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Volumn 31, Issue 5, 2005, Pages 568-577

The relative thermal stability of tissue macromolecules and cellular structure in burn injury

Author keywords

Burn; Membrane poration; Model; Molecular stability; Protein denaturation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNA; FAT; PROTEIN; RNA;

EID: 21344472612     PISSN: 03054179     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.burns.2005.01.015     Document Type: Article
Times cited : (89)

References (45)
  • 1
    • 0038376295 scopus 로고    scopus 로고
    • Cellular effects of hyperthermia: Relevance to the minimum dose for thermal damage
    • J.R. Lepock Cellular effects of hyperthermia: relevance to the minimum dose for thermal damage Int J Hyperthermia 19 2003 252 266
    • (2003) Int J Hyperthermia , vol.19 , pp. 252-266
    • Lepock, J.R.1
  • 2
  • 4
    • 77957030185 scopus 로고
    • Modeling of bio-heat transfer process at high and low temperatures
    • K.R. Diller Modeling of bio-heat transfer process at high and low temperatures Adv Heat Transfer 22 1992 157 357
    • (1992) Adv Heat Transfer , vol.22 , pp. 157-357
    • Diller, K.R.1
  • 5
    • 0032764044 scopus 로고    scopus 로고
    • Issues in modeling thermal alterations in tissues
    • K.R. Diller, and J.A. Pearce Issues in modeling thermal alterations in tissues Ann N Y Acad Sci 888 1999 153 163
    • (1999) Ann N Y Acad Sci , vol.888 , pp. 153-163
    • Diller, K.R.1    Pearce, J.A.2
  • 6
    • 0030298439 scopus 로고    scopus 로고
    • The physico-chemical basis for thermal and non-thermal burn injury
    • R.C. Lee, and R.D. Astumian The physico-chemical basis for thermal and non-thermal burn injury Burns 22 1996 509 519
    • (1996) Burns , vol.22 , pp. 509-519
    • Lee, R.C.1    Astumian, R.D.2
  • 7
    • 0034575127 scopus 로고    scopus 로고
    • Biophysical injury mechanisms in electrical shock trauma
    • R.C. Lee, D. Zhang, and J. Hannig Biophysical injury mechanisms in electrical shock trauma Annu Rev Biomed Eng 2 2000 477 509
    • (2000) Annu Rev Biomed Eng , vol.2 , pp. 477-509
    • Lee, R.C.1    Zhang, D.2    Hannig, J.3
  • 8
    • 0031863873 scopus 로고    scopus 로고
    • A finite-element model predicts thermal damage in cutaneous contact burns
    • D.P. Orgill, M.G. Solari, M.S. Barlow, and N.E. O'Connor A finite-element model predicts thermal damage in cutaneous contact burns J Burn Care Rehabil 19 1998 203 209
    • (1998) J Burn Care Rehabil , vol.19 , pp. 203-209
    • Orgill, D.P.1    Solari, M.G.2    Barlow, M.S.3    O'Connor, N.E.4
  • 10
    • 0015409137 scopus 로고
    • Thermal noise in cells: A cause of spontaneous loss of cell junction
    • H.A. Johnson, and M. Pavalec Thermal noise in cells: a cause of spontaneous loss of cell junction Am J Pathol 69 1972 119 130
    • (1972) Am J Pathol , vol.69 , pp. 119-130
    • Johnson, H.A.1    Pavalec, M.2
  • 11
    • 0035829705 scopus 로고    scopus 로고
    • Inter-basin dynamics on multidimensional potential surfaces. I. Escape rates on complex basin surfaces
    • F. Despa, and R.S. Berry Inter-basin dynamics on multidimensional potential surfaces. I. Escape rates on complex basin surfaces J Chem Phys 115 2001 8274 9278
    • (2001) J Chem Phys , vol.115 , pp. 8274-9278
    • Despa, F.1    Berry, R.S.2
  • 12
    • 0042572488 scopus 로고    scopus 로고
    • Inter-basin dynamics on multidimensional potential surfaces, kinetic traps
    • F. Despa, and R.S. Berry Inter-basin dynamics on multidimensional potential surfaces, kinetic traps Eur Phys JD 24 2003 203 206
    • (2003) Eur Phys JD , vol.24 , pp. 203-206
    • Despa, F.1    Berry, R.S.2
  • 13
    • 0344951101 scopus 로고    scopus 로고
    • Inter-basin motion approach to dynamics of conformationally constrained peptides
    • F. Despa, A. Fernàndez, R.S. Berry, Y. Levy, and J. Jortner Inter-basin motion approach to dynamics of conformationally constrained peptides J Chem Phys 118 2003 5673 5682
    • (2003) J Chem Phys , vol.118 , pp. 5673-5682
    • Despa, F.1    Fernàndez, A.2    Berry, R.S.3    Levy, Y.4    Jortner, J.5
  • 14
    • 0034258186 scopus 로고    scopus 로고
    • Relaxation dynamics in the presence of unequally spaced attractors along the reaction coordinate
    • F. Despa, and R.S. Berry Relaxation dynamics in the presence of unequally spaced attractors along the reaction coordinate Eur Phys JD 16 2001 55 58
    • (2001) Eur Phys JD , vol.16 , pp. 55-58
    • Despa, F.1    Berry, R.S.2
  • 16
    • 0035576379 scopus 로고    scopus 로고
    • Free energy distributions in proteins
    • D. Poland Free energy distributions in proteins Proteins 45 2001 325 336
    • (2001) Proteins , vol.45 , pp. 325-336
    • Poland, D.1
  • 18
    • 23844453002 scopus 로고    scopus 로고
    • Effects on crowding on the thermal stability of heterogeneous protein solutions
    • submitted.
    • Despa F, Orgill DP, Lee RC. Effects on crowding on the thermal stability of heterogeneous protein solutions. Ann Biomed Eng; submitted.
    • Ann Biomed Eng
    • Despa, F.1    Orgill, D.P.2    Lee, R.C.3
  • 20
    • 0031000601 scopus 로고    scopus 로고
    • Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: Cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion
    • R. Swaminathan, C.P. Hoang, and A.S. Verkman Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion Biophys J 72 1997 1900 1907
    • (1997) Biophys J , vol.72 , pp. 1900-1907
    • Swaminathan, R.1    Hoang, C.P.2    Verkman, A.S.3
  • 21
    • 0041822089 scopus 로고    scopus 로고
    • Cell biology: Join the crowd
    • R.J. Ellis, and A.P. Minton Cell biology: join the crowd Nature 425 2003 27 28
    • (2003) Nature , vol.425 , pp. 27-28
    • Ellis, R.J.1    Minton, A.P.2
  • 22
    • 0034039755 scopus 로고    scopus 로고
    • Effect of a concentrated inert macromolecular cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: A statistical-thermodynamic model
    • A.P. Minton Effect of a concentrated inert macromolecular cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: a statistical-thermodynamic model Biophys J 78 2000 101 109
    • (2000) Biophys J , vol.78 , pp. 101-109
    • Minton, A.P.1
  • 23
    • 0035860681 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on the refolding of glucose-6phosphate dehydrogenase and protein disulfide isomerase
    • J. Li, S. Zhang, and C. Wang Effects of macromolecular crowding on the refolding of glucose-6phosphate dehydrogenase and protein disulfide isomerase J Biol Chem 37 2001 34396 34401
    • (2001) J Biol Chem , vol.37 , pp. 34396-34401
    • Li, J.1    Zhang, S.2    Wang, C.3
  • 24
    • 0020828094 scopus 로고
    • Influence of poly(ethylene glicol) 6000 on the properties of skeletal-muscle actin
    • R.L. Tellam, M.J. Sculley, L.V. Nichol, and P.R. Wills Influence of poly(ethylene glicol) 6000 on the properties of skeletal-muscle actin Biochem J 213 1983 651 659
    • (1983) Biochem J , vol.213 , pp. 651-659
    • Tellam, R.L.1    Sculley, M.J.2    Nichol, L.V.3    Wills, P.R.4
  • 25
    • 0035824871 scopus 로고    scopus 로고
    • Crowding and hydration effects on protein conformation: A study with sol-gel encapsulated proteins
    • D.K. Eggers, and J.S. Valentine Crowding and hydration effects on protein conformation: a study with sol-gel encapsulated proteins J Mol Biol 314 2001 911 922
    • (2001) J Mol Biol , vol.314 , pp. 911-922
    • Eggers, D.K.1    Valentine, J.S.2
  • 26
    • 0028918983 scopus 로고
    • The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry
    • C.A. Miles, T.V. Burjanadze, and A.J. Bailey The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry J Mol Biol 245 1995 437 446
    • (1995) J Mol Biol , vol.245 , pp. 437-446
    • Miles, C.A.1    Burjanadze, T.V.2    Bailey, A.J.3
  • 28
    • 0022645159 scopus 로고
    • A direct correlation between hyperthermia-induced membrane blebbing and survival in synchronous G1 CHO cells
    • M.J. Borrelli, R.S. Wong, and W.C. Dewey A direct correlation between hyperthermia-induced membrane blebbing and survival in synchronous G1 CHO cells J Cell Physiol 126 1986 181 190
    • (1986) J Cell Physiol , vol.126 , pp. 181-190
    • Borrelli, M.J.1    Wong, R.S.2    Dewey, W.C.3
  • 29
    • 0033045105 scopus 로고    scopus 로고
    • A thermodynamic analysis of a family of small globular proteins: SH3 domains
    • V.V. Filimonov, A.I. Azuaga, A.R. Viguera, L. Serrano, and P.L. Mateo A thermodynamic analysis of a family of small globular proteins: SH3 domains Biophys Chem 77 1999 195 208
    • (1999) Biophys Chem , vol.77 , pp. 195-208
    • Filimonov, V.V.1    Azuaga, A.I.2    Viguera, A.R.3    Serrano, L.4    Mateo, P.L.5
  • 31
    • 0034142076 scopus 로고    scopus 로고
    • Thermal stability of the plasma membrane calcium pump. Quantitative analysis of its dependence on lipid-protein interactions
    • V. Levi, J.P.F.C. Rossi, M.M. Echarte, P.R. Castelo, and F.L. Gonzalez Flecha Thermal stability of the plasma membrane calcium pump. Quantitative analysis of its dependence on lipid-protein interactions J Membrane Biol 173 2000 215 225
    • (2000) J Membrane Biol , vol.173 , pp. 215-225
    • Levi, V.1    Rossi, J.P.F.C.2    Echarte, M.M.3    Castelo, P.R.4    Gonzalez Flecha, F.L.5
  • 33
    • 0036318088 scopus 로고    scopus 로고
    • Temperature dependence of thermodynamic properties for DNA/DNA and RNA/DNA duplex formation
    • P. Wu, S. Nakano, and N. Sugimoto Temperature dependence of thermodynamic properties for DNA/DNA and RNA/DNA duplex formation Eur J Biochem 269 2002 2821 2830
    • (2002) Eur J Biochem , vol.269 , pp. 2821-2830
    • Wu, P.1    Nakano, S.2    Sugimoto, N.3
  • 35
    • 0029053420 scopus 로고
    • Thermodynamic studies of the core histones: Ionic strength and pH dependence of H2A-H2B dimmer stability
    • V. Karantza, A.D. Baxevanis, E. Freire, and E.N. Moudrianakis Thermodynamic studies of the core histones: ionic strength and pH dependence of H2A-H2B dimmer stability Biochemistry 34 1995 5988 5996
    • (1995) Biochemistry , vol.34 , pp. 5988-5996
    • Karantza, V.1    Baxevanis, A.D.2    Freire, E.3    Moudrianakis, E.N.4
  • 36
    • 0033406008 scopus 로고    scopus 로고
    • Thermal stability of hydrophobic heme pocket variants of oxidized cytochrome c
    • J.R. Liggins, T.P. Lo, G.D. Brayer, and B.T. Nall Thermal stability of hydrophobic heme pocket variants of oxidized cytochrome c Protein Sci 8 1999 2645 2654
    • (1999) Protein Sci , vol.8 , pp. 2645-2654
    • Liggins, J.R.1    Lo, T.P.2    Brayer, G.D.3    Nall, B.T.4
  • 37
    • 0027384957 scopus 로고
    • Influence of nucleotide binding site occupancy on the thermal stability of the F1 portion of the chloroplast ATP synthase
    • Z.-Y. Wang, E. Freire, and R.E. McCarty Influence of nucleotide binding site occupancy on the thermal stability of the F1 portion of the chloroplast ATP synthase J Biol Chem 268 1993 20785 20790
    • (1993) J Biol Chem , vol.268 , pp. 20785-20790
    • Wang, Z.-Y.1    Freire, E.2    McCarty, R.E.3
  • 38
    • 0025328912 scopus 로고
    • Effects of ions and pH on the thermal stability of thin and thick filaments of skeletal muscle: High-sensitivity differential scanning calorimetric study
    • A. Bertazzon, and T.Y. Tsong Effects of ions and pH on the thermal stability of thin and thick filaments of skeletal muscle: high-sensitivity differential scanning calorimetric study Biochemistry 29 1990 6447 6452
    • (1990) Biochemistry , vol.29 , pp. 6447-6452
    • Bertazzon, A.1    Tsong, T.Y.2
  • 39
    • 0024805554 scopus 로고
    • High-resolution differential scanning calorimetric study of myosin, functional domains, and supramolecular structures
    • A. Bertazzon, and T.Y. Tsong High-resolution differential scanning calorimetric study of myosin, functional domains, and supramolecular structures Biochemistry 28 1989 9784 9790
    • (1989) Biochemistry , vol.28 , pp. 9784-9790
    • Bertazzon, A.1    Tsong, T.Y.2
  • 40
    • 0039940808 scopus 로고    scopus 로고
    • Control of the structural stability of the tubulin dimer by one high affinity bound magnesium ion at nucleotide N-site
    • M. Menendez, G. Rivas, J. Fernando Diaz, and J.M. Andreu Control of the structural stability of the tubulin dimer by one high affinity bound magnesium ion at nucleotide N-site J Biol Chem 273 1998 167 176
    • (1998) J Biol Chem , vol.273 , pp. 167-176
    • Menendez, M.1    Rivas, G.2    Fernando Diaz, J.3    Andreu, J.M.4
  • 43
  • 44
    • 0034144268 scopus 로고    scopus 로고
    • Supraphysiological thermal injury in dunning AT-1 prostate tumor cells
    • S. Bhowmick, D.J. Swanlund, and J.C. Bischof Supraphysiological thermal injury in dunning AT-1 prostate tumor cells ASME J Biomech Eng 122 2000 51 59
    • (2000) ASME J Biomech Eng , vol.122 , pp. 51-59
    • Bhowmick, S.1    Swanlund, D.J.2    Bischof, J.C.3


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