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Volumn 94, Issue 3, 2008, Pages 717-725

A structural, kinetic model of soft tissue thermomechanics

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN FIBRIL;

EID: 38549117293     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.111716     Document Type: Article
Times cited : (13)

References (58)
  • 1
    • 0344629717 scopus 로고    scopus 로고
    • Thermal capsular shrinkage for treatment of multidirectional instability of the shoulder
    • Miniaci, A., and J. McBirnie. 2003. Thermal capsular shrinkage for treatment of multidirectional instability of the shoulder. J. Bone Joint Surg. Am. 85-A:2283-2287.
    • (2003) J. Bone Joint Surg. Am , vol.85-A , pp. 2283-2287
    • Miniaci, A.1    McBirnie, J.2
  • 2
    • 0035221011 scopus 로고    scopus 로고
    • Electrothermal shrinkage reduces laxity but alters creep behavior in a lapine ligament model
    • Wallace, A. L., R. M. Hollinshead, and C. B. Frank. 2001. Electrothermal shrinkage reduces laxity but alters creep behavior in a lapine ligament model. J. Shoulder Elbow Surg. 10:1-6.
    • (2001) J. Shoulder Elbow Surg , vol.10 , pp. 1-6
    • Wallace, A.L.1    Hollinshead, R.M.2    Frank, C.B.3
  • 3
    • 25444529699 scopus 로고    scopus 로고
    • Thermal modification of the lax anterior cruciate ligament using radiofrequency: Efficacy or catastrophe?
    • Lubowitz, J. H. 2005. Thermal modification of the lax anterior cruciate ligament using radiofrequency: efficacy or catastrophe? Knee Surg. Sports Traumatol. Arthrosc. 13:432-436.
    • (2005) Knee Surg. Sports Traumatol. Arthrosc , vol.13 , pp. 432-436
    • Lubowitz, J.H.1
  • 4
    • 0034030776 scopus 로고    scopus 로고
    • Influence of temperature and time on thermally induced forces in corneal collagen and the effect on laser thermokeratoplasty
    • Brinkmann, R., B. Radt, C. Flamm, J. Kampmeier, N. Koop, and R. Birngruber. 2000. Influence of temperature and time on thermally induced forces in corneal collagen and the effect on laser thermokeratoplasty. J. Cataract Refract. Surg. 26:744-754.
    • (2000) J. Cataract Refract. Surg , vol.26 , pp. 744-754
    • Brinkmann, R.1    Radt, B.2    Flamm, C.3    Kampmeier, J.4    Koop, N.5    Birngruber, R.6
  • 5
    • 0031693244 scopus 로고    scopus 로고
    • Collagen thermal damage and collagen synthesis after cutaneous laser resurfacing
    • Kuo, T., M. T. Speyer, W. R. Ries, and L. Reinisch. 1998. Collagen thermal damage and collagen synthesis after cutaneous laser resurfacing. Lasers Surg. Med. 23:66-71.
    • (1998) Lasers Surg. Med , vol.23 , pp. 66-71
    • Kuo, T.1    Speyer, M.T.2    Ries, W.R.3    Reinisch, L.4
  • 6
    • 0036405394 scopus 로고    scopus 로고
    • Denaturation of collagen via heating: An irreversible rate process
    • Wright, N. T., and J. D. Humphrey. 2002. Denaturation of collagen via heating: an irreversible rate process. Annu. Rev. Biomed. Eng. 4:109-128.
    • (2002) Annu. Rev. Biomed. Eng , vol.4 , pp. 109-128
    • Wright, N.T.1    Humphrey, J.D.2
  • 7
    • 0034263909 scopus 로고    scopus 로고
    • Thermal modification of connective tissues: Basic science considerations and clinical implications
    • Arnoczky, S. P., and A. Aksan. 2000. Thermal modification of connective tissues: basic science considerations and clinical implications. J. Am. Acad. Orthop. Surg. 8:305-313.
    • (2000) J. Am. Acad. Orthop. Surg , vol.8 , pp. 305-313
    • Arnoczky, S.P.1    Aksan, A.2
  • 9
    • 0027376116 scopus 로고
    • Kinetics of collagen denaturation in mammalian lens capsules studied by differential scanning calorimetry
    • Miles, C. A. 1993. Kinetics of collagen denaturation in mammalian lens capsules studied by differential scanning calorimetry. Int. J. Biol. Macromol. 15:265-271.
    • (1993) Int. J. Biol. Macromol , vol.15 , pp. 265-271
    • Miles, C.A.1
  • 10
    • 0028918983 scopus 로고
    • The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry
    • Miles, C. A., T. V. Burjanadze, and A. J. Bailey. 1995. The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry. J. Mol. Biol. 245:437-446.
    • (1995) J. Mol. Biol , vol.245 , pp. 437-446
    • Miles, C.A.1    Burjanadze, T.V.2    Bailey, A.J.3
  • 11
    • 0027213859 scopus 로고
    • Kinetic models of laser-tissue fusion processes
    • Pearce, J. A., and S. Thomsen. 1993. Kinetic models of laser-tissue fusion processes. Biomed. Sci. Instrum. 29:355-360.
    • (1993) Biomed. Sci. Instrum , vol.29 , pp. 355-360
    • Pearce, J.A.1    Thomsen, S.2
  • 12
    • 33749051927 scopus 로고    scopus 로고
    • Thermal stability of proteins
    • Bischof, J. C., and X. He. 2006. Thermal stability of proteins. Ann. N. Y. Acad. Sci. 1066:12-33.
    • (2006) Ann. N. Y. Acad. Sci , vol.1066 , pp. 12-33
    • Bischof, J.C.1    He, X.2
  • 13
    • 0142169846 scopus 로고    scopus 로고
    • Thermomechanical analysis of soft-tissue thermotherapy
    • Aksan, A., and J. J. McGrath. 2003. Thermomechanical analysis of soft-tissue thermotherapy. J. Biomech. Eng. 125:700-708.
    • (2003) J. Biomech. Eng , vol.125 , pp. 700-708
    • Aksan, A.1    McGrath, J.J.2
  • 14
    • 0032103901 scopus 로고    scopus 로고
    • Heat-induced changes in the mechanics of a collagenous tissue: Isothermal, isotonic shrinkage
    • Chen, S. S., N. T. Wright, and J. D. Humphrey. 1998. Heat-induced changes in the mechanics of a collagenous tissue: isothermal, isotonic shrinkage. J. Biomech. Eng. 120:382-388.
    • (1998) J. Biomech. Eng , vol.120 , pp. 382-388
    • Chen, S.S.1    Wright, N.T.2    Humphrey, J.D.3
  • 15
    • 0038374173 scopus 로고    scopus 로고
    • Altered mechanical behavior of epicardium due to isothermal heating under biaxial isotonic loads
    • Harris, J. L., P. B. Wells, and J. D. Humphrey. 2003. Altered mechanical behavior of epicardium due to isothermal heating under biaxial isotonic loads. J. Biomech. Eng. 125:381-388.
    • (2003) J. Biomech. Eng , vol.125 , pp. 381-388
    • Harris, J.L.1    Wells, P.B.2    Humphrey, J.D.3
  • 16
    • 0024831978 scopus 로고
    • Changes in birefringence as markers of thermal damage in tissues
    • Thomsen, S., J. A. Pearce, and W. F. Cheong. 1989. Changes in birefringence as markers of thermal damage in tissues. IEEE Trans. Biomed. Eng. 36:1174-1179.
    • (1989) IEEE Trans. Biomed. Eng , vol.36 , pp. 1174-1179
    • Thomsen, S.1    Pearce, J.A.2    Cheong, W.F.3
  • 17
    • 0015509381 scopus 로고
    • Aging of collagen in complex tissues. A micromethodological study of the thermal reaction
    • Viidik, A. 1972. Aging of collagen in complex tissues. A micromethodological study of the thermal reaction. Experientia. 28:641-642.
    • (1972) Experientia , vol.28 , pp. 641-642
    • Viidik, A.1
  • 18
    • 0032190595 scopus 로고    scopus 로고
    • Phenomenological evolution equations for heat-induced shrinkage of a collagenous tissue
    • Chen, S. S., N. T. Wright, and J. D. Humphrey. 1998. Phenomenological evolution equations for heat-induced shrinkage of a collagenous tissue. IEEE Trans. Biomed. Eng. 45:1234-1240.
    • (1998) IEEE Trans. Biomed. Eng , vol.45 , pp. 1234-1240
    • Chen, S.S.1    Wright, N.T.2    Humphrey, J.D.3
  • 19
    • 0019436410 scopus 로고
    • Thermal stability of reconstituted collagen fibrils. Shrinkage characteristics upon in vitro maturation
    • Danielsen, C. C. 1981. Thermal stability of reconstituted collagen fibrils. Shrinkage characteristics upon in vitro maturation. Mech. Ageing Dev. 15:269-278.
    • (1981) Mech. Ageing Dev , vol.15 , pp. 269-278
    • Danielsen, C.C.1
  • 21
    • 0035452722 scopus 로고    scopus 로고
    • A mixture theory for heat-induced alterations in hydration and mechanical properties in soft tissues
    • Tao, L., J. D. Humphrey, and K. R. Rajagopal. 2001. A mixture theory for heat-induced alterations in hydration and mechanical properties in soft tissues. Int. J. Eng. Sci. 39:1535-1556.
    • (2001) Int. J. Eng. Sci , vol.39 , pp. 1535-1556
    • Tao, L.1    Humphrey, J.D.2    Rajagopal, K.R.3
  • 22
    • 3342993179 scopus 로고    scopus 로고
    • Atomic force microscopy: Mechanical unfolding of proteins
    • Rounsevell, R., J. R. Forman, and J. Clarke. 2004. Atomic force microscopy: mechanical unfolding of proteins. Methods. 34:100-111.
    • (2004) Methods , vol.34 , pp. 100-111
    • Rounsevell, R.1    Forman, J.R.2    Clarke, J.3
  • 23
    • 33646192682 scopus 로고    scopus 로고
    • A coarse-grained model for force-induced protein deformation and kinetics
    • Karcher, H., S. E. Lee, M. R. Kaazempur-Mofrad, and R. D. Kamm. 2006. A coarse-grained model for force-induced protein deformation and kinetics. Biophys. J. 90:2686-2697.
    • (2006) Biophys. J , vol.90 , pp. 2686-2697
    • Karcher, H.1    Lee, S.E.2    Kaazempur-Mofrad, M.R.3    Kamm, R.D.4
  • 24
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell, G. I. 1978. Models for the specific adhesion of cells to cells. Science. 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 25
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E., and K. Ritchie. 1997. Dynamic strength of molecular adhesion bonds. Biophys. J. 72:1541-1555.
    • (1997) Biophys. J , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 27
  • 28
    • 0036064087 scopus 로고    scopus 로고
    • Direct quantification of the flexibility of type I collagen monomer
    • Sun, Y. L., Z. P. Luo, A. Fertala, and K. N. An. 2002. Direct quantification of the flexibility of type I collagen monomer. Biochem. Biophys. Res. Commun. 295:382-386.
    • (2002) Biochem. Biophys. Res. Commun , vol.295 , pp. 382-386
    • Sun, Y.L.1    Luo, Z.P.2    Fertala, A.3    An, K.N.4
  • 29
    • 22244448651 scopus 로고    scopus 로고
    • Topography and mechanical properties of single molecules of type I collagen using atomic force microscopy
    • Bozec, L., and M. Horton. 2005. Topography and mechanical properties of single molecules of type I collagen using atomic force microscopy. Biophys. J. 88:4223-4231.
    • (2005) Biophys. J , vol.88 , pp. 4223-4231
    • Bozec, L.1    Horton, M.2
  • 30
    • 0033804203 scopus 로고    scopus 로고
    • Biaxial mechanical properties of the native and glutaraldehyde-treated aortic valve cusp: Part II - A structural constitutive model
    • Billiar, K. L., and M. S. Sacks. 2000. Biaxial mechanical properties of the native and glutaraldehyde-treated aortic valve cusp: Part II - A structural constitutive model. J. Biomech. Eng. 122:327-335.
    • (2000) J. Biomech. Eng , vol.122 , pp. 327-335
    • Billiar, K.L.1    Sacks, M.S.2
  • 31
    • 34248166980 scopus 로고    scopus 로고
    • Volume-averaging theory for the study of the mechanics of collagen networks
    • Stylianopoulos, T., and V. H. Barocas. 2007. Volume-averaging theory for the study of the mechanics of collagen networks. Comput. Methods Appl. Mech. Eng. 196:2981-2990.
    • (2007) Comput. Methods Appl. Mech. Eng , vol.196 , pp. 2981-2990
    • Stylianopoulos, T.1    Barocas, V.H.2
  • 32
    • 34548288437 scopus 로고    scopus 로고
    • Multiscale, structure-based modeling for the elastic mechanical behavior of arterial walls
    • Stylianopoulos, T., and V. H. Barocas. 2007. Multiscale, structure-based modeling for the elastic mechanical behavior of arterial walls. J. Biomech. Eng. 129:611-618.
    • (2007) J. Biomech. Eng , vol.129 , pp. 611-618
    • Stylianopoulos, T.1    Barocas, V.H.2
  • 35
    • 0031282039 scopus 로고    scopus 로고
    • Heat-induced changes in the mechanics of a collagenous tissue: Isothermal free shrinkage
    • Chen, S. S., N. T. Wright, and J. D. Humphrey. 1997. Heat-induced changes in the mechanics of a collagenous tissue: isothermal free shrinkage. J. Biomech. Eng. 119:372-378.
    • (1997) J. Biomech. Eng , vol.119 , pp. 372-378
    • Chen, S.S.1    Wright, N.T.2    Humphrey, J.D.3
  • 36
    • 0020545965 scopus 로고
    • Molecular conformation and packing in collagen fibrils
    • Fraser, R. D., T. P. MacRae, A. Miller, and E. Suzuki. 1983. Molecular conformation and packing in collagen fibrils. J. Mol. Biol. 167:497-521.
    • (1983) J. Mol. Biol , vol.167 , pp. 497-521
    • Fraser, R.D.1    MacRae, T.P.2    Miller, A.3    Suzuki, E.4
  • 37
    • 0032536160 scopus 로고    scopus 로고
    • Molecular packing of type I collagen in tendon
    • Wess, T. J., A. P. Hammersley, L. Wess, and A. Miller. 1998. Molecular packing of type I collagen in tendon. J. Mol. Biol. 275:255-267.
    • (1998) J. Mol. Biol , vol.275 , pp. 255-267
    • Wess, T.J.1    Hammersley, A.P.2    Wess, L.3    Miller, A.4
  • 38
    • 0034526523 scopus 로고    scopus 로고
    • How is a tissue built?
    • Cowin, S. C. 2000. How is a tissue built? J. Biomech. Eng. 122:553-569.
    • (2000) J. Biomech. Eng , vol.122 , pp. 553-569
    • Cowin, S.C.1
  • 39
    • 25844517949 scopus 로고    scopus 로고
    • Computational modeling of type I collagen fibers to determine the extracellular matrix structure of connective tissues
    • Israelowitz, M., S. W. Rizvi, J. Kramer, and H. P. von Schroeder. 2005. Computational modeling of type I collagen fibers to determine the extracellular matrix structure of connective tissues. Protein Eng. Des. Sel. 18:329-335.
    • (2005) Protein Eng. Des. Sel , vol.18 , pp. 329-335
    • Israelowitz, M.1    Rizvi, S.W.2    Kramer, J.3    von Schroeder, H.P.4
  • 40
    • 0030152813 scopus 로고    scopus 로고
    • Stress-strain curve and Young's modulus of a collagen molecule as determined by the X-ray diffraction technique
    • Sasaki, N., and S. Odajima. 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
    • Sasaki, N.1    Odajima, S.2
  • 41
    • 0022586967 scopus 로고
    • Water content in type I collagen tissues calculated from the generalized packing model
    • Lees, S. 1985. Water content in type I collagen tissues calculated from the generalized packing model. Int. J. Biol. Macromol. 8:66-72.
    • (1985) Int. J. Biol. Macromol , vol.8 , pp. 66-72
    • Lees, S.1
  • 43
    • 84984821750 scopus 로고
    • Studies of thermal injury: V. The predictability and the significance of thermally induced rate processes leading to irreversible epidermal injury
    • Henriques, F. C. J. 1947. Studies of thermal injury: V. The predictability and the significance of thermally induced rate processes leading to irreversible epidermal injury. Arch. Pathol. 43:489-502.
    • (1947) Arch. Pathol , vol.43 , pp. 489-502
    • Henriques, F.C.J.1
  • 44
    • 19744370421 scopus 로고    scopus 로고
    • Elastic properties, Young's modulus determination and structural stability of the tropocollagen molecule: A computational study by steered molecular dynamics
    • Lorenzo, A. C., and E. R. Caffarena. 2005. Elastic properties, Young's modulus determination and structural stability of the tropocollagen molecule: a computational study by steered molecular dynamics. J. Biomech. 38:1527-1533.
    • (2005) J. Biomech , vol.38 , pp. 1527-1533
    • Lorenzo, A.C.1    Caffarena, E.R.2
  • 45
    • 0035170791 scopus 로고    scopus 로고
    • Viscoelasticity of the vessel wall: The role of collagen and elastic fibers
    • Silver, F. H., I. Horvath, and D. J. Foran. 2001. Viscoelasticity of the vessel wall: the role of collagen and elastic fibers. Crit. Rev. Biomed. Eng. 29:279-301.
    • (2001) Crit. Rev. Biomed. Eng , vol.29 , pp. 279-301
    • Silver, F.H.1    Horvath, I.2    Foran, D.J.3
  • 46
    • 33645765218 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin
    • Brujic, J., R. I. Hermans, K. A. Walther, and J. M. Fernandez. 2006. Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin. Nature Physics. 2:282-286.
    • (2006) Nature Physics , vol.2 , pp. 282-286
    • Brujic, J.1    Hermans, R.I.2    Walther, K.A.3    Fernandez, J.M.4
  • 48
    • 0028910961 scopus 로고
    • Radial packing, order, and disorder in collagen fibrils
    • Hulmes, D. J., T. J. Wess, D. J. Prockop, and P. Fratzl. 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.1    Wess, T.J.2    Prockop, D.J.3    Fratzl, P.4
  • 49
    • 33747610222 scopus 로고    scopus 로고
    • Nature designs tough collagen: Explaining the nanostructure of collagen fibrils
    • Buehler, M. J. 2006. Nature designs tough collagen: explaining the nanostructure of collagen fibrils. Proc. Natl. Acad. Sci. USA. 103:12285-12290.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12285-12290
    • Buehler, M.J.1
  • 50
    • 0028078724 scopus 로고
    • Direct measurement of forces between self-assembled proteins: Temperature-dependent exponential forces between collagen triple helices
    • Leikin, S., D. C. Rau, and V. A. Parsegian. 1994. Direct measurement of forces between self-assembled proteins: temperature-dependent exponential forces between collagen triple helices. Proc. Natl. Acad. Sci. USA. 91:276-280.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 276-280
    • Leikin, S.1    Rau, D.C.2    Parsegian, V.A.3
  • 51
    • 0031020875 scopus 로고    scopus 로고
    • Solvent hydrogen-bond network in protein self-assembly: Solvation of collagen triple helices in nonaqueous solvents
    • Kuznetsova, N., D. C. Rau, V. A. Parsegian, and S. Leikin. 1997. Solvent hydrogen-bond network in protein self-assembly: solvation of collagen triple helices in nonaqueous solvents. Biophys. J. 72:353-362.
    • (1997) Biophys. J , vol.72 , pp. 353-362
    • Kuznetsova, N.1    Rau, D.C.2    Parsegian, V.A.3    Leikin, S.4
  • 52
    • 0031578633 scopus 로고    scopus 로고
    • Heat-induced changes in the mechanics of a collagenous tissue: Pseudoelastic behavior at 37°C
    • Chen, S. S., and J. D. Humphrey. 1998. Heat-induced changes in the mechanics of a collagenous tissue: pseudoelastic behavior at 37°C. J. Biomech. 31:211-216.
    • (1998) J. Biomech , vol.31 , pp. 211-216
    • Chen, S.S.1    Humphrey, J.D.2
  • 53
    • 28344439954 scopus 로고    scopus 로고
    • Histological evidence for the role of mechanical stress in modulating thermal denaturation of collagen
    • Wells, P. B., S. Thomsen, M. A. Jones, S. Baek, and J. D. Humphrey. 2005. Histological evidence for the role of mechanical stress in modulating thermal denaturation of collagen. Biomech. Model. Mechanobiol. 4:201-210.
    • (2005) Biomech. Model. Mechanobiol , vol.4 , pp. 201-210
    • Wells, P.B.1    Thomsen, S.2    Jones, M.A.3    Baek, S.4    Humphrey, J.D.5
  • 54
    • 34547853938 scopus 로고    scopus 로고
    • Mechanical unfolding revisited through a simple but realistic model
    • West, D. K., P. D. Olmsted, and E. Paci. 2006. Mechanical unfolding revisited through a simple but realistic model. J. Chem. Phys. 124:1-8.
    • (2006) J. Chem. Phys , vol.124 , pp. 1-8
    • West, D.K.1    Olmsted, P.D.2    Paci, E.3
  • 55
    • 1842559515 scopus 로고    scopus 로고
    • Equilibrium thermal transitions of collagen model peptides
    • Persikov, A. V., Y. Xu, and B. Brodsky. 2004. Equilibrium thermal transitions of collagen model peptides. Protein Sci. 13:893-902.
    • (2004) Protein Sci , vol.13 , pp. 893-902
    • Persikov, A.V.1    Xu, Y.2    Brodsky, B.3
  • 57
    • 0033029015 scopus 로고    scopus 로고
    • Polymer-in-a-box mechanism for the thermal stabilization of collagen molecules in fibers
    • Miles, C. A., and M. Ghelashvili. 1999. Polymer-in-a-box mechanism for the thermal stabilization of collagen molecules in fibers. Biophys. J. 76:3243-3252.
    • (1999) Biophys. J , vol.76 , pp. 3243-3252
    • Miles, C.A.1    Ghelashvili, M.2
  • 58
    • 1642499406 scopus 로고    scopus 로고
    • Kinetics of thermal damage to a collagenous membrane under biaxial isotonic loading
    • Harris, J. L., and J. D. Humphrey. 2004. Kinetics of thermal damage to a collagenous membrane under biaxial isotonic loading. IEEE Trans. Biomed. Eng. 51:371-379.
    • (2004) IEEE Trans. Biomed. Eng , vol.51 , pp. 371-379
    • Harris, J.L.1    Humphrey, J.D.2


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