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Volumn 26, Issue 7, 2008, Pages 971-976

Effect of NKISK on tendon lengthening: An in vivo model for various clinically applicable dosing regimens

Author keywords

Decorin; Fibril sliding; NKISK; Tendon creep; Tendon lengthening

Indexed keywords

ASPARAGINYLLYSYLISOLEUCYLSERYLLYSINE; GLUTAMINYLLYSYLTHREONYLSERYLLYSINE; PENTAPEPTIDE; PHOSPHATE BUFFERED SALINE; UNCLASSIFIED DRUG; NKISK PEPTIDE; OLIGOPEPTIDE;

EID: 46449105265     PISSN: 07360266     EISSN: None     Source Type: Journal    
DOI: 10.1002/jor.20594     Document Type: Article
Times cited : (5)

References (20)
  • 1
    • 0034232649 scopus 로고    scopus 로고
    • The pentapeptide NKISK affects collagen fibril interactions in a vertebrate tissue
    • Dahners LE, Lester GE, Caprise P.2000. The pentapeptide NKISK affects collagen fibril interactions in a vertebrate tissue. J Orthop Res 18:532-536.
    • (2000) J Orthop Res , vol.18 , pp. 532-536
    • Dahners, L.E.1    Lester, G.E.2    Caprise, P.3
  • 3
    • 0035010291 scopus 로고    scopus 로고
    • Suppression of fibrous adhesion by proteoglycan decorin
    • Fukui N, Fukuda A, Kojima K, et al. 2001. Suppression of fibrous adhesion by proteoglycan decorin. J Orthop Res 19: 456-462.
    • (2001) J Orthop Res , vol.19 , pp. 456-462
    • Fukui, N.1    Fukuda, A.2    Kojima, K.3
  • 4
    • 0027717615 scopus 로고
    • Binding of fibromodulin and decorin to separate sites on fibrillar collagens
    • Hedbom E, Heinegard D. 1993. Binding of fibromodulin and decorin to separate sites on fibrillar collagens. J Biol Chem 268:27307-27312.
    • (1993) J Biol Chem , vol.268 , pp. 27307-27312
    • Hedbom, E.1    Heinegard, D.2
  • 5
    • 0034253758 scopus 로고    scopus 로고
    • Tip-mediated fusion involving unipolar collagen fibrils accounts for rapid fibril elongation, the occurrence of fibrillar branched networks in skin and the paucity of collagen fibril ends in vertebrates
    • Kadler KE, Holmes DF, Graham H, et al. 2000. Tip-mediated fusion involving unipolar collagen fibrils accounts for rapid fibril elongation, the occurrence of fibrillar branched networks in skin and the paucity of collagen fibril ends in vertebrates. Matrix Biol 19:359-365.
    • (2000) Matrix Biol , vol.19 , pp. 359-365
    • Kadler, K.E.1    Holmes, D.F.2    Graham, H.3
  • 7
    • 0001365841 scopus 로고    scopus 로고
    • Small polycations facilitate strain through collagen fibril sliding
    • Overcash JS, Hickman JH, Lester GE, et al. 1998. Small polycations facilitate strain through collagen fibril sliding. Trans Orthop Res Soc 23:611.
    • (1998) Trans Orthop Res Soc , vol.23 , pp. 611
    • Overcash, J.S.1    Hickman, J.H.2    Lester, G.E.3
  • 9
    • 0032124584 scopus 로고    scopus 로고
    • Collagen fiber sliding during ligament growth and contracture
    • Wood ML, Lester GA, Dahners LE. 1998. Collagen fiber sliding during ligament growth and contracture. J Orthop Res 16:438-440.
    • (1998) J Orthop Res , vol.16 , pp. 438-440
    • Wood, M.L.1    Lester, G.A.2    Dahners, L.E.3
  • 10
    • 0028923480 scopus 로고
    • Collagen fibril-logenesis in situ: Fibril segments undergo post-depositional modifications resulting in linear and lateral growth during matrix development
    • Birk DE, Nurminskaya MV, Zycband EI. 1995. Collagen fibril-logenesis 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
  • 11
    • 0034858556 scopus 로고    scopus 로고
    • The effect of NKISK on tendon in an in vivo model
    • Caprise PA, Lester GE, Weinhold P, et al. 2001. The effect of NKISK on tendon in an in vivo model. J Orthop Res 19:858-861.
    • (2001) J Orthop Res , vol.19 , pp. 858-861
    • Caprise, P.A.1    Lester, G.E.2    Weinhold, P.3
  • 12
    • 0024389687 scopus 로고
    • Collagen and proteoglycan in a sea urchin ligament with mutable mechanical properties
    • Trotter JA, Koob T. 1989. Collagen and proteoglycan in a sea urchin ligament with mutable mechanical properties. Cell Tissue Res 258:527-539.
    • (1989) Cell Tissue Res , vol.258 , pp. 527-539
    • Trotter, J.A.1    Koob, T.2
  • 13
    • 0025954786 scopus 로고
    • Interaction of the small proteoglycan decorin with fibronectin
    • Schmidt G, Hausser H, Kresse H. 1991. Interaction of the small proteoglycan decorin with fibronectin. J Biochem 280: 411-414.
    • (1991) J Biochem , vol.280 , pp. 411-414
    • Schmidt, G.1    Hausser, H.2    Kresse, H.3
  • 14
    • 0020600448 scopus 로고
    • Fine structure and mechanical properties of the catch apparatus of the sea-urchin spine, a collagenous connective tissue with muscle-like holding capacity
    • Hidaka M, Takahashi K. 1983. Fine structure and mechanical properties of the catch apparatus of the sea-urchin spine, a collagenous connective tissue with muscle-like holding capacity. J Exp Biol 103:1-14.
    • (1983) J Exp Biol , vol.103 , pp. 1-14
    • Hidaka, M.1    Takahashi, K.2
  • 15
    • 0028915521 scopus 로고
    • Decorin-type I collagen interaction. Presence of separate core protein-binding domains
    • Schonherr E, Hausser H, Beavan L, et al. 1995. Decorin-type I collagen interaction. Presence of separate core protein-binding domains. J Biol Chem 270:8877-8883.
    • (1995) J Biol Chem , vol.270 , pp. 8877-8883
    • Schonherr, E.1    Hausser, H.2    Beavan, L.3
  • 16
    • 52449101178 scopus 로고    scopus 로고
    • Takahashi K. 1967. The catch apparatus of the sea-urchin spine. I. Gross histology. J Fac Sci Univ Tokyo, Sec IV 11: 109-120.
    • Takahashi K. 1967. The catch apparatus of the sea-urchin spine. I. Gross histology. J Fac Sci Univ Tokyo, Sec IV 11: 109-120.
  • 17
    • 0034698179 scopus 로고    scopus 로고
    • Decorin binds near the C terminus of type I collagen
    • Keene DR, San Antonio JD, Mayne R, et al. 2000. Decorin binds near the C terminus of type I collagen. J Biol Chem 275:21801-21804.
    • (2000) J Biol Chem , vol.275 , pp. 21801-21804
    • Keene, D.R.1    San Antonio, J.D.2    Mayne, R.3
  • 18
    • 0034232654 scopus 로고    scopus 로고
    • Decorin antisense gene therapy improves functional healing of early rabbit ligament scar with enhanced collagen fibrillogenesis in vivo
    • Nakamura N, Hart DA, Boorman RS, et al. 2000. Decorin antisense gene therapy improves functional healing of early rabbit ligament scar with enhanced collagen fibrillogenesis in vivo. J Orthop Res 18:517-523.
    • (2000) J Orthop Res , vol.18 , pp. 517-523
    • Nakamura, N.1    Hart, D.A.2    Boorman, R.S.3
  • 19
    • 0030875449 scopus 로고    scopus 로고
    • Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin and mechanical properties
    • Pins GD, Christiansen DL, Patel R, et al. 1997. Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin and 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
  • 20
    • 0028158454 scopus 로고
    • Vertebrate (chick) collagen fibrils formed in vivo can exhibit a reversal in molecular polarity
    • Holmes DF, Lowe MP, Chapman JA. 1994. Vertebrate (chick) collagen fibrils formed in vivo can exhibit a reversal in molecular polarity. J Mol Biol 235:80-83.
    • (1994) J Mol Biol , vol.235 , pp. 80-83
    • Holmes, D.F.1    Lowe, M.P.2    Chapman, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.