg. Am. , vol.90 , pp. 129-135
    • Taguchi, M.1    Sun, Y.-L.2    Zhao, C.3
  • 104
    • 59449094033 scopus 로고    scopus 로고
    • Lubricin surface modification improves tendon gliding after tendon repair in a canine model in vitro
    • Taguchi M., Sun Y.-L., Zhao C. et al. (2009) Lubricin surface modification improves tendon gliding after tendon repair in a canine model in vitro. J. Orthop. Res. 27, 257-263.
    • (2009) J. Orthop. Res. , vol.27 , pp. 257-263
    • Taguchi, M.1    Sun, Y.-L.2    Zhao, C.3
  • 106
    • 77049106836 scopus 로고    scopus 로고
    • A review of tendon injury: why is the equine superficial digital flexor tendon most at risk?
    • Thorpe C.T., Clegg P.D., Birch H.L. (2010a) A review of tendon injury: why is the equine superficial digital flexor tendon most at risk? Equine Vet. J. 42, 174-180.
    • (2010) Equine Vet. J. , vol.42 , pp. 174-180
    • Thorpe, C.T.1    Clegg, P.D.2    Birch, H.L.3
  • 107
    • 77952409743 scopus 로고    scopus 로고
    • Aspartic acid racemization and collagen degradation markers reveal an accumulation of damage in tendon collagen that is enhanced with aging
    • Thorpe C.T., Streeter I., Pinchbeck G.L., Goodship A.E., Clegg P.D., Birch H.L. (2010b) Aspartic acid racemization and collagen degradation markers reveal an accumulation of damage in tendon collagen that is enhanced with aging. J. Biol. Chem. 285, 15674-15681.
    • (2010) J. Biol. Chem. , vol.285 , pp. 15674-15681
    • Thorpe, C.T.1    Streeter, I.2    Pinchbeck, G.L.3    Goodship, A.E.4    Clegg, P.D.5    Birch, H.L.6
  • 108
    • 84867466160 scopus 로고    scopus 로고
    • Specialization of tendon mechanical properties results from interfascicular differences
    • Thorpe C.T., Udeze C.P., Birch H.L., Clegg P.D., Screen H.R.C. (2012) Specialization of tendon mechanical properties results from interfascicular differences. J. R. Soc. Interface 9, 3108-3117.
    • (2012) J. R. Soc. Interface , vol.9 , pp. 3108-3117
    • Thorpe, C.T.1    Udeze, C.P.2    Birch, H.L.3    Clegg, P.D.4    Screen, H.R.C.5
  • 109
    • 84878423070 scopus 로고    scopus 로고
    • Capacity for sliding between tendon fascicles decreases with ageing in injury prone equine tendons: a possible mechanism for age-related tendinopathy?
    • Thorpe C.T., Udeze C.P., Birch H.L., Clegg P.D., Screen H.R.C. (2013) Capacity for sliding between tendon fascicles decreases with ageing in injury prone equine tendons: a possible mechanism for age-related tendinopathy? Eur. Cell. Mater. 25, 48-60.
    • (2013) Eur. Cell. Mater. , vol.25 , pp. 48-60
    • Thorpe, C.T.1    Udeze, C.P.2    Birch, H.L.3    Clegg, P.D.4    Screen, H.R.C.5
  • 110
    • 0021840012 scopus 로고
    • Patellar tendon matrix changes associated with aging and voluntary exercise
    • Vailas A.C., Pedrini V.A., Pedrini-Mille A., Holloszy J.O. (1985) Patellar tendon matrix changes associated with aging and voluntary exercise. J. Appl. Physiol. 58, 1572-1576.
    • (1985) J. Appl. Physiol. , vol.58 , pp. 1572-1576
    • Vailas, A.C.1    Pedrini, V.A.2    Pedrini-Mille, A.3    Holloszy, J.O.4
  • 111
    • 12344287057 scopus 로고    scopus 로고
    • Estimation of the binding force of the collagen molecule-decorin core protein complex in collagen fibril
    • Vesentini S., Redaelli A., Montevecchi F.M. (2005) Estimation of the binding force of the collagen molecule-decorin core protein complex in collagen fibril. J. Biomech. 38, 433-443.
    • (2005) J. Biomech. , vol.38 , pp. 433-443
    • Vesentini, S.1    Redaelli, A.2    Montevecchi, F.M.3
  • 112
    • 0019293421 scopus 로고
    • Influence of maturation and aging on mechanical and biochemical properties of connective tissue in rats
    • Vogel H.G. (1980) Influence of maturation and aging on mechanical and biochemical properties of connective tissue in rats. Mech. Ageing Dev. 14, 283-292.
    • (1980) Mech. Ageing Dev. , vol.14 , pp. 283-292
    • Vogel, H.G.1
  • 113
    • 84857034827 scopus 로고    scopus 로고
    • Murine tendon function is adversely affected by aggrecan accumulation due to the knockout of ADAMTS5
    • Wang V.M., Bell R.M., Thakore R. et al. (2012) Murine tendon function is adversely affected by aggrecan accumulation due to the knockout of ADAMTS5. J. Orthop. Res. 30, 620-626.
    • (2012) J. Orthop. Res. , vol.30 , pp. 620-626
    • Wang, V.M.1    Bell, R.M.2    Thakore, R.3
  • 114
    • 0029778529 scopus 로고    scopus 로고
    • Model structure of decorin and implications for collagen fibrillogenesis
    • Weber I.T., Harrison R.W., Iozzo R.V. (1996) Model structure of decorin and implications for collagen fibrillogenesis. J. Biol. Chem. 271, 31767-31770.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31767-31770
    • Weber, I.T.1    Harrison, R.W.2    Iozzo, R.V.3
  • 115
    • 0035378666 scopus 로고    scopus 로고
    • Biglycan and decorin bind close to the N-terminal region of the collagen VI triple helix
    • Wiberg C., Hedbom E., Khairullina A. et al. (2001) Biglycan and decorin bind close to the N-terminal region of the collagen VI triple helix. J. Biol. Chem. 276, 18947-18952.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18947-18952
    • Wiberg, C.1    Hedbom, E.2    Khairullina, A.3
  • 116
    • 0036775241 scopus 로고    scopus 로고
    • Versican: a versatile extracellular matrix proteoglycan in cell biology
    • Wight T.N. (2002) Versican: a versatile extracellular matrix proteoglycan in cell biology. Curr. Opin. Cell Biol. 14, 617-623.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 617-623
    • Wight, T.N.1
  • 117
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner J.F. (1991) Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5, 2145-2154.
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner, J.F.1
  • 118
    • 44149125624 scopus 로고    scopus 로고
    • Tendon creep is potentiated by NKISK and relaxin which produce collagen fiber sliding
    • Wood M.L., Luthin W.N., Lester G.E., Dahners L.E. (2003) Tendon creep is potentiated by NKISK and relaxin which produce collagen fiber sliding. Iowa Orthop. J. 23, 75-79.
    • (2003) Iowa Orthop. J. , vol.23 , pp. 75-79
    • Wood, M.L.1    Luthin, W.N.2    Lester, G.E.3    Dahners, L.E.4
  • 120
    • 18744385300 scopus 로고    scopus 로고
    • Development of tendon structure and function: regulation of collagen fibrillogenesis
    • Zhang G., Young B.B., Ezura Y. et al. (2005) Development of tendon structure and function: regulation of collagen fibrillogenesis. J. Musculoskelet. Neuronal Interact. 5, 5-21.
    • (2005) J. Musculoskelet. Neuronal Interact. , vol.5 , pp. 5-21
    • Zhang, G.1    Young, B.B.2    Ezura, Y.3
  • 121
    • 33746536017 scopus 로고    scopus 로고
    • Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon development
    • Zhang G., Ezura Y., Chervoneva I. et al. (2006) Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon development. J. Cell. Biochem. 98, 1436-1449.
    • (2006) J. Cell. Biochem. , vol.98 , pp. 1436-1449
    • Zhang, G.1    Ezura, Y.2    Chervoneva, I.3


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