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Volumn 6, Issue , 2015, Pages

Osmotic pressure induced tensile forces in tendon collagen

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; MACROGOL; WATER;

EID: 84928331740     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6942     Document Type: Article
Times cited : (181)

References (44)
  • 1
    • 32844466504 scopus 로고    scopus 로고
    • Evidence that collagen and tendon have monolayer water coverage in the native state
    • Fullerton, G. D. & Amurao, M. R. Evidence that collagen and tendon have monolayer water coverage in the native state. Cell Biol. Int. 30, 56-65 (2006).
    • (2006) Cell Biol. Int. , vol.30 , pp. 56-65
    • Fullerton, G.D.1    Amurao, M.R.2
  • 2
    • 33748365032 scopus 로고    scopus 로고
    • X-ray diffraction study into the effects of liming on the structure of collagen
    • Maxwell, C. A., Wess, T. J. & Kennedy, C. J. X-ray diffraction study into the effects of liming on the structure of collagen. Biomacromolecules 7, 2321-2326 (2006).
    • (2006) Biomacromolecules , vol.7 , pp. 2321-2326
    • Maxwell, C.A.1    Wess, T.J.2    Kennedy, C.J.3
  • 4
    • 0029645406 scopus 로고
    • Hydration structure of a collagen peptide
    • Bella, J., Brodsky, B. & Berman, H. Hydration structure of a collagen peptide. Structure. 3, 893-906 (1995).
    • (1995) Structure. , vol.3 , pp. 893-906
    • Bella, J.1    Brodsky, B.2    Berman, H.3
  • 5
    • 0034731219 scopus 로고    scopus 로고
    • Changes in collagen structure: Drying, dehydrothermal treatment and relation to long term deterioration
    • Wess, T. J. & Orgel, J. P. Changes in collagen structure: drying, dehydrothermal treatment and relation to long term deterioration. Thermochim. Acta 365, 119-128 (2000).
    • (2000) Thermochim. Acta , vol.365 , pp. 119-128
    • Wess, T.J.1    Orgel, J.P.2
  • 6
    • 60949107887 scopus 로고    scopus 로고
    • Deformation and failure of protein materials in physiologically extreme conditions and disease
    • Buehler, M. J. & Yung, Y. C. Deformation and failure of protein materials in physiologically extreme conditions and disease. Nat. Mater. 8, 175-188 (2009).
    • (2009) Nat. Mater. , vol.8 , pp. 175-188
    • Buehler, M.J.1    Yung, Y.C.2
  • 7
    • 38349102440 scopus 로고    scopus 로고
    • The role of kinetics of water and amide bonding in protein stability
    • Porter, D. & Vollrath, F. The role of kinetics of water and amide bonding in protein stability. Soft Matter 4, 328-336 (2008).
    • (2008) Soft Matter , vol.4 , pp. 328-336
    • Porter, D.1    Vollrath, F.2
  • 8
    • 0001113489 scopus 로고
    • Subunit model for tropocollagen macromolecule
    • Petruska, J. A. & Hodge, A. J. Subunit model for tropocollagen macromolecule. Proc. Natl Acad. Sci. USA 51, 871-876 (1964).
    • (1964) Proc. Natl Acad. Sci. USA , vol.51 , pp. 871-876
    • Petruska, J.A.1    Hodge, A.J.2
  • 9
    • 0031686056 scopus 로고    scopus 로고
    • Fibrillar structure and mechanical properties of collagen
    • Fratzl, P. et al. Fibrillar structure and mechanical properties of collagen. J. Struct. Biol. 122, 119-122 (1998).
    • (1998) J. Struct. Biol. , vol.122 , pp. 119-122
    • Fratzl, P.1
  • 11
    • 0018400235 scopus 로고
    • Chain conformation in the collagen molecule
    • Fraser, R. D. B., MacRae, T. P. & Suzuki, E. Chain conformation in the collagen molecule. J. Mol. Biol. 129, 463-481 (1979).
    • (1979) J. Mol. Biol. , vol.129 , pp. 463-481
    • Fraser, R.D.B.1    MacRae, T.P.2    Suzuki, E.3
  • 12
    • 0030935291 scopus 로고    scopus 로고
    • X-ray diffraction analysis of tendon collagen at ambient and cryogenic temperatures: Role of hydration
    • Price, R. I., Lees, S. & Kirschner, D. A. X-ray diffraction analysis of tendon collagen at ambient and cryogenic temperatures: role of hydration. Int. J. Biol. Macromol. 20, 23-33 (1997).
    • (1997) Int. J. Biol. Macromol. , vol.20 , pp. 23-33
    • Price, R.I.1    Lees, S.2    Kirschner, D.A.3
  • 13
    • 34548501731 scopus 로고    scopus 로고
    • Nature's hierarchical materials
    • Fratzl, P. & Weinkamer, R. Nature's hierarchical materials. Prog. Mater. Sci. 52, 1263-1334 (2007).
    • (2007) Prog. Mater. Sci. , vol.52 , pp. 1263-1334
    • Fratzl, P.1    Weinkamer, R.2
  • 14
    • 0030246115 scopus 로고    scopus 로고
    • Elongation mechanism of collagen fibrils and forcestrain relations of tendon at each level of structural hierarchy
    • Sasaki, N. & Odajim, a, S. Elongation mechanism of collagen fibrils and forcestrain relations of tendon at each level of structural hierarchy. J. Biomech. 29, 1131-1136 (1996).
    • (1996) J. Biomech. , vol.29 , pp. 1131-1136
    • Sasaki, N.1    Odajim, A.S.2
  • 15
    • 0037185947 scopus 로고    scopus 로고
    • Viscoelastic properties of collagen: Synchrotron radiation investigations and structural model
    • Puxkandl, R. et al. Viscoelastic properties of collagen: synchrotron radiation investigations and structural model. Phil. Trans. R. Soc. Lond B Biol. Sci. 357, 191-197 (2002).
    • (2002) Phil. Trans. R. Soc. Lond B Biol. Sci. , vol.357 , pp. 191-197
    • Puxkandl, R.1
  • 16
    • 0031041821 scopus 로고    scopus 로고
    • A new molecular model for collagen elasticity based on synchrotron X-ray scattering evidence
    • Misof, K., Rapp, G. & Fratzl, P. A new molecular model for collagen elasticity based on synchrotron X-ray scattering evidence. Biophys. J. 72, 1376-1381 (1997).
    • (1997) Biophys. J. , vol.72 , pp. 1376-1381
    • Misof, K.1    Rapp, G.2    Fratzl, P.3
  • 17
    • 74849088007 scopus 로고    scopus 로고
    • In situ multilevel analysis of viscoelastic deformation mechanisms in tendon collagen
    • Gupta, H. S., Seto, J., Krauss, S., Boesecke, P. & Screen, H. R. C. In situ multilevel analysis of viscoelastic deformation mechanisms in tendon collagen. J. Struct. Biol. 169, 183-191 (2009).
    • (2009) J. Struct. Biol. , vol.169 , pp. 183-191
    • Gupta, H.S.1    Seto, J.2    Krauss, S.3    Boesecke, P.4    Screen, H.R.C.5
  • 18
    • 33747610222 scopus 로고    scopus 로고
    • Nature designs tough collagen: Explaining the nanostructure of collagen fibrils
    • Buehler, M. J. Nature designs tough collagen: explaining the nanostructure of collagen fibrils. Proc. Natl Acad. Sci. USA 103, 12285-12290 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 12285-12290
    • Buehler, M.J.1
  • 19
    • 81255171882 scopus 로고    scopus 로고
    • Observations of multiscale, stress-induced changes of collagen orientation in tendon by polarized Raman spectroscopy
    • Masic, A. et al. Observations of multiscale, stress-induced changes of collagen orientation in tendon by polarized Raman spectroscopy. Biomacromolecules 12, 3989-3996 (2011).
    • (2011) Biomacromolecules , vol.12 , pp. 3989-3996
    • Masic, A.1
  • 20
    • 0017329109 scopus 로고
    • Interpretation of the meridional diffraction pattern from collagen fibres in terms of the known amino acid sequence
    • Hulmes, D. J. S., Miller, A., White, S. W. & Brodsky-Doyle, B. Interpretation of the meridional diffraction pattern from collagen fibres in terms of the known amino acid sequence. J. Mol. Biol. 110, 643-666 (1977).
    • (1977) J. Mol. Biol. , vol.110 , pp. 643-666
    • Hulmes, D.J.S.1    Miller, A.2    White, S.W.3    Brodsky-Doyle, B.4
  • 21
    • 0006442511 scopus 로고
    • Low-angle X-ray diffraction pattern of collagen
    • Wright, B. A. Low-angle X-ray diffraction pattern of collagen. Nature 162, 23-23 (1948).
    • (1948) Nature , vol.162 , pp. 23
    • Wright, B.A.1
  • 22
    • 79851488199 scopus 로고    scopus 로고
    • Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up
    • Gautieri, A., Vesentini, S., Redaelli, A. & Buehler, M. J. Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up. Nano Lett. 11, 757-766 (2011).
    • (2011) Nano Lett. , vol.11 , pp. 757-766
    • Gautieri, A.1    Vesentini, S.2    Redaelli, A.3    Buehler, M.J.4
  • 23
    • 0013905011 scopus 로고
    • Variation in isometric tension with sarcomere length in vertebrate muscle fibres
    • Gordon, A. M., Huxley, A. F. & Julian, F. J. Variation in isometric tension with sarcomere length in vertebrate muscle fibres. J Physiol. 184, 170-192 (1966).
    • (1966) J Physiol. , vol.184 , pp. 170-192
    • Gordon, A.M.1    Huxley, A.F.2    Julian, F.J.3
  • 24
    • 84886191047 scopus 로고    scopus 로고
    • ed. Fratzl, P. Springer Science & Business Media
    • Wess, T. J. in Collagen: Structure and Mechanics (ed. Fratzl, P.) (Springer Science & Business Media, 2008).
    • (2008) Collagen: Structure and Mechanics
    • Wess, T.J.1
  • 25
    • 34347403503 scopus 로고    scopus 로고
    • Entropic elasticity controls nanomechanics of single tropocollagen molecules
    • Buehler, M. J. & Wong, S. Y. Entropic elasticity controls nanomechanics of single tropocollagen molecules. Biophys. J. 93, 37-43 (2007).
    • (2007) Biophys. J. , vol.93 , pp. 37-43
    • Buehler, M.J.1    Wong, S.Y.2
  • 26
    • 35648954122 scopus 로고    scopus 로고
    • Force-induced unfolding of fibronectin in the extracellular matrix of living cells
    • Smith, M. L. et al. Force-induced unfolding of fibronectin in the extracellular matrix of living cells. PLoS Biol. 5, e268 (2007).
    • (2007) PLoS Biol. , vol.5 , pp. e268
    • Smith, M.L.1
  • 27
    • 0027475398 scopus 로고
    • Collagen packing and mineralization-an X-ray scattering investigation of Turkey leg tendon
    • Fratzl, P., Fratzl-Zelman, N. & Klaushofer, K. Collagen packing and mineralization-an X-ray scattering investigation of Turkey leg tendon. Biophys. J. 64, 260-266 (1993).
    • (1993) Biophys. J. , vol.64 , pp. 260-266
    • Fratzl, P.1    Fratzl-Zelman, N.2    Klaushofer, K.3
  • 28
    • 56349098272 scopus 로고    scopus 로고
    • Revisiting the molecular structure of collagen
    • Okuyama, K. Revisiting the molecular structure of collagen. Conn. Tissue Res 49, 299-310 (2008).
    • (2008) Conn. Tissue Res , vol.49 , pp. 299-310
    • Okuyama, K.1
  • 29
    • 34548489679 scopus 로고    scopus 로고
    • The variability in type i collagen helical pitch is reflected in the D periodic fibrillar structure
    • Cameron, G. J., Cairns, D. E. & Wess, T. J. The variability in type I collagen helical pitch is reflected in the D periodic fibrillar structure. J. Mol. Biol. 372, 1097-1107 (2007).
    • (2007) J. Mol. Biol. , vol.372 , pp. 1097-1107
    • Cameron, G.J.1    Cairns, D.E.2    Wess, T.J.3
  • 30
    • 84877761020 scopus 로고    scopus 로고
    • Polarized raman anisotropic response of collagen in tendon: Towards 3D orientation mapping of collagen in tissues
    • Galvis, L., Dunlop, J. W. C., Duda, G., Fratzl, P. & Masic, A. Polarized raman anisotropic response of collagen in tendon: Towards 3D orientation mapping of collagen in tissues. PLoS ONE 8, e63518 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e63518
    • Galvis, L.1    Dunlop, J.W.C.2    Duda, G.3    Fratzl, P.4    Masic, A.5
  • 31
    • 0026827330 scopus 로고
    • A 13C NMR study on collagens in the solid state: Hydration/dehydration-induced conformational change of collagen and detection of internal motions
    • Saito, H. & Yokoi, M. A 13C NMR study on collagens in the solid state: hydration/dehydration-induced conformational change of collagen and detection of internal motions. J. Biochem. 111, 376-382 (1992).
    • (1992) J. Biochem , vol.111 , pp. 376-382
    • Saito, H.1    Yokoi, M.2
  • 32
    • 0032320412 scopus 로고    scopus 로고
    • The osmotic pressure of chondroitin sulphate solutions: Experimental measurements and theoretical analysis
    • Ehrlich, S. et al. The osmotic pressure of chondroitin sulphate solutions: experimental measurements and theoretical analysis. Biorheology 35, 383-397 (1998).
    • (1998) Biorheology , vol.35 , pp. 383-397
    • Ehrlich, S.1
  • 33
    • 0029130871 scopus 로고
    • Macromolecules and water: Probing with osmotic stress
    • Parsegian, V. A., Rand, R. P. & Rau, D. C. Macromolecules and water: probing with osmotic stress. Methods Enzymol. 259, 43-94 (1995).
    • (1995) Methods Enzymol. , vol.259 , pp. 43-94
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 34
    • 77956396107 scopus 로고    scopus 로고
    • Effect of sulfated glycosaminoglycan digestion on the transverse permeability of medial collateral ligament
    • Henninger, H. B., Underwood, C. J., Ateshian, G. A. & Weiss, J. A. Effect of sulfated glycosaminoglycan digestion on the transverse permeability of medial collateral ligament. J. Biomech. 43, 2567-2573 (2010).
    • (2010) J. Biomech. , vol.43 , pp. 2567-2573
    • Henninger, H.B.1    Underwood, C.J.2    Ateshian, G.A.3    Weiss, J.A.4
  • 35
    • 77951975120 scopus 로고    scopus 로고
    • Micromechanical models of helical superstructures in ligament and tendon fibers predict large Poisson's ratios
    • Reese, S. P., Maas, S. A. & Weiss, J. A. Micromechanical models of helical superstructures in ligament and tendon fibers predict large Poisson's ratios. J. Biomech. 43, 1394-1400 (2010).
    • (2010) J. Biomech. , vol.43 , pp. 1394-1400
    • Reese, S.P.1    Maas, S.A.2    Weiss, J.A.3
  • 36
    • 0014929614 scopus 로고
    • Mechanochemical turbine: A new power cycle
    • Sussman, M. V. & Katchalsky, A. Mechanochemical turbine: A new power cycle. Science 167, 45-47 (1970).
    • (1970) Science , vol.167 , pp. 45-47
    • Sussman, M.V.1    Katchalsky, A.2
  • 38
    • 0022429081 scopus 로고
    • Neutron diffraction studies of collagen in fully mineralized bone
    • Bonar, L. C., Lees, S. & Mook, H. A. Neutron diffraction studies of collagen in fully mineralized bone. J. Mol. Biol. 181, 265-270 (1985).
    • (1985) J. Mol. Biol. , vol.181 , pp. 265-270
    • Bonar, L.C.1    Lees, S.2    Mook, H.A.3
  • 39
    • 79957775953 scopus 로고    scopus 로고
    • Cooperation of length scales and orientations in the deformation of bovine bone
    • Hoo, R. P. et al. Cooperation of length scales and orientations in the deformation of bovine bone. Acta Biomater. 7, 2943-2951 (2011).
    • (2011) Acta Biomater. , vol.7 , pp. 2943-2951
    • Hoo, R.P.1
  • 40
    • 25644432877 scopus 로고    scopus 로고
    • Internal strains and stresses measured in cortical bone via high-energy X-ray diffraction
    • Almer, J. D. & Stock, S. R. Internal strains and stresses measured in cortical bone via high-energy X-ray diffraction. J. Struct. Biol. 152, 14-27 (2005).
    • (2005) J. Struct. Biol. , vol.152 , pp. 14-27
    • Almer, J.D.1    Stock, S.R.2
  • 41
    • 77953024895 scopus 로고    scopus 로고
    • On the effect of X-ray irradiation on the deformation and fracture behavior of human cortical bone
    • Barth, H. D., Launey, M. E., MacDowell, A. A., Ager, III J. W. & Ritchie, R. O. On the effect of X-ray irradiation on the deformation and fracture behavior of human cortical bone. Bone 46, 1475-1485 (2010).
    • (2010) Bone , vol.46 , pp. 1475-1485
    • Barth, H.D.1    Launey, M.E.2    MacDowell, A.A.3    Ager, J.W.4    Ritchie, R.O.5
  • 44
    • 84863012650 scopus 로고    scopus 로고
    • Structural and mechanical differences between collagen homo-and heterotrimers: Relevance for the molecular origin of brittle bone disease
    • Chang, S. W., Shefelbine, S. J. & Buehler, M. J. Structural and mechanical differences between collagen homo-and heterotrimers: relevance for the molecular origin of brittle bone disease. Biophys. J. 102, 640-648 (2012).
    • (2012) Biophys. J. , vol.102 , pp. 640-648
    • Chang, S.W.1    Shefelbine, S.J.2    Buehler, M.J.3


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