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Volumn 1, Issue 1, 1999, Pages 101-105

Adaptation of proteins from hyperthermophiles to high pressure and high temperature

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 0033170850     PISSN: 14641801     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (39)

References (61)
  • 1
    • 0028072338 scopus 로고
    • Biochemical diversity among sulfur-dependent, hyperthermophilic microorganisms
    • Adams, M.W. 1994. Biochemical diversity among sulfur-dependent, hyperthermophilic microorganisms. FEMS Microbiol. Rev. 15: 261-277.
    • (1994) FEMS Microbiol. Rev. , vol.15 , pp. 261-277
    • Adams, M.W.1
  • 2
    • 0001479540 scopus 로고    scopus 로고
    • Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus: Role of the cluster-coordinating aspartate in physiological electron transfer reactions
    • Adams, M.W., and Zhou, Z.. 1997. Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus: role of the cluster-coordinating aspartate in physiological electron transfer reactions. Biochem. 36: 10892-10900.
    • (1997) Biochem. , vol.36 , pp. 10892-10900
    • Adams, M.W.1    Zhou, Z.2
  • 3
    • 0021772804 scopus 로고
    • Selective chemical modification of a functionally linked lysine in cytochrome P-450 LM2
    • Bernhardt, R., Makower, A., Janig, G.R., and Ruckpaul, K. 1984. Selective chemical modification of a functionally linked lysine in cytochrome P-450 LM2. Biochim. Biophys. Acta. 785: 186-190.
    • (1984) Biochim. Biophys. Acta. , vol.785 , pp. 186-190
    • Bernhardt, R.1    Makower, A.2    Janig, G.R.3    Ruckpaul, K.4
  • 4
    • 0031061411 scopus 로고    scopus 로고
    • Pyrolobus fumarii, gen. and sp. nov., represents a novel group of archaea, extending the upper temperature limit of life to 113 °C
    • Blochl, E., Rachel, R., Burggraf, S., Hafenbradl, D., Jannasch H.W., and Stetter, K.O. 1997. Pyrolobus fumarii, gen. and sp. nov., represents a novel group of archaea, extending the upper temperature limit of life to 113 °C. Extremophiles. 1: 114-121.
    • (1997) Extremophiles , vol.1 , pp. 114-121
    • Blochl, E.1    Rachel, R.2    Burggraf, S.3    Hafenbradl, D.4    Jannasch, H.W.5    Stetter, K.O.6
  • 5
    • 0031039353 scopus 로고    scopus 로고
    • Characterization of the reverse gyrase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Borges, K.M., Bergerat, A., Bogert, A.M., DiRuggiero, J., Forterre, P., and Robb, F.T. 1997. Characterization of the reverse gyrase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 179: 1721-1726.
    • (1997) J. Bacteriol. , vol.179 , pp. 1721-1726
    • Borges, K.M.1    Bergerat, A.2    Bogert, A.M.3    DiRuggiero, J.4    Forterre, P.5    Robb, F.T.6
  • 7
    • 0032502317 scopus 로고    scopus 로고
    • Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxins
    • Cavagnero, S., Debe, D.A., Zhou, Z..H., Adams, M.W., and Chan, S.I. 1998. Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxins. Biochem. 37: 3369-76
    • (1998) Biochem. , vol.37 , pp. 3369-3376
    • Cavagnero, S.1    Debe, D.A.2    Zhou, Z.H.3    Adams, M.W.4    Chan, S.I.5
  • 9
    • 0028833474 scopus 로고
    • Expression and in vitro assembly of recombinant glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
    • DiRuggiero, J., and Robb, F.T. 1995. Expression and in vitro assembly of recombinant glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. Appl. Environ. Microbiol. 61: 159-164.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 159-164
    • DiRuggiero, J.1    Robb, F.T.2
  • 10
    • 0029811087 scopus 로고    scopus 로고
    • Enzymes of central nitrogen metabolism from hyperthermophiles: Characterization, thermostability, and genetics
    • DiRuggiero, J., and Robb, F.T. 1996. Enzymes of central nitrogen metabolism from hyperthermophiles: characterization, thermostability, and genetics. Adv. Protein Chem. 48: 311-339.
    • (1996) Adv. Protein Chem. , vol.48 , pp. 311-339
    • DiRuggiero, J.1    Robb, F.T.2
  • 11
    • 0031039802 scopus 로고    scopus 로고
    • Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus
    • Glasemacher, J., Bock, A.K., Schmid, R., and Schonheit, P. 1997. Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus. Eur. J. Biochem. 244: 561-567
    • (1997) Eur. J. Biochem. , vol.244 , pp. 561-567
    • Glasemacher, J.1    Bock, A.K.2    Schmid, R.3    Schonheit, P.4
  • 12
    • 0030931040 scopus 로고    scopus 로고
    • Both DNA gyrase and reverse gyrase are present in the hyperthermophilic bacterium Thermotoga maritima
    • Guipaud, O., Marguet, E., Noll, K.M., de la Tour, C.B., and Forterre, P. 1997. Both DNA gyrase and reverse gyrase are present in the hyperthermophilic bacterium Thermotoga maritima. Proc. Natl. Acad. Sci. USA. 94: 10606-10611.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10606-10611
    • Guipaud, O.1    Marguet, E.2    Noll, K.M.3    De La Tour, C.B.4    Forterre, P.5
  • 13
    • 0028217082 scopus 로고
    • Pressure stabilization of proteins from extreme thermophiles
    • Hei, D.J., and Clark, D.S. 1994. Pressure stabilization of proteins from extreme thermophiles. Appl. Environ. Microbiol. 60: 932-939.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 932-939
    • Hei, D.J.1    Clark, D.S.2
  • 14
    • 0030977659 scopus 로고    scopus 로고
    • Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: Possible determinants of protein stability
    • Hennig, M., Sterner, R., Kirschner, K., and Jansonius, J.N. 1997. Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability. Biochem. 36: 6009-6016.
    • (1997) Biochem. , vol.36 , pp. 6009-6016
    • Hennig, M.1    Sterner, R.2    Kirschner, K.3    Jansonius, J.N.4
  • 15
    • 0026736883 scopus 로고
    • Proteins from hyperthermophilic archaea: Stability towards covalent modification of the peptide chain
    • Hensel, R., Jakob, I., Scheer, H., and Lottspeich, F. 1992. Proteins from hyperthermophilic archaea: stability towards covalent modification of the peptide chain. Biochem. Soc. Symp. 58: 127-33.
    • (1992) Biochem. Soc. Symp. , vol.58 , pp. 127-133
    • Hensel, R.1    Jakob, I.2    Scheer, H.3    Lottspeich, F.4
  • 16
    • 0030822593 scopus 로고    scopus 로고
    • Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 °C
    • Hiller, R., Zhou, Z..H., Adams, M.W., and Englander, S.W. 1997. Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 °C. Proc. Natl. Acad. Sci. USA. 94: 11329-11332.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11329-11332
    • Hiller, R.1    Zhou, Z.H.2    Adams, M.W.3    Englander, S.W.4
  • 17
    • 0028827595 scopus 로고
    • Enhanced thermotolerance by hydrostatic pressure in the deep-sea hyperthermophile Pyrococcus strain ES4
    • Holden, J.F., and Baross, J.A. 1995. Enhanced thermotolerance by hydrostatic pressure in the deep-sea hyperthermophile Pyrococcus strain ES4. FEMS Microbiol. Ecol. 18: 27-33.
    • (1995) FEMS Microbiol. Ecol. , vol.18 , pp. 27-33
    • Holden, J.F.1    Baross, J.A.2
  • 18
    • 0026320508 scopus 로고
    • Protein stability and molecular adaption to extreme conditions
    • Jaenicke, R. 1991. Protein stability and molecular adaption to extreme conditions. Eur. J. Biochem. 202: 715-728.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 19
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of hyperstable proteins: Glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima
    • Jaenicke, R. 1996a. Structure and stability of hyperstable proteins: glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima. Adv. Protein. Chem. 48: 181-269.
    • (1996) Adv. Protein. Chem. , vol.48 , pp. 181-269
    • Jaenicke, R.1
  • 20
    • 0029922615 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: Strategies of protein stabilization
    • Jaenicke, R. 1996b. Glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: strategies of protein stabilization. FEMS Microbiol. Rev. 18: 215-224.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 215-224
    • Jaenicke, R.1
  • 21
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke, R., and Bohm, G. 1998. The stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 8: 738-48.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 24
    • 0029417337 scopus 로고
    • Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Kengen, S.W., Tuininga, J.E., de Bok, F.A., Stams, A.J., and de Vos, W.M. 1995. Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 270: 30453-30457.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30453-30457
    • Kengen, S.W.1    Tuininga, J.E.2    De Bok, F.A.3    Stams, A.J.4    De Vos, W.M.5
  • 25
  • 26
    • 0026566944 scopus 로고
    • Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus. Thermal denaturation and activation
    • Klump, H., Di Ruggiero, J., Kessel, M., Park, J.B., Adams, M.W., and Robb, F.T. 1992. Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus. Thermal denaturation and activation. J. Biol. Chem. 267: 22681-22685.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22681-22685
    • Klump, H.1    Di Ruggiero, J.2    Kessel, M.3    Park, J.B.4    Adams, M.W.5    Robb, F.T.6
  • 27
    • 0030748521 scopus 로고    scopus 로고
    • The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 A resolution: Structural basis for thermostability
    • Lim, J.H., Yu, Y.G., Han, Y.S., Cho, S., Ahn, B.Y., Kim, S.H., and Cho, Y. 1997. The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 A resolution: structural basis for thermostability. J. Mol. Biol. 270: 259-274.
    • (1997) J. Mol. Biol. , vol.270 , pp. 259-274
    • Lim, J.H.1    Yu, Y.G.2    Han, Y.S.3    Cho, S.4    Ahn, B.Y.5    Kim, S.H.6    Cho, Y.7
  • 28
    • 0032549781 scopus 로고    scopus 로고
    • Redesigning enzyme topology by directed evolution
    • MacBeath, G., Kast, P., and Hilvert, D. 1998. Redesigning enzyme topology by directed evolution. Science. 279: 1958-1961.
    • (1998) Science. , vol.279 , pp. 1958-1961
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 29
    • 0030992315 scopus 로고    scopus 로고
    • Structural features correlated with the extreme thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritime
    • Macedo-Ribeiro, S., Darimont, B., and Sterner, R. 1997. Structural features correlated with the extreme thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritime. J. Biol. Chem. 378: 331-336.
    • (1997) J. Biol. Chem. , vol.378 , pp. 331-336
    • Macedo-Ribeiro, S.1    Darimont, B.2    Sterner, R.3
  • 30
    • 0030620895 scopus 로고    scopus 로고
    • Physiological responses to stress conditions and barophilic behavior of the hyperthermophilic vent Archaeon Pyrococcus abyssi
    • Marteinsson, M.T., Moulin, P., Birrien, J.-L., Gambacorta, A., Vernet, M., and Prieur, D. 1997. Physiological responses to stress conditions and barophilic behavior of the hyperthermophilic vent Archaeon Pyrococcus abyssi. Appl. Env. Micro. 63. 1230-1236.
    • (1997) Appl. Env. Micro. , vol.63 , pp. 1230-1236
    • Marteinsson, M.T.1    Moulin, P.2    Birrien, J.-L.3    Gambacorta, A.4    Vernet, M.5    Prieur, D.6
  • 31
    • 0030582620 scopus 로고    scopus 로고
    • Hyperthermophile protein folding thermodynamics: Differential scanning calorimetry and chemical denaturation of Sac7d
    • McCrary, B.S., Edmondson, S.P., and Shriver, J.W. 1996. Hyperthermophile protein folding thermodynamics: differential scanning calorimetry and chemical denaturation of Sac7d. J. Mol. Biol. 264: 784-805.
    • (1996) J. Mol. Biol. , vol.264 , pp. 784-805
    • McCrary, B.S.1    Edmondson, S.P.2    Shriver, J.W.3
  • 32
    • 0011098198 scopus 로고
    • Pressure dependence of enzyme catalysis
    • M.W.W. Adams and R.M. Kelly, eds. American Chemical Society, Washington, DC
    • Michels, P.C., and Clark, D.S. 1992. Pressure dependence of enzyme catalysis. In: Biocatalysis at Extreme Temperatures. M.W.W. Adams and R.M. Kelly, eds. American Chemical Society, Washington, DC. p. 1088-1121.
    • (1992) Biocatalysis at Extreme Temperatures , pp. 1088-1121
    • Michels, P.C.1    Clark, D.S.2
  • 33
    • 0030773807 scopus 로고    scopus 로고
    • Pressure-enhanced activity and stability of a hyperthermophilic protease from a deep-sea methanogen
    • Michels, P.C., and Clark, D.S. 1997. Pressure-enhanced activity and stability of a hyperthermophilic protease from a deep-sea methanogen. Appl. Environ. Microbiol. 63: 3985-3991.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3985-3991
    • Michels, P.C.1    Clark, D.S.2
  • 34
    • 0029832690 scopus 로고    scopus 로고
    • Pressure effects on enzyme activity and stability at high temperatures
    • Michels, P.C., Hei, D., and Clark, D.S. 1996. Pressure effects on enzyme activity and stability at high temperatures. Adv. Protein Chem. 48: 341-376.
    • (1996) Adv. Protein Chem. , vol.48 , pp. 341-376
    • Michels, P.C.1    Hei, D.2    Clark, D.S.3
  • 35
    • 0000519053 scopus 로고
    • Pressure-temperature effects on the growth and methane production of the extreme thermophile Methanococcus jannaschii
    • Miller, J.F., Shah, N.N., Nelson, C.M., Ludlow, J.M., and Clark, D.S. 1988. Pressure-temperature effects on the growth and methane production of the extreme thermophile Methanococcus jannaschii. Appl. Environ. Microbiol. 54: 3039-3046.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 3039-3046
    • Miller, J.F.1    Shah, N.N.2    Nelson, C.M.3    Ludlow, J.M.4    Clark, D.S.5
  • 36
    • 0024962539 scopus 로고
    • High pressure-temperature bioreactor: Assays of thermostable hydrogenase with fiber optics
    • Miller, J.F., Nelson, C.M., Ludlow, J.M., Shah, N.N., and. Clark. D.S. 1989. High pressure-temperature bioreactor: assays of thermostable hydrogenase with fiber optics. Biotechnol. Bioeng. 34. 1015.
    • (1989) Biotechnol. Bioeng. , vol.34 , pp. 1015
    • Miller, J.F.1    Nelson, C.M.2    Ludlow, J.M.3    Shah, N.N.4    Clark, D.S.5
  • 37
    • 0030065265 scopus 로고    scopus 로고
    • High pressure effects on protein structure and function
    • Mozhaev, V.V., Heremans, K., Frank, J., Masson, P., and Balny, C. 1996. High pressure effects on protein structure and function. Proteins. 24: 81-91.
    • (1996) Proteins. , vol.24 , pp. 81-91
    • Mozhaev, V.V.1    Heremans, K.2    Frank, J.3    Masson, P.4    Balny, C.5
  • 38
    • 0026650176 scopus 로고
    • High-pressure, high-temperature bioreactor for comparing effects of hyperbaric and hydrostatic pressure on bacterial growth
    • Nelson, C.M., Schuppenhauer, M.R., and Clark, D.S. 1992. High-pressure, high-temperature bioreactor for comparing effects of hyperbaric and hydrostatic pressure on bacterial growth. Appl. Environ. Microbiol. 58: 1789-1793.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1789-1793
    • Nelson, C.M.1    Schuppenhauer, M.R.2    Clark, D.S.3
  • 39
    • 0029923296 scopus 로고    scopus 로고
    • Extremely thermostable L(+)-lactate dehydrogenase from Thermotoga maritima: Cloning, characterization, and crystallization of the recombinant enzyme in its tetrameric and octameric state
    • Ostendorp, R., Auerbach, G., and Jaenicke, R. 1996. Extremely thermostable L(+)-lactate dehydrogenase from Thermotoga maritima: cloning, characterization, and crystallization of the recombinant enzyme in its tetrameric and octameric state. Protein. Sci. 5: 862-873.
    • (1996) Protein. Sci. , vol.5 , pp. 862-873
    • Ostendorp, R.1    Auerbach, G.2    Jaenicke, R.3
  • 40
    • 0031244525 scopus 로고    scopus 로고
    • Protein splicing and autoproteolysis mechanisms
    • Perler, F.B., Xu, M.Q., and Paulus, H. 1997. Protein splicing and autoproteolysis mechanisms. Curr. Opin. Chem. Biol. 1: 292-299.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 292-299
    • Perler, F.B.1    Xu, M.Q.2    Paulus, H.3
  • 41
    • 0031551572 scopus 로고    scopus 로고
    • Ferredoxin from the hyperthermophile Thermotoga maritima is stable beyond the boiling point of water
    • Pfeil, W., Gesierich, U., Kleemann, G.R., and Sterner, R. 1997. Ferredoxin from the hyperthermophile Thermotoga maritima is stable beyond the boiling point of water. J. Mol. Biol. 272: 591-596.
    • (1997) J. Mol. Biol. , vol.272 , pp. 591-596
    • Pfeil, W.1    Gesierich, U.2    Kleemann, G.R.3    Sterner, R.4
  • 42
    • 0028159750 scopus 로고
    • A barophilic response by two hyperthermophilic, hydrothermal vent archaea-an upward shift in the optimal temperature and acceleration of growth rate at supraoptimal temperatures by elevated pressure
    • Pledger, R.J., Crump, B.C., and Baross, J.A. 1994. A barophilic response by two hyperthermophilic, hydrothermal vent archaea-an upward shift in the optimal temperature and acceleration of growth rate at supraoptimal temperatures by elevated pressure. FEMS Microbiol. Ecol. 14: 233-241.
    • (1994) FEMS Microbiol. Ecol. , vol.14 , pp. 233-241
    • Pledger, R.J.1    Crump, B.C.2    Baross, J.A.3
  • 43
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov, P.L., and Gill, S. 1988. Stability of protein structure and hydrophobic interaction. Adv. Protein Chem. 39: 191-234.
    • (1988) Adv. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.2
  • 45
    • 0031025616 scopus 로고    scopus 로고
    • Ribonucleotide reductase in the archaeon Pyrococcus furiosus: A critical enzyme in the evolution of DNA genomes?
    • Riera, J., Robb, F.T., Weiss, R., and Fontecave, M. 1997. Ribonucleotide reductase in the archaeon Pyrococcus furiosus: a critical enzyme in the evolution of DNA genomes? Proc. Natl. Acad. Sci. USA. 94: 475-478.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 475-478
    • Riera, J.1    Robb, F.T.2    Weiss, R.3    Fontecave, M.4
  • 46
    • 0031865608 scopus 로고    scopus 로고
    • Novel evolutionary histories and adaptive features of proteins from hyperthermophiles
    • Robb, F.T., and Maeder, D.L. 1998. Novel evolutionary histories and adaptive features of proteins from hyperthermophiles. Curr. Opin. Biotechnol. 9: 288-291.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 288-291
    • Robb, F.T.1    Maeder, D.L.2
  • 48
    • 0030741375 scopus 로고    scopus 로고
    • The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 A resolution
    • Russell, R.J., Ferguson, J.M., Hough, D.W., Danson, M.J., and Taylor, G.L. 1997. The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 A resolution. Biochem. 36: 9983-9994.
    • (1997) Biochem. , vol.36 , pp. 9983-9994
    • Russell, R.J.1    Ferguson, J.M.2    Hough, D.W.3    Danson, M.J.4    Taylor, G.L.5
  • 49
    • 0029099960 scopus 로고
    • Engineering thermostability: Lessons from thermophilic proteins
    • Russell, R.J., and Taylor, G.L. 1995. Engineering thermostability: lessons from thermophilic proteins. Curr. Opin. Biotechnol: 6: 370-374.
    • (1995) Curr. Opin. Biotechnol , vol.6 , pp. 370-374
    • Russell, R.J.1    Taylor, G.L.2
  • 50
    • 0026781884 scopus 로고
    • High resolution NMR study of the pressure-induced unfolding of lysozyme
    • Samarasighe, S.D., Campbell, D.M., Jonas, A., and Jonas, J. 1992. High resolution NMR study of the pressure-induced unfolding of lysozyme. Biochem. 31: 7773-7778
    • (1992) Biochem. , vol.31 , pp. 7773-7778
    • Samarasighe, S.D.1    Campbell, D.M.2    Jonas, A.3    Jonas, J.4
  • 51
    • 0029842905 scopus 로고    scopus 로고
    • Three extremely thermostable proteins from Sulfolobus and a reappraisal of the 'traffic rules'
    • Schafer, T., Bonisch, H., Kardinahl, S., Schmidt, C., and Schafer, G. 1996. Three extremely thermostable proteins from Sulfolobus and a reappraisal of the 'traffic rules'. J. Biol. Chem. 377: 505-512.
    • (1996) J. Biol. Chem. , vol.377 , pp. 505-512
    • Schafer, T.1    Bonisch, H.2    Kardinahl, S.3    Schmidt, C.4    Schafer, G.5
  • 52
    • 0030834850 scopus 로고    scopus 로고
    • Temperature, stability, and the hydrophobic interaction
    • Schellman, J.A. 1997. Temperature, stability, and the hydrophobic interaction. Biophys. J. 73: 2960-2964.
    • (1997) Biophys. J. , vol.73 , pp. 2960-2964
    • Schellman, J.A.1
  • 53
    • 0029924193 scopus 로고    scopus 로고
    • NMR structure of HMfB from the hyperthermophile, Methanothermus fervidus, confirms that this archaeal protein is a histone
    • Starich, M.R., Sandman, K., Reeve, J.N., and Summers, M.F. 1996. NMR structure of HMfB from the hyperthermophile, Methanothermus fervidus, confirms that this archaeal protein is a histone. J. Mol. Biol. 255: 187-203.
    • (1996) J. Mol. Biol. , vol.255 , pp. 187-203
    • Starich, M.R.1    Sandman, K.2    Reeve, J.N.3    Summers, M.F.4
  • 54
    • 0029912086 scopus 로고    scopus 로고
    • Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer
    • Sterner, R., Kleemann, G.R., Szadkowski, H., Lustig, A., Hennig, M., and Kirschner, K. 1996. Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer. Protein Sci. 5: 2000-2008.
    • (1996) Protein Sci. , vol.5 , pp. 2000-2008
    • Sterner, R.1    Kleemann, G.R.2    Szadkowski, H.3    Lustig, A.4    Hennig, M.5    Kirschner, K.6
  • 55
    • 0029991767 scopus 로고    scopus 로고
    • Hyperthermophilic prokaryotes
    • Stetter, K.O. 1996. Hyperthermophilic prokaryotes. FEMS Microbiol. Rev. 18: 149-158.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 149-158
    • Stetter, K.O.1
  • 56
    • 0032144049 scopus 로고    scopus 로고
    • Pressure enhances thermal stability of DNA polymerase from three thermophilic organisms
    • Summit, M., Scott, B., Nielson, K., and Baross, J. 1998. Pressure enhances thermal stability of DNA polymerase from three thermophilic organisms. Extremophiles. 2: 339-345.
    • (1998) Extremophiles. , vol.2 , pp. 339-345
    • Summit, M.1    Scott, B.2    Nielson, K.3    Baross, J.4
  • 57
    • 0032926175 scopus 로고    scopus 로고
    • Pressure-induced thermostabilization of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus."
    • Sun, M.M.C., Tolliday, N., Vetriani, C., Robb, F.T., and Clark, D.S. 1999. Pressure-induced thermostabilization of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus." Protein Sci. 8: 1-8.
    • (1999) Protein Sci. , vol.8 , pp. 1-8
    • Sun, M.M.C.1    Tolliday, N.2    Vetriani, C.3    Robb, F.T.4    Clark, D.S.5
  • 59
    • 0029920131 scopus 로고    scopus 로고
    • A review of acquired thermotolerance, heat-shock proteins, and molecular chaperones in archaea
    • Trent, J.D. 1996. A review of acquired thermotolerance, heat-shock proteins, and molecular chaperones in archaea. FEMS Micro. Rev. 18: 249-258.
    • (1996) FEMS Micro. Rev. , vol.18 , pp. 249-258
    • Trent, J.D.1
  • 61
    • 0020712468 scopus 로고
    • The effect of high pressure upon proteins and other biomolecules
    • Weber, G., and Drickamer, H.G. 1983. The effect of high pressure upon proteins and other biomolecules. Quat. Rev. Biophys. 16: 89-112.
    • (1983) Quat. Rev. Biophys. , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, H.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.