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Volumn 36, Issue 1, 2001, Pages 39-106

Thermophilic adaptation of proteins

Author keywords

[No Author keywords available]

Indexed keywords

2,3 DIPHOSPHOGLYCERIC ACID; CHAPERONE; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; INOSITOL PHOSPHATE;

EID: 0035092271     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.1080/20014091074174     Document Type: Review
Times cited : (335)

References (205)
  • 1
    • 0031935580 scopus 로고    scopus 로고
    • Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution
    • Akanuma, S., Yamagishi, A., Tanaka, N., and Oshima, T. 1998. Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution. Prot. Sci. 7: 698-705.
    • (1998) Prot. Sci. , vol.7 , pp. 698-705
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 2
    • 0033106205 scopus 로고    scopus 로고
    • Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis
    • Akanuma, S., Yamagishi, A., Tanaka, N., and Oshima, T. 1999. Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis. Eur. J. Biochem. 260: 499-504.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 499-504
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 4
    • 0033598189 scopus 로고    scopus 로고
    • Recurrent paralogy in the evolution of archaeal chaperonins
    • Archibald, J. M., Logsdon, J. M. Jr., and Doolittle, W. F. 1999. Recurrent paralogy in the evolution of archaeal chaperonins. Curr. Biol. 9: 1053-1056.
    • (1999) Curr. Biol. , vol.9 , pp. 1053-1056
    • Archibald, J.M.1    Logsdon Jr., J.M.2    Doolittle, W.F.3
  • 5
    • 0033771067 scopus 로고    scopus 로고
    • Physiological roles of trehalose in bacteria and yeasts: A comparative analysis
    • Argüelles, J. C. 2000. Physiological roles of trehalose in bacteria and yeasts: a comparative analysis. Arch. Microbiol. 174: 217-224.
    • (2000) Arch. Microbiol. , vol.174 , pp. 217-224
    • Argüelles, J.C.1
  • 7
    • 0034623981 scopus 로고    scopus 로고
    • Thermostability and Thermoactivity of Citrate Synthases from the Thermophilic and Hyperthermophilic Archaea, Thermoplasma acidophilum and Pyrococcus furiosus
    • Arnott, M. A., Michael, R. A., Thompson, C. R., Hough, D., and Danson, M. J. 2000. Thermostability and Thermoactivity of Citrate Synthases from the Thermophilic and Hyperthermophilic Archaea, Thermoplasma acidophilum and Pyrococcus furiosus. J. Mol. Biol. 304: 657-668.
    • (2000) J. Mol. Biol. , vol.304 , pp. 657-668
    • Arnott, M.A.1    Michael, R.A.2    Thompson, C.R.3    Hough, D.4    Danson, M.J.5
  • 8
    • 0032526414 scopus 로고    scopus 로고
    • Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: The crystal structure at 2.1 Å resolution reveals strategies for intrinsic protein stabilization
    • Auerbach, G., Ostendorp, R., Prade, L., Korndörfer, I., Dams, T., Huber, R., and Jaenicke, R. 1998. Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: the crystal structure at 2.1 Å resolution reveals strategies for intrinsic protein stabilization. Structure 6: 769-781.
    • (1998) Structure , vol.6 , pp. 769-781
    • Auerbach, G.1    Ostendorp, R.2    Prade, L.3    Korndörfer, I.4    Dams, T.5    Huber, R.6    Jaenicke, R.7
  • 9
    • 0028343555 scopus 로고
    • Remarkable archaeal diversity in a Yellowstone National Park hot spring environment
    • Barns, S. M., Fundyga, R. E., Jeffries, M. W., and Pace, N. R. 1994. Remarkable archaeal diversity in a Yellowstone National Park hot spring environment. Proc. Natl. Acad. Sci. USA 91: 1609-1613.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1609-1613
    • Barns, S.M.1    Fundyga, R.E.2    Jeffries, M.W.3    Pace, N.R.4
  • 10
    • 0029832927 scopus 로고    scopus 로고
    • Perspectives on archaeal diversity, thermophily and monophyly from environmental rRNA sequences
    • Barns, S. M., Delwiche, C. F., Palmer, J. D., and Pace, N. R. 1996. Perspectives on archaeal diversity, thermophily and monophyly from environmental rRNA sequences. Proc. Natl. Acad. Sci. USA 93: 9188-9193.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9188-9193
    • Barns, S.M.1    Delwiche, C.F.2    Palmer, J.D.3    Pace, N.R.4
  • 11
    • 0031061411 scopus 로고    scopus 로고
    • Pyrolobus fumarii, gen. and sp. Nov., represents a novel group of archaea, extending the upper temperature limit for life to 113°C
    • Blöchl, 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 for life to 113°C. Extremophiles 1: 14-21.
    • (1997) Extremophiles , vol.1 , pp. 14-21
    • Blöchl, E.1    Rachel, R.2    Burggraf, S.3    Hafenbradl, D.4    Jannasch, H.W.5    Stetter, K.O.6
  • 12
    • 0027992730 scopus 로고
    • Repair of spontaneously deamidated HPr phosphocarrier protein catalyzed by the L-isoaspartate-(D-aspartate) O-methyltransferase
    • Brennan, T. V., Anderson, J. W., Jia, Z., Waygood, E. B., and Clarke, S. 1994. Repair of spontaneously deamidated HPr phosphocarrier protein catalyzed by the L-isoaspartate-(D-aspartate) O-methyltransferase. J. Biol. Chem. 269: 24586-24595.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24586-24595
    • Brennan, T.V.1    Anderson, J.W.2    Jia, Z.3    Waygood, E.B.4    Clarke, S.5
  • 13
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B. and Horwich, A. L. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 14
    • 0031049119 scopus 로고    scopus 로고
    • A pivotal Archaea group
    • Burggraf, S., Heyder, P., and Eis, N. 1997. A pivotal Archaea group. Nature 385: 780.
    • (1997) Nature , vol.385 , pp. 780
    • Burggraf, S.1    Heyder, P.2    Eis, N.3
  • 15
    • 0034693042 scopus 로고    scopus 로고
    • Structural and genomic correlates of hyperthermostability
    • Cambillau, C. and Claverie, J.-M. 2000. Structural and genomic correlates of hyperthermostability. J. Biol. Chem. 275: 32383-32386.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32383-32386
    • Cambillau, C.1    Claverie, J.-M.2
  • 16
    • 0029090926 scopus 로고
    • Response of rubredoxin from Pyrococcus furiosus to environmental changes: Implications for the origin of hyperthermostabiliy
    • Cavagnero, S., Zhou, Z. H., Adams, M. W., and Chan, S. I. 1995. Response of rubredoxin from Pyrococcus furiosus to environmental changes: implications for the origin of hyperthermostabiliy. Biochemistry 34: 9865-9873.
    • (1995) Biochemistry , vol.34 , pp. 9865-9873
    • Cavagnero, S.1    Zhou, Z.H.2    Adams, M.W.3    Chan, S.I.4
  • 17
    • 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. Biochemistry 37: 3369-3376.
    • (1998) Biochemistry , vol.37 , pp. 3369-3376
    • Cavagnero, S.1    Debe, D.A.2    Zhou, Z.H.3    Adams, M.W.4    Chan, S.I.5
  • 18
    • 0034677790 scopus 로고    scopus 로고
    • Elucidation of determinants of protein stability through genome sequence analysis
    • Chakravarty, S. and Varadarajan, R. 2000. Elucidation of determinants of protein stability through genome sequence analysis. FEBS Lett. 470: 65-69.
    • (2000) FEBS Lett. , vol.470 , pp. 65-69
    • Chakravarty, S.1    Varadarajan, R.2
  • 19
    • 0027966149 scopus 로고
    • Occurrence and role of di-myo-inositol-1,1'-phosphate in Methanococcus igneus
    • Ciulla, R. A., Burggraf, S., Stetter, K. O., and Roberts, M. F. 1994. Occurrence and role of di-myo-inositol-1,1'-phosphate in Methanococcus igneus. Appl. Environ. Microbiol. 60: 3660-3664.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3660-3664
    • Ciulla, R.A.1    Burggraf, S.2    Stetter, K.O.3    Roberts, M.F.4
  • 20
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri, A., Raillard, S. A., Bermudez, E., and Stemmer, W. P. 1998. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391: 288-291.
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.A.2    Bermudez, E.3    Stemmer, W.P.4
  • 21
    • 0031613817 scopus 로고    scopus 로고
    • An overview of the role and diversity of compatible solutes in Bacteria and Archaea
    • Antranikian, G., Ed., Springer-Verlag, Berlin
    • DaCosta, M. S., Santos, H., and Galinski, E. A. 1998. An overview of the role and diversity of compatible solutes in Bacteria and Archaea. In: Biotechnology of Extremophiles, pp. 118-153 (Antranikian, G., Ed.), Springer-Verlag, Berlin.
    • (1998) Biotechnology of Extremophiles , pp. 118-153
    • Dacosta, M.S.1    Santos, H.2    Galinski, E.A.3
  • 22
    • 0033551438 scopus 로고    scopus 로고
    • Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima
    • Dams, T. and Jaenicke, R. 1999. Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima. Biochemistry 38: 9169-9178.
    • (1999) Biochemistry , vol.38 , pp. 9169-9178
    • Dams, T.1    Jaenicke, R.2
  • 23
    • 0029977715 scopus 로고    scopus 로고
    • The denaturation and degradation of stable enzymes at high temperatures
    • Daniel, R. M., Dines, M., and Petach, H. H. 1996. The denaturation and degradation of stable enzymes at high temperatures. Biochem. J. 317: 1-11.
    • (1996) Biochem. J. , vol.317 , pp. 1-11
    • Daniel, R.M.1    Dines, M.2    Petach, H.H.3
  • 24
    • 0025718955 scopus 로고
    • Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis
    • Dao-Pin, S., Sauer, U., Nicholson, H., and Matthews, B. W. 1991. Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry 30: 7142-7153.
    • (1991) Biochemistry , vol.30 , pp. 7142-7153
    • Dao-Pin, S.1    Sauer, U.2    Nicholson, H.3    Matthews, B.W.4
  • 26
    • 0031863441 scopus 로고    scopus 로고
    • Mutational analysis of the active site of indoleglycerol phosphate synthase from Escherichia coli
    • Darimont, B., Stehlin, C., Szadkowski, H., and Kirschner, K. 1998. Mutational analysis of the active site of indoleglycerol phosphate synthase from Escherichia coli. Prot. Sci. 7: 1221-1232.
    • (1998) Prot. Sci. , vol.7 , pp. 1221-1232
    • Darimont, B.1    Stehlin, C.2    Szadkowski, H.3    Kirschner, K.4
  • 27
    • 0344609869 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the hyperthermophilic protein sac7d from Sulfolobus acidocaldarius: Contribution of salt bridges to thermostability
    • De Bakker, P. I., Hunenberger, P. H., and McCammon, J. A. 1999. Molecular dynamics simulations of the hyperthermophilic protein sac7d from Sulfolobus acidocaldarius: contribution of salt bridges to thermostability. J. Mol. Biol. 285: 1811-1830.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1811-1830
    • De Bakker, P.I.1    Hunenberger, P.H.2    McCammon, J.A.3
  • 29
    • 0033549770 scopus 로고    scopus 로고
    • Trigger factor and DnaK cooperate in folding of newly synthesized proteins
    • Deuerling, E., Schulze-Specking, A., Tomoyasu, T., Mogk, A., and Bukau, B. 1999. Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature 400: 693-696.
    • (1999) Nature , vol.400 , pp. 693-696
    • Deuerling, E.1    Schulze-Specking, A.2    Tomoyasu, T.3    Mogk, A.4    Bukau, B.5
  • 30
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • Ditzel, L., Lowe, J., Stock, D., Stetter, K. O., Huber, H., Huber, R., and Steinbacher, S. 1998. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93: 125-138.
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Lowe, J.2    Stock, D.3    Stetter, K.O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 31
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins
    • Elcock, A. H. 1998. The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins. J. Mol. Biol. 284: 489-502.
    • (1998) J. Mol. Biol. , vol.284 , pp. 489-502
    • Elcock, A.H.1
  • 32
    • 0031273621 scopus 로고    scopus 로고
    • Continuum solvation model for studying protein hydration thermodynamics at high temperatures
    • Elcock, A. H. and McCammon, J. A. 1997. Continuum solvation model for studying protein hydration thermodynamics at high temperatures. J. Phys. Chem. 101: 9624-9634.
    • (1997) J. Phys. Chem. , vol.101 , pp. 9624-9634
    • Elcock, A.H.1    McCammon, J.A.2
  • 33
    • 0032581501 scopus 로고    scopus 로고
    • Characterization and sequence comparison of temperature-regulated chaperonins from the hyperthermophilic archaeon Archaeoglobus fulgidus
    • Emmerhoff, O. J., Klenk, H. P., and Birkeland, N. K. 1998. Characterization and sequence comparison of temperature-regulated chaperonins from the hyperthermophilic archaeon Archaeoglobus fulgidus. Gene 215: 431-438.
    • (1998) Gene , vol.215 , pp. 431-438
    • Emmerhoff, O.J.1    Klenk, H.P.2    Birkeland, N.K.3
  • 34
    • 0023219801 scopus 로고
    • Purification and characterization of D-glyceraldehyde-3-phosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus
    • Fabry, S. and Hensel, R. 1987. Purification and characterization of D-glyceraldehyde-3-phosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus. Eur. J. Biochem. 165: 147-155.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 147-155
    • Fabry, S.1    Hensel, R.2
  • 35
    • 0031686238 scopus 로고    scopus 로고
    • Helix stabilizing factors and stabilization of thermophilic proteins: An X-ray based study
    • Facchiano, A. M., Colonna, G., and Ragone, R. 1998. Helix stabilizing factors and stabilization of thermophilic proteins: an X-ray based study. Prot. Eng. 11: 753-760.
    • (1998) Prot. Eng. , vol.11 , pp. 753-760
    • Facchiano, A.M.1    Colonna, G.2    Ragone, R.3
  • 36
    • 0032561205 scopus 로고    scopus 로고
    • Group II chaperonin in a thermophilic methanogen, Methanococcus thermolithotrophicus - Chaperone activity and filament-forming ability
    • Furutani, M., Iida, T., Yoshida, T., and Maruyama, T. 1998. Group II chaperonin in a thermophilic methanogen, Methanococcus thermolithotrophicus - chaperone activity and filament-forming ability. J. Biol. Chem. 273: 28399-28407.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28399-28407
    • Furutani, M.1    Iida, T.2    Yoshida, T.3    Maruyama, T.4
  • 37
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation
    • Geiger, T. and Clarke, S. 1987. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J. Biol. Chem. 262: 785-794.
    • (1987) J. Biol. Chem. , vol.262 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 39
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70 and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover, J. R. and Lindquist, S. 1998. Hsp104, Hsp70 and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94: 73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 40
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilisation and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff, P., Mogk, A., Peres Ben Zvi, A., Tomoyasu, T., and Bukau, B. 1999. Sequential mechanism of solubilisation and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. USA 96: 13732-13737.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Peres Ben Zvi, A.3    Tomoyasu, T.4    Bukau, B.5
  • 41
    • 0032956536 scopus 로고    scopus 로고
    • Discontinuous occurrence of the hsp70 (dnaK) gene among Archaea and sequence features of HSP70 suggest a novel outlook on phylogenies inferrred from this protein
    • Gribaldo, S., Lumia, V., Creti, R., de Macario, E. C., Sanangelantoni, A., and Cammarano, P. 1999. Discontinuous occurrence of the hsp70 (dnaK) gene among Archaea and sequence features of HSP70 suggest a novel outlook on phylogenies inferrred from this protein. J. Bacteriol. 181: 434-443.
    • (1999) J. Bacteriol. , vol.181 , pp. 434-443
    • Gribaldo, S.1    Lumia, V.2    Creti, R.3    De Macario, E.C.4    Sanangelantoni, A.5    Cammarano, P.6
  • 43
    • 0031744571 scopus 로고    scopus 로고
    • Hyperthermophiles and the problem of DNA instability
    • Grogan, D. W. 1998. Hyperthermophiles and the problem of DNA instability. Mol. Microbiol. 28: 1043-1049.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1043-1049
    • Grogan, D.W.1
  • 44
    • 0032701797 scopus 로고    scopus 로고
    • Group II chaperonins: New TriC(k)s and turns of a protein folding machine
    • Gutsche, I., Essen, L.-O., and Baumeister, W. 1999. Group II chaperonins: new TriC(k)s and turns of a protein folding machine. J. Mol. Biol. 293: 295-312.
    • (1999) J. Mol. Biol. , vol.293 , pp. 295-312
    • Gutsche, I.1    Essen, L.-O.2    Baumeister, W.3
  • 45
  • 46
  • 47
    • 0034698423 scopus 로고    scopus 로고
    • ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo-electron microscopy
    • Gutsche, I., Mihalache, O., Hegerl, R., Typke, D., and Baumeister, W. 2000c. ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo-electron microscopy. FEBS Lett. 477: 278-282.
    • (2000) FEBS Lett. , vol.477 , pp. 278-282
    • Gutsche, I.1    Mihalache, O.2    Hegerl, R.3    Typke, D.4    Baumeister, W.5
  • 48
    • 0034724559 scopus 로고    scopus 로고
    • Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
    • Haley, D. A., Bova, M. P., Huang, Q.-L., Michaourab, H. S., and Stewart, P. L. 2000. Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies. J. Mol. Biol. 298: 261-272.
    • (2000) J. Mol. Biol. , vol.298 , pp. 261-272
    • Haley, D.A.1    Bova, M.P.2    Huang, Q.-L.3    Michaourab, H.S.4    Stewart, P.L.5
  • 49
    • 0033616712 scopus 로고    scopus 로고
    • Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species
    • Haney, P. J., Badger, J. H., Buldak, G. L., Reich, C. I., Woese, C. R., and Olsen, G. J. 1999. Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species. Proc. Natl. Acad. Sci. USA 96: 3578-3583.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3578-3583
    • Haney, P.J.1    Badger, J.H.2    Buldak, G.L.3    Reich, C.I.4    Woese, C.R.5    Olsen, G.J.6
  • 50
    • 0030884116 scopus 로고    scopus 로고
    • Analysis of deamidation of small, acid-soluble spore proteins from Bacillus subtilis in vitro and in vivo
    • Hayes, C. S. and Setlow, P. 1997. Analysis of deamidation of small, acid-soluble spore proteins from Bacillus subtilis in vitro and in vivo. J. Bacteriol. 179: 6020-6027.
    • (1997) J. Bacteriol. , vol.179 , pp. 6020-6027
    • Hayes, C.S.1    Setlow, P.2
  • 51
    • 0028994307 scopus 로고
    • 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
    • Hennig, M., Darimont, B., Sterner, R., Kirschner, K., and Jansonius, J. N. 1995. 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability Structure 3: 1295-1306.
    • (1995) Structure , vol.3 , pp. 1295-1306
    • Hennig, M.1    Darimont, B.2    Sterner, R.3    Kirschner, K.4    Jansonius, J.N.5
  • 52
    • 0030977659 scopus 로고    scopus 로고
    • Crystal structure at 2.0 Å resolution of phosphoribosylanthranilate isomerase from the hyperthermophile Thermofoga maritima: Possible determinants of protein stability
    • Hennig, M., Sterner, R., Kirschner, K., and Jansonius, J. N. 1997. Crystal structure at 2.0 Å resolution of phosphoribosylanthranilate isomerase from the hyperthermophile Thermofoga maritima: possible determinants of protein stability. Biochemistry 36: 6009-6016.
    • (1997) Biochemistry , vol.36 , pp. 6009-6016
    • Hennig, M.1    Sterner, R.2    Kirschner, K.3    Jansonius, J.N.4
  • 53
    • 0028294022 scopus 로고
    • Stability of glyceraldehyde-3-phosphate dehydrogenases from hyperthermophilic archaea at high temperature
    • Hensel, R. and Jakob, I. 1994. Stability of glyceraldehyde-3-phosphate dehydrogenases from hyperthermophilic archaea at high temperature. System. Appl. Microbiol. 16: 742-745.
    • (1994) System. Appl. Microbiol. , vol.16 , pp. 742-745
    • Hensel, R.1    Jakob, I.2
  • 54
    • 0001912876 scopus 로고
    • Thermoadaptation of methanogenic bacteria by intracellular ion concentration
    • Hensel, R. and König, H. 1988. Thermoadaptation of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol. Lett. 49: 75-79.
    • (1988) FEMS Microbiol. Lett. , vol.49 , pp. 75-79
    • Hensel, R.1    König, H.2
  • 55
    • 0034724392 scopus 로고    scopus 로고
    • Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature
    • Hernandez, G., Jenney, F. E., Jr., Adams, M. W., and LeMaster, D. M. 2000. Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature. Proc. Natl. Acad. Sci. USA 97: 3166-3170.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3166-3170
    • Hernandez, G.1    Jenney Jr., F.E.2    Adams, M.W.3    LeMaster, D.M.4
  • 56
    • 0032541496 scopus 로고    scopus 로고
    • Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli
    • Hesterkamp, T. and Bukau, B. 1998. Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli. EMBO J. 17: 4818-4828.
    • (1998) EMBO J. , vol.17 , pp. 4818-4828
    • Hesterkamp, T.1    Bukau, B.2
  • 57
    • 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
  • 58
    • 0033596902 scopus 로고    scopus 로고
    • A thermodynamic comparison of mesophilic and thermophilic ribonucleases H
    • Hollien, J. and Marqusee, S. 1999. A thermodynamic comparison of mesophilic and thermophilic ribonucleases H. Biochemistry 38: 3831-3836.
    • (1999) Biochemistry , vol.38 , pp. 3831-3836
    • Hollien, J.1    Marqusee, S.2
  • 60
    • 0032730861 scopus 로고    scopus 로고
    • Directed evolution of thermostable kanamycin-resistance gene: A convenient selection marker for Thermus thermophilus
    • Hoseki, J., Yano, T., Koyama, Y., Kuramitsu, S., and Kagamiyama, H. 1999. Directed evolution of thermostable kanamycin-resistance gene: a convenient selection marker for Thermus thermophilus. J. Biochem. 126: 951-956.
    • (1999) J. Biochem. , vol.126 , pp. 951-956
    • Hoseki, J.1    Yano, T.2    Koyama, Y.3    Kuramitsu, S.4    Kagamiyama, H.5
  • 62
    • 0029061139 scopus 로고
    • Isolation of a hyperthermophilic archaeum predicted by in situ RNA analysis
    • Huber, R., Burggraf, S., Mayer, T., Barns, S. M., Roßnagel, P., and Stetter, K. O. 1995. Isolation of a hyperthermophilic archaeum predicted by in situ RNA analysis. Nature 376: 57-58.
    • (1995) Nature , vol.376 , pp. 57-58
    • Huber, R.1    Burggraf, S.2    Mayer, T.3    Barns, S.M.4    Roßnagel, P.5    Stetter, K.O.6
  • 63
    • 0031912606 scopus 로고    scopus 로고
    • Novel division level bacterial diversity in a Yellowstone hot spring
    • Hugenholtz, P., Pitulle, C., Herschberger, K. L., and Pace, N. R. 1998. Novel division level bacterial diversity in a Yellowstone hot spring. J. Bacteriol. 180: 366-376.
    • (1998) J. Bacteriol. , vol.180 , pp. 366-376
    • Hugenholtz, P.1    Pitulle, C.2    Herschberger, K.L.3    Pace, N.R.4
  • 64
    • 0033594989 scopus 로고    scopus 로고
    • Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability
    • Ibarra-Molero, B., Loladze, V,V, Makhatadze, G. I., and Sanchez-Ruiz, J. M. 1999. Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability. Biochemistry 38: 8138-8149.
    • (1999) Biochemistry , vol.38 , pp. 8138-8149
    • Ibarra-Molero, B.1    Loladze, V.V.2    Makhatadze, G.I.3    Sanchez-Ruiz, J.M.4
  • 65
    • 0032532099 scopus 로고    scopus 로고
    • A highly active protein repair enzyme from an extreme thermophile: The L-isoaspartyl methyltransferase from Thermotoga maritima
    • Ichikawa, J. K. and Clarke, S. 1998. A highly active protein repair enzyme from an extreme thermophile: the L-isoaspartyl methyltransferase from Thermotoga maritima. Arch. Biochem. Biophys. 358: 222-231.
    • (1998) Arch. Biochem. Biophys. , vol.358 , pp. 222-231
    • Ichikawa, J.K.1    Clarke, S.2
  • 66
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptations to extreme conditions
    • Jaenicke, R. 1991. Protein stability and molecular adaptations to extreme conditions. Eur. J. Biochem. 202: 715-728.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 67
    • 0032011351 scopus 로고    scopus 로고
    • What ultrastable globular proteins teach us about protein stability
    • Jaenicke, R. 1998. What ultrastable globular proteins teach us about protein stability. Biochemistry (Moscow) 63: 312-321.
    • (1998) Biochemistry (Moscow) , vol.63 , pp. 312-321
    • Jaenicke, R.1
  • 68
    • 0034724271 scopus 로고    scopus 로고
    • Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity?
    • Jaenicke, R. 2000. Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity? Proc. Natl. Acad. Sci. USA 97: 2962-2964.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2962-2964
    • Jaenicke, R.1
  • 69
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke, R. and Böhm, G. 1998. The stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 8: 738-748.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 70
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of hyperstable proteins: Glycolytic enzymes from the hyperthermophilic bacterium Thermotoga maritima
    • Jaenicke, R., Schurig, H., Beaucamp, N., and Ostendorp, R. 1996. Structure and stability of hyperstable proteins: glycolytic enzymes from the hyperthermophilic bacterium Thermotoga maritima. Adv. Prot. Chem. 48: 181-269.
    • (1996) Adv. Prot. Chem. , vol.48 , pp. 181-269
    • Jaenicke, R.1    Schurig, H.2    Beaucamp, N.3    Ostendorp, R.4
  • 72
    • 0023664284 scopus 로고
    • Protein carboxyl methyltransferase facilitates conversion of atypical L-isoaspartyl peptides to normal L-aspartyl peptides
    • Johnson, B. A., Murray, E. D., Jr., Clarke, S., Glass, D. B., and Aswad, D. W. 1987. Protein carboxyl methyltransferase facilitates conversion of atypical L-isoaspartyl peptides to normal L-aspartyl peptides. J. Biol. Chem. 262: 5622-5629.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5622-5629
    • Johnson, B.A.1    Murray Jr., E.D.2    Clarke, S.3    Glass, D.B.4    Aswad, D.W.5
  • 74
    • 0001667712 scopus 로고
    • Methanophosphagen: Unique cyclic pyrophosphate isolated from Methanobacterium thermoautotrophicum
    • Kanodia, S., and Roberts, M. F. 1983. Methanophosphagen: unique cyclic pyrophosphate isolated from Methanobacterium thermoautotrophicum. Proc. Natl. Acad. Sci. USA 80: 5217-5221.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5217-5221
    • Kanodia, S.1    Roberts, M.F.2
  • 75
    • 0031731672 scopus 로고    scopus 로고
    • Proteins from thermophilic and mesophilic organisms essentially do not differ in packing
    • Karshikoff, A. and Ladenstein, R. 1998. Proteins from thermophilic and mesophilic organisms essentially do not differ in packing. Protein Eng. 11: 867-872.
    • (1998) Protein Eng. , vol.11 , pp. 867-872
    • Karshikoff, A.1    Ladenstein, R.2
  • 76
    • 0028245448 scopus 로고
    • Evidence for the operation of a novel Embden-Meyerhof pathway that involves ADP-dependent kinases during sugar fermentation by Pyrococcus furiosus
    • Kengen, S. W. M., de Bok, F. A. M., van Loo, N. D., Dijkema, C., Stams, A. J. M., and de Vos, W. M. 1994. Evidence for the operation of a novel Embden-Meyerhof pathway that involves ADP-dependent kinases during sugar fermentation by Pyrococcus furiosus. J. Biol. Chem. 269: 17537-17541.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17537-17541
    • Kengen, S.W.M.1    De Bok, F.A.M.2    Van Loo, N.D.3    Dijkema, C.4    Stams, A.J.M.5    De Vos, W.M.6
  • 78
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • Kim, K. K., Kim, R., and Kim, S.-H. 1998a. Crystal structure of a small heat-shock protein. Nature 394: 595-599.
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.-H.3
  • 79
    • 13144276278 scopus 로고    scopus 로고
    • Small heat-shock protein of Methanococcus jannaschii, a hyperthermophile
    • Kim, R., Kim, K. K., and Kim, S.-H. 1998b. Small heat-shock protein of Methanococcus jannaschii, a hyperthermophile. Proc. Natl. Acad. Sci. USA 95: 9129-9133.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9129-9133
    • Kim, R.1    Kim, K.K.2    Kim, S.-H.3
  • 80
    • 0033515528 scopus 로고    scopus 로고
    • The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system
    • Klostermeier, D., Seidel, R., and Reinstein, J. 1999. The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system. J. Mol. Biol. 287: 511-525.
    • (1999) J. Mol. Biol. , vol.287 , pp. 511-525
    • Klostermeier, D.1    Seidel, R.2    Reinstein, J.3
  • 81
    • 0030668929 scopus 로고    scopus 로고
    • Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
    • Klumpp, M., Baumeister, W., and Essen, L. O. 1997. Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Cell 91: 263-270.
    • (1997) Cell , vol.91 , pp. 263-270
    • Klumpp, M.1    Baumeister, W.2    Essen, L.O.3
  • 82
    • 0030596013 scopus 로고    scopus 로고
    • Thermal unfolding of the DNA-binding protein Sso7d from the hyperthermophile Sulfolobus solfataricus
    • Knapp, S., Karshikoff, A., Berndt, K. D., Christova, P., Atanasov, B., and Ladenstein, R., 1996. Thermal unfolding of the DNA-binding protein Sso7d from the hyperthermophile Sulfolobus solfataricus. J. Mol. Biol. 264: 1132-1144.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1132-1144
    • Knapp, S.1    Karshikoff, A.2    Berndt, K.D.3    Christova, P.4    Atanasov, B.5    Ladenstein, R.6
  • 83
    • 0033180252 scopus 로고    scopus 로고
    • Extrinsic protein stabilization by the naturally occurring osmolytes β-hydroxyectoine and betaine
    • Knapp, S., Ladenstein, R., and Galinski, E. A. 1999. Extrinsic protein stabilization by the naturally occurring osmolytes β-hydroxyectoine and betaine. Extremophiles 3: 191-198.
    • (1999) Extremophiles , vol.3 , pp. 191-198
    • Knapp, S.1    Ladenstein, R.2    Galinski, E.A.3
  • 84
    • 0025890307 scopus 로고
    • Purification and properties of a α-amylase from the archaeobacterium Pyrococcus woesei
    • Koch, R., Spreinat, A., Lemke, K., and Antranikian, G. 1991. Purification and properties of a α-amylase from the archaeobacterium Pyrococcus woesei. Arch. Microbiol. 155: 572-578.
    • (1991) Arch. Microbiol. , vol.155 , pp. 572-578
    • Koch, R.1    Spreinat, A.2    Lemke, K.3    Antranikian, G.4
  • 85
    • 0029976451 scopus 로고    scopus 로고
    • Tetrameric triosephosphate isomerase from hyperthermophilic Archaea
    • Kohlhoff, M., Dahm, A., and Hensel, R. 1996. Tetrameric triosephosphate isomerase from hyperthermophilic Archaea. FEBS Lett. 383: 245-250.
    • (1996) FEBS Lett. , vol.383 , pp. 245-250
    • Kohlhoff, M.1    Dahm, A.2    Hensel, R.3
  • 86
    • 0028903461 scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
    • Korndörfer, I., Steipe, B., Huber, R., Tomschy, A., and Jaenicke, R. 1995. The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution. J. Mol. Biol. 246: 511-521.
    • (1995) J. Mol. Biol. , vol.246 , pp. 511-521
    • Korndörfer, I.1    Steipe, B.2    Huber, R.3    Tomschy, A.4    Jaenicke, R.5
  • 87
    • 0031824703 scopus 로고    scopus 로고
    • Purification and functional characterization of a chaperone from Methanococcus jannaschii
    • Kowalski, J. M., Kelly, R. M., Konisky, J., Clark, D. S., and Wittrup, K. D. 1998. Purification and functional characterization of a chaperone from Methanococcus jannaschii. Syst. Appl. Microbiol. 21: 173-178.
    • (1998) Syst. Appl. Microbiol. , vol.21 , pp. 173-178
    • Kowalski, J.M.1    Kelly, R.M.2    Konisky, J.3    Clark, D.S.4    Wittrup, K.D.5
  • 88
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar, S., Tsai, C. J., and Nussinov, R. 2000a. Factors enhancing protein thermostability. Prot. Eng. 13: 179-191.
    • (2000) Prot. Eng. , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 89
    • 0033994586 scopus 로고    scopus 로고
    • Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers
    • Kumar, S., Ma, B., Tsai, C. J., and Nussinov, R. 2000b. Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers. Proteins 38: 368-383.
    • (2000) Proteins , vol.38 , pp. 368-383
    • Kumar, S.1    Ma, B.2    Tsai, C.J.3    Nussinov, R.4
  • 90
    • 0031662628 scopus 로고    scopus 로고
    • Effects of temperature, salinity, and medium composition on compatible solute accumulation by Thermococcus spp
    • Lamosa, P., Martins, L. O., DaCosta, M. S., and Santos, H. 1998. Effects of temperature, salinity, and medium composition on compatible solute accumulation by Thermococcus spp. Appl. Environ. Microbiol. 64: 3591-3598.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3591-3598
    • Lamosa, P.1    Martins, L.O.2    DaCosta, M.S.3    Santos, H.4
  • 92
    • 0034603740 scopus 로고    scopus 로고
    • Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus β-glucosidase CelB by directed evolution
    • Lebbink, J. H., Kaper, T., Bron, P., van der Oost, J., and de Vos, W. M. 2000. Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus β-glucosidase CelB by directed evolution. Biochemistry 39: 3656-3665.
    • (2000) Biochemistry , vol.39 , pp. 3656-3665
    • Lebbink, J.H.1    Kaper, T.2    Bron, P.3    Van Der Oost, J.4    De Vos, W.M.5
  • 93
    • 0034731381 scopus 로고    scopus 로고
    • The consensus concept for thermostability engineering of proteins
    • Lehmann, M., Pasamontes, L., Lassen, S.F., and Wyss, M. 2000. The consensus concept for thermostability engineering of proteins. Biochem. Biophys. Acta 1543: 408-415.
    • (2000) Biochem. Biophys. Acta , vol.1543 , pp. 408-415
    • Lehmann, M.1    Pasamontes, L.2    Lassen, S.F.3    Wyss, M.4
  • 94
    • 0028953751 scopus 로고
    • Non-enzymatic hydrolysis of ATP at high temperatures and high pressures
    • Leibrock, E., Bayer, P., and Lüdemann, H.-D. 1995. Non-enzymatic hydrolysis of ATP at high temperatures and high pressures. Biophys. Chem. 54: 175-180.
    • (1995) Biophys. Chem. , vol.54 , pp. 175-180
    • Leibrock, E.1    Bayer, P.2    Lüdemann, H.-D.3
  • 95
    • 0034611628 scopus 로고    scopus 로고
    • Protein folding: Versatility of the cytosolic chaperonin TriC/CCT
    • Leroux, M. P. and Hartl, F. U. 2000. Protein folding: Versatility of the cytosolic chaperonin TriC/CCT. Curr. Biol. 10: R260-R264.
    • (2000) Curr. Biol. , vol.10
    • Leroux, M.P.1    Hartl, F.U.2
  • 97
    • 0026661893 scopus 로고
    • A protein methyltransferase specific for altered aspartyl residues is important in Escherichia coli stationary-phase survival and heat-shock resistance
    • Li, C. and Clarke, S. 1992. A protein methyltransferase specific for altered aspartyl residues is important in Escherichia coli stationary-phase survival and heat-shock resistance. Proc. Natl. Acad. Sci. USA 89: 9885-9889.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9885-9889
    • Li, C.1    Clarke, S.2
  • 99
    • 0033972056 scopus 로고    scopus 로고
    • Mutational analysis of differences in thermostability between histones from mesophilic and hyperthermophilic archaea
    • Li, W. T., Shriver, J. W., and Reeve, J. N. 2000. Mutational analysis of differences in thermostability between histones from mesophilic and hyperthermophilic archaea. J. Bacteriol. 182: 812-817.
    • (2000) J. Bacteriol. , vol.182 , pp. 812-817
    • Li, W.T.1    Shriver, J.W.2    Reeve, J.N.3
  • 100
    • 0026598013 scopus 로고
    • Enzyme stabilization by ectoine-type compatible solutes: Protection against heating, freezing and drying
    • Lippert, K. and Galinski, E. A. 1992. Enzyme stabilization by ectoine-type compatible solutes: protection against heating, freezing and drying. Appl. Microbiol. Biotechnol. 37: 61-65.
    • (1992) Appl. Microbiol. Biotechnol. , vol.37 , pp. 61-65
    • Lippert, K.1    Galinski, E.A.2
  • 101
    • 0033554840 scopus 로고    scopus 로고
    • Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface
    • Loladze, V. V., Ibarra-Molero, B., Sanchez-Ruiz, J. M., and Makhatadze, G. I. 1999. Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry 38: 16419-16423.
    • (1999) Biochemistry , vol.38 , pp. 16419-16423
    • Loladze, V.V.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3    Makhatadze, G.I.4
  • 102
    • 0030766287 scopus 로고    scopus 로고
    • Folding with a two-stroke motor
    • Lorimer, G. H. 1997. Folding with a two-stroke motor. Nature 388: 720-723.
    • (1997) Nature , vol.388 , pp. 720-723
    • Lorimer, G.H.1
  • 104
    • 0032709104 scopus 로고    scopus 로고
    • The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparative thermostability structural analysis often different TIM structures
    • Maes, D., Zeelen, J. P., Thanki, N., Beaucamp, N., Alvarez, M., Thi, M. H., Backmann, J., Martial, J. A., Wyns, L., Jaenicke, R., and Wierenga, R. K. 1999. The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis often different TIM structures. Proteins 37: 441-453.
    • (1999) Proteins , vol.37 , pp. 441-453
    • Maes, D.1    Zeelen, J.P.2    Thanki, N.3    Beaucamp, N.4    Alvarez, M.5    Thi, M.H.6    Backmann, J.7    Martial, J.A.8    Wyns, L.9    Jaenicke, R.10    Wierenga, R.K.11
  • 106
    • 0031779918 scopus 로고    scopus 로고
    • Design, structure and stability of a hyperthermophilic protein variant
    • Malakauskas, S. M. and Mayo, S. L. 1998. Design, structure and stability of a hyperthermophilic protein variant. Nat. Struct. Biol. 5: 470-475.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 470-475
    • Malakauskas, S.M.1    Mayo, S.L.2
  • 107
    • 0030031726 scopus 로고    scopus 로고
    • Induction of synthesis of tetrahydropyrimidine derivatives in Streptomyces strains and their effect on Escherichia coli in response to osmotic and heat stress
    • Malin, G. and Lapidot, A. 1996. Induction of synthesis of tetrahydropyrimidine derivatives in Streptomyces strains and their effect on Escherichia coli in response to osmotic and heat stress. J. Bacteriol. 178: 385-395.
    • (1996) J. Bacteriol. , vol.178 , pp. 385-395
    • Malin, G.1    Lapidot, A.2
  • 108
    • 0028981456 scopus 로고
    • Accumulation of mannosylglycerate and di-myoinositol-phosphate by Pyrococcus furiosus in response to salinity and temperature
    • Martins, L. O. and Santos, H. 1995. Accumulation of mannosylglycerate and di-myoinositol-phosphate by Pyrococcus furiosus in response to salinity and temperature. Appl. Environ. Microbiol. 61: 3299-3303.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3299-3303
    • Martins, L.O.1    Santos, H.2
  • 109
    • 0029838122 scopus 로고    scopus 로고
    • New compatible solutes related to di-myo-inositol-phosphate in members of the order Thermotogales
    • Martins, L. O., Carreto, L. S., Da Costa, M. S., and Santos, H. 1996. New compatible solutes related to di-myo-inositol-phosphate in members of the order Thermotogales. J. Bacteriol. 178: 5644-5651.
    • (1996) J. Bacteriol. , vol.178 , pp. 5644-5651
    • Martins, L.O.1    Carreto, L.S.2    Da Costa, M.S.3    Santos, H.4
  • 111
    • 0031791395 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding cyclic 2,3-diphosphoglycerate synthetase, the key enzyme of cyclic 2,3-diphosphoglycerate metabolism in Methanothermus fervidus
    • Matussek, K., Moritz, P., Brunner, N., Eckerskorn, C., and Hensel, R. 1998. Cloning, sequencing, and expression of the gene encoding cyclic 2,3-diphosphoglycerate synthetase, the key enzyme of cyclic 2,3-diphosphoglycerate metabolism in Methanothermus fervidus. J. Bacteriol. 180: 5997-6004.
    • (1998) J. Bacteriol. , vol.180 , pp. 5997-6004
    • Matussek, K.1    Moritz, P.2    Brunner, N.3    Eckerskorn, C.4    Hensel, R.5
  • 112
    • 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
  • 113
    • 0344848664 scopus 로고    scopus 로고
    • The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges
    • Merz, A., Knöchel, T., Jansonius, J. N., and Kirschner, K. 1999. The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges. J. Mol. Biol. 288: 753-763.
    • (1999) J. Mol. Biol. , vol.288 , pp. 753-763
    • Merz, A.1    Knöchel, T.2    Jansonius, J.N.3    Kirschner, K.4
  • 115
    • 0032401547 scopus 로고    scopus 로고
    • Recombinant homo- and hetero-oligomers of an ultrastable chaperonin from the archaeon Pyrodictium occultum show chaperone activity in vitro
    • Minuth, T., Frey, G., Lindner, P., Rachel, R., Stetter, K. O., and Jaenicke, R. 1998. Recombinant homo- and hetero-oligomers of an ultrastable chaperonin from the archaeon Pyrodictium occultum show chaperone activity in vitro. Eur. J. Biochem. 258: 837-845.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 837-845
    • Minuth, T.1    Frey, G.2    Lindner, P.3    Rachel, R.4    Stetter, K.O.5    Jaenicke, R.6
  • 116
    • 0032930104 scopus 로고    scopus 로고
    • The recombinant thermosome from the archaeon Methanopyrus kandleri: In vitro analysis of its chaperone activity
    • Minuth, T., Henn, M., Rutkat, K., Andrä, S., Frey, G., Rachel, R., Stetter, K. O., and Jaenicke, R. 1999. The recombinant thermosome from the archaeon Methanopyrus kandleri: in vitro analysis of its chaperone activity. Biol. Chem. 380: 55-62.
    • (1999) Biol. Chem. , vol.380 , pp. 55-62
    • Minuth, T.1    Henn, M.2    Rutkat, K.3    Andrä, S.4    Frey, G.5    Rachel, R.6    Stetter, K.O.7    Jaenicke, R.8
  • 117
    • 0033280672 scopus 로고    scopus 로고
    • Exploring nonnatural evolutionary pathways by saturation mutagenesis: Rapid improvement of protein function
    • Miyazaki, K. and Arnold, F. H. 1999. Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function. J. Mol. Evol. 49: 716-720.
    • (1999) J. Mol. Evol. , vol.49 , pp. 716-720
    • Miyazaki, K.1    Arnold, F.H.2
  • 118
    • 0034615775 scopus 로고    scopus 로고
    • Directed evolution study of temperature adaptation in a psychrophilic enzyme
    • Miyazaki, K., Wintrode, P. L., Grayling, R. A., Rubingh, D. N., and Arnold, F. H. 2000. Directed evolution study of temperature adaptation in a psychrophilic enzyme. J. Mol. Biol. 297: 1015-1026.
    • (2000) J. Mol. Biol. , vol.297 , pp. 1015-1026
    • Miyazaki, K.1    Wintrode, P.L.2    Grayling, R.A.3    Rubingh, D.N.4    Arnold, F.H.5
  • 119
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk, A., Tomoyasu, T., Goloubinoff, P., Rüdiger, S., Röder, D., Langen, H., and Bukau, B. 1999. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18: 6934-6949.
    • (1999) EMBO J. , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rüdiger, S.4    Röder, D.5    Langen, H.6    Bukau, B.7
  • 120
    • 0033594880 scopus 로고    scopus 로고
    • Heat-inactivated proteins are rescued by the DnaK·J-GrpE set and ClpB chaperones
    • Motohashi, K., Watanabe, Y., Yohda, M., and Yoshida, M. 1999. Heat-inactivated proteins are rescued by the DnaK·J-GrpE set and ClpB chaperones. Proc. Natl. Acad. Sci. USA 96: 7184-7189.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7184-7189
    • Motohashi, K.1    Watanabe, Y.2    Yohda, M.3    Yoshida, M.4
  • 121
    • 0034615784 scopus 로고    scopus 로고
    • Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticits cold shock protein
    • Mueller, U., Perl, D., Schmid, F. X., and Heinemann, U. 2000. Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticits cold shock protein. J. Mol. Biol. 297: 975-988.
    • (2000) J. Mol. Biol. , vol.297 , pp. 975-988
    • Mueller, U.1    Perl, D.2    Schmid, F.X.3    Heinemann, U.4
  • 122
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Murphy, K. P. and Freire, E. 1992. Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv. Protein Chem. 43: 313-361.
    • (1992) Adv. Protein Chem. , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 123
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., Pace, C. N., and Scholtz, J. M. 1995. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Prot. Sci. 4: 2138-2148.
    • (1995) Prot. Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 125
    • 0343986414 scopus 로고    scopus 로고
    • Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase
    • Nemeth, A., Svingor, A., Pocsik, M., Dobo, J., Magyar, C., Szilagyi, A., Gal, P., and Závodszky, P. (2000). Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase. FEBS Lett. 468: 48-52.
    • (2000) FEBS Lett. , vol.468 , pp. 48-52
    • Nemeth, A.1    Svingor, A.2    Pocsik, M.3    Dobo, J.4    Magyar, C.5    Szilagyi, A.6    Gal, P.7    Závodszky, P.8
  • 126
    • 0032005026 scopus 로고    scopus 로고
    • Protein folding in the cytosol: Chaperonin-dependent and -independent mechanisms
    • Netzer, W. J. and Hartl, F. U. 1998. Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms. Trends Biochem. Sci. 23: 68-73.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 68-73
    • Netzer, W.J.1    Hartl, F.U.2
  • 128
    • 0029031690 scopus 로고
    • Compatible solutes in the thermophilic bacteria Rhodothermus marinus and Thermus thermophilus
    • Nunes, O. C., Manaia, C. M., Da Costa, M. S., and Santos, H. 1995. Compatible solutes in the thermophilic bacteria Rhodothermus marinus and Thermus thermophilus. Appl. Environ. Microbiol. 61: 2351-2357.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2351-2357
    • Nunes, O.C.1    Manaia, C.M.2    Da Costa, M.S.3    Santos, H.4
  • 129
    • 0034020833 scopus 로고    scopus 로고
    • Single surface stabilizer
    • Pace, C. N. 2000. Single surface stabilizer. Nat. Struct. Biol. 7: 345-346.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 345-346
    • Pace, C.N.1
  • 130
    • 0002846347 scopus 로고    scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton, T. E., Ed.. Oxford University Press, Oxford, New York
    • Pace, C. N. and Scholtz, J. M. 1997. Measuring the conformational stability of a protein. In: Protein structure-a practical approach, pp. 299-321. (Creighton, T. E., Ed.). Oxford University Press, Oxford, New York.
    • (1997) Protein Structure-a Practical Approach , pp. 299-321
    • Pace, C.N.1    Scholtz, J.M.2
  • 131
    • 0031565980 scopus 로고    scopus 로고
    • Disruption of an ionic network leads to accelerated thermal denaturation of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima
    • Pappenberger, G., Schurig, H., and Jaenicke, R. 1997. Disruption of an ionic network leads to accelerated thermal denaturation of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima. J. Mol. Biol. 274: 676-683.
    • (1997) J. Mol. Biol. , vol.274 , pp. 676-683
    • Pappenberger, G.1    Schurig, H.2    Jaenicke, R.3
  • 132
    • 0031890195 scopus 로고    scopus 로고
    • Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins
    • Perl, D., Welker, C., Schindler, T., Schröder, K., Marahiel, M. A., Jaenicke, R., and Schmid, F. X. 1998. Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat. Struct. Biol. 5: 229-235.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 229-235
    • Perl, D.1    Welker, C.2    Schindler, T.3    Schröder, K.4    Marahiel, M.A.5    Jaenicke, R.6    Schmid, F.X.7
  • 133
    • 0034100848 scopus 로고    scopus 로고
    • Two exposed amino acid residues confer thermostability on a cold shock protein
    • Perl, D., Mueller, U., Heinemann, U., and Schmid, F. X. 2000. Two exposed amino acid residues confer thermostability on a cold shock protein Nat. Struct. Biol. 7: 380-383.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 380-383
    • Perl, D.1    Mueller, U.2    Heinemann, U.3    Schmid, F.X.4
  • 134
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
    • Perutz, M. F. and Raidt, H. 1975. Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2. Nature 255: 256-259.
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.F.1    Raidt, H.2
  • 135
    • 0030781507 scopus 로고    scopus 로고
    • Insights into thermal resistance of proteins from the intrinsic stability of their alpha-helices
    • Petukhov, M., Kil, Y., Kuramitsu, S., and Lanzov, V. 1997. Insights into thermal resistance of proteins from the intrinsic stability of their alpha-helices. Proteins 29: 309-320.
    • (1997) Proteins , vol.29 , pp. 309-320
    • Petukhov, M.1    Kil, Y.2    Kuramitsu, S.3    Lanzov, V.4
  • 137
    • 0031551572 scopus 로고    scopus 로고
    • Ferredoxin of the hyperthermophile Thermotoga maritima is stable beyond the boiling point of water
    • Pfeil, W., Gesierich, U., Kleemann, G. R., and Sterner, R. 1997. Ferredoxin of 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
  • 139
    • 0034237295 scopus 로고    scopus 로고
    • Lower kinetic limit to protein thermal stability: A proposal regarding protein stability in vivo and its relation with misfolding diseases
    • Plaza del Pino, I. M., Ibarra-Molero, B., and Sanchez-Ruiz, J. M. 2000. Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases. Proteins 40: 58-70.
    • (2000) Proteins , vol.40 , pp. 58-70
    • Plaza Del Pino, I.M.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3
  • 140
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov, P.L. 1979. Stability of proteins: small globular proteins. Adv. Prot. Chem. 33: 167-241.
    • (1979) Adv. Prot. Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 141
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov, P.L. and Khechinashvili, N.N. 1974. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86: 665-684.
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 142
    • 0028867591 scopus 로고
    • Conformational cycle of the archaeosome, a TCP1-like chaperonin from Sulfolobus shibatae
    • Quaite-Randall, E., Trent, J. D., Josephs, R., and Joachimiak, A. 1995. Conformational cycle of the archaeosome, a TCP1-like chaperonin from Sulfolobus shibatae. J. Biol. Chem. 270: 28818-28823.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28818-28823
    • Quaite-Randall, E.1    Trent, J.D.2    Josephs, R.3    Joachimiak, A.4
  • 143
    • 0031031303 scopus 로고    scopus 로고
    • Characterization of di-myo-inositol-1,1′-phosphate in the hyperthermophilic bacterium Thermotoga maritima
    • Ramakrishnan, V., Verhagen, M. F. J. M., and Adams, M. W. W. 1997. Characterization of di-myo-inositol-1,1′-phosphate in the hyperthermophilic bacterium Thermotoga maritima. Appl. Environ. Microbiol. 63: 347-350.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 347-350
    • Ramakrishnan, V.1    Verhagen, M.F.J.M.2    Adams, M.W.W.3
  • 145
    • 0034013150 scopus 로고    scopus 로고
    • Microbial diversity at 83°C in Calcite springs, Yellowstone National Park: Another environment where the Aquificiales and "Korarchaeota" coexist
    • Reysenbach, A.-L., Ehringer, M., and Hershberger, K. 2000. Microbial diversity at 83°C in Calcite springs, Yellowstone National Park: another environment where the Aquificiales and "Korarchaeota" coexist. Extremophiles 4: 61-67.
    • (2000) Extremophiles , vol.4 , pp. 61-67
    • Reysenbach, A.-L.1    Ehringer, M.2    Hershberger, K.3
  • 146
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman, A. M., Chen, S., White, H., Braig, K., and Saibil, H. R. 1996. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell 87: 241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 147
  • 148
    • 0002518285 scopus 로고    scopus 로고
    • Optical spectroscopy to characterize protein conformation and conformational changes
    • Creighton, T. E., Ed.. Oxford University Press, Oxford
    • Schmid, F. X. 1997. Optical spectroscopy to characterize protein conformation and conformational changes. In: Protein Structure - A Practical Approach, pp. 261-297. (Creighton, T. E., Ed.). Oxford University Press, Oxford.
    • (1997) Protein Structure - A Practical Approach , pp. 261-297
    • Schmid, F.X.1
  • 149
  • 150
    • 0026766429 scopus 로고
    • Di-myo-insitol-1,1′-phosphate: A new inositol phosphate isolated from Pyrococcus woesei
    • Scholz, S., Sonnenbichler, J., Schäfer, W., and Hensel, R. 1992. Di-myo-insitol-1,1′-phosphate: a new inositol phosphate isolated from Pyrococcus woesei. FEBS Lett. 306: 239-242.
    • (1992) FEBS Lett. , vol.306 , pp. 239-242
    • Scholz, S.1    Sonnenbichler, J.2    Schäfer, W.3    Hensel, R.4
  • 151
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder, H., Langer, T., Hartl, F. U., and Bukau, B. 1993. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12: 4137-4144.
    • (1993) EMBO J. , vol.12 , pp. 4137-4144
    • Schröder, H.1    Langer, T.2    Hartl, F.U.3    Bukau, B.4
  • 152
    • 0021112604 scopus 로고
    • A novel diphospho-P,P′-diester from Methanobacterium thermoautotrophicum
    • Seely, R. J. and Fahrney, D. E. 1983. A novel diphospho-P,P′-diester from Methanobacterium thermoautotrophicum. J. Biol. Chem. 258: 10835-10838.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10835-10838
    • Seely, R.J.1    Fahrney, D.E.2
  • 153
    • 0034661506 scopus 로고    scopus 로고
    • Enhancement of the thermostability and hydrolytic activity of xylanase by random gene shuffling
    • Shibuya, H., Kaneko, S., and Hayashi, K. 2000. Enhancement of the thermostability and hydrolytic activity of xylanase by random gene shuffling. Biochem. J. 349: 651-656.
    • (2000) Biochem. J. , vol.349 , pp. 651-656
    • Shibuya, H.1    Kaneko, S.2    Hayashi, K.3
  • 154
    • 0031785262 scopus 로고    scopus 로고
    • Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri
    • Shima, S., Herault, D. A., Berkessel, A., and Thauer, R. K. 1998. Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri. Arch. Microbiol. 170: 469-472.
    • (1998) Arch. Microbiol. , vol.170 , pp. 469-472
    • Shima, S.1    Herault, D.A.2    Berkessel, A.3    Thauer, R.K.4
  • 155
    • 0033769510 scopus 로고    scopus 로고
    • A mutation affecting the association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's activity and thermostability
    • Shima, S., Thauer, R. K., Ermler, U., Durchschlag, H., Tziatzios, C., and Schubert, D. 2000. A mutation affecting the association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's activity and thermostability. Eur. J. Biochem. 267: 6619-6623.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6619-6623
    • Shima, S.1    Thauer, R.K.2    Ermler, U.3    Durchschlag, H.4    Tziatzios, C.5    Schubert, D.6
  • 157
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: Folding by forced unfolding
    • Shtilerman, M., Lorimer, G. H., and Englander, S. W. 1999. Chaperonin function: folding by forced unfolding. Science 284: 822-825.
    • (1999) Science , vol.284 , pp. 822-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 158
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
    • Siegers, K., Waldmann, T., Leroux, M. R., Grein, K., Shevchenko, A., Schiebel, E., and Hartl, F. U. 1999. Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 18: 75-84.
    • (1999) EMBO J. , vol.18 , pp. 75-84
    • Siegers, K.1    Waldmann, T.2    Leroux, M.R.3    Grein, K.4    Shevchenko, A.5    Schiebel, E.6    Hartl, F.U.7
  • 159
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins
    • Siegert, R., Leroux, M. R., Scheuffler, C., Hartl, F. U., and Moarefi, I. 2000. Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103: 621-623.
    • (2000) Cell , vol.103 , pp. 621-623
    • Siegert, R.1    Leroux, M.R.2    Scheuffler, C.3    Hartl, F.U.4    Moarefi, I.5
  • 160
    • 0033136552 scopus 로고    scopus 로고
    • Combined effect of the growth temperature and salinity of the medium on the accumulation of compatible solutes by Rhodothermus marinus and Rhodothermus obamensis
    • Silva, Z., Borges, N., Martins, L. O., Wait, R., DaCosta, M. S., and Santos, H. 1999. Combined effect of the growth temperature and salinity of the medium on the accumulation of compatible solutes by Rhodothermus marinus and Rhodothermus obamensis. Extremophiles 3: 163-172.
    • (1999) Extremophiles , vol.3 , pp. 163-172
    • Silva, Z.1    Borges, N.2    Martins, L.O.3    Wait, R.4    DaCosta, M.S.5    Santos, H.6
  • 161
    • 0032799043 scopus 로고    scopus 로고
    • Dissimilatory reduction of Fe(III) by thermophilic bacteria and archaea in deep subsurface petroleum reservoirs of Western Siberia
    • Slobodkin, A. I., Jeanthon, C., L'Haridon, S., Nazina, T., Miroshnichenko, M., and Bonch-Osmolovskaya, E. 1999. Dissimilatory reduction of Fe(III) by thermophilic bacteria and archaea in deep subsurface petroleum reservoirs of Western Siberia Curr. Microbiol. 39: 99-102.
    • (1999) Curr. Microbiol. , vol.39 , pp. 99-102
    • Slobodkin, A.I.1    Jeanthon, C.2    L'Haridon, S.3    Nazina, T.4    Miroshnichenko, M.5    Bonch-Osmolovskaya, E.6
  • 162
    • 0006688434 scopus 로고    scopus 로고
    • Simultaneous enhancement of thermostability and catalytic activity of phospholipase A(1) by evolutionary molecular engineering
    • Song, J. K. and Rhee, J. S. 2000. Simultaneous enhancement of thermostability and catalytic activity of phospholipase A(1) by evolutionary molecular engineering. Appl. Environ. Microbiol. 66: 890-894.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 890-894
    • Song, J.K.1    Rhee, J.S.2
  • 165
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer, W. P. 1994a. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc. Natl. Acad. Sci. USA 91: 10747-10751.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.1
  • 166
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. P. 1994b. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370: 389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 167
    • 0024516367 scopus 로고
    • Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins
    • Stephenson, R. C. and Clarke, S. 1989. Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J. Biol. Chem. 264: 6164-6170.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6164-6170
    • Stephenson, R.C.1    Clarke, S.2
  • 168
    • 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. Prot. Sci. 5: 2000-2008.
    • (1996) Prot. 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
  • 169
    • 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
  • 170
    • 0033066726 scopus 로고    scopus 로고
    • Extremophiles and their adaptation to hot environments
    • Stetter, K. O. 1999. Extremophiles and their adaptation to hot environments. FEBS Lett. 452: 22-25.
    • (1999) FEBS Lett. , vol.452 , pp. 22-25
    • Stetter, K.O.1
  • 171
    • 0027676205 scopus 로고
    • Hyperthermophilic archaea are thriving in deep North Sea and Alaskan oil reservoirs
    • Stetter, K. O., Huber, R., Blöchl, E., Kurr, M., Eden, R. D., Fiedler, M., Cash, H., and Vance, I. 1993. Hyperthermophilic archaea are thriving in deep North Sea and Alaskan oil reservoirs. Nature 300: 743-745.
    • (1993) Nature , vol.300 , pp. 743-745
    • Stetter, K.O.1    Huber, R.2    Blöchl, E.3    Kurr, M.4    Eden, R.D.5    Fiedler, M.6    Cash, H.7    Vance, I.8
  • 172
    • 0034673153 scopus 로고    scopus 로고
    • Contribution of surface salt bridges to protein stability
    • Strop, P. and Mayo, S. L. 2000. Contribution of surface salt bridges to protein stability. Biochemistry 39: 1251-1255.
    • (2000) Biochemistry , vol.39 , pp. 1251-1255
    • Strop, P.1    Mayo, S.L.2
  • 173
    • 0033867241 scopus 로고    scopus 로고
    • Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design
    • Strop, P., Marinescu, A.M., and Mayo, S.L. 2000. Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design. Prot. Sci. 9: 1391-1394.
    • (2000) Prot. Sci. , vol.9 , pp. 1391-1394
    • Strop, P.1    Marinescu, A.M.2    Mayo, S.L.3
  • 174
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • Szilagyi, A. and Závodszky, P. 2000. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Structure Fold. Des. 8: 493-504.
    • (2000) Structure Fold. Des. , vol.8 , pp. 493-504
    • Szilagyi, A.1    Závodszky, P.2
  • 175
    • 0033042910 scopus 로고    scopus 로고
    • A molecular view of archaeal diversity in marine and terrestrial hot water environments
    • Takai, K. and Sako, Y. 1999. A molecular view of archaeal diversity in marine and terrestrial hot water environments. FEMS Microbiol. Ecol. 28: 177-188.
    • (1999) FEMS Microbiol. Ecol. , vol.28 , pp. 177-188
    • Takai, K.1    Sako, Y.2
  • 176
    • 0029936488 scopus 로고    scopus 로고
    • Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5 Å resolution
    • Tanner, J. J., Hecht, R. M., and Krause, K. L. 1996. Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5 Å resolution. Biochemistry 35: 2597-2609.
    • (1996) Biochemistry , vol.35 , pp. 2597-2609
    • Tanner, J.J.1    Hecht, R.M.2    Krause, K.L.3
  • 177
    • 0033032592 scopus 로고    scopus 로고
    • Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains
    • Teter, S. A., Houry, W. A., Ang, D., Tradler, T., Rockabrand, D., Fischer, G., Blum, P., Georgopoulos, C., and Haitl, F. U. 1999. Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell 97: 755-765.
    • (1999) Cell , vol.97 , pp. 755-765
    • Teter, S.A.1    Houry, W.A.2    Ang, D.3    Tradler, T.4    Rockabrand, D.5    Fischer, G.6    Blum, P.7    Georgopoulos, C.8    Haitl, F.U.9
  • 178
    • 0034654087 scopus 로고    scopus 로고
    • Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima
    • Thoma, R., Hennig, M., Sterner, R., and Kirschner, K. 2000. Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima. Structure Fold. Des. 8: 265-276.
    • (2000) Structure Fold. Des. , vol.8 , pp. 265-276
    • Thoma, R.1    Hennig, M.2    Sterner, R.3    Kirschner, K.4
  • 179
    • 0022727906 scopus 로고
    • DNA-dependent RNA polymerases of the three orders of methanogens
    • Thomm, M., Madon, J., and Stetter, K. O. 1986. DNA-dependent RNA polymerases of the three orders of methanogens. Biol. Chem. Hoppe-Seyler 367: 473-481.
    • (1986) Biol. Chem. Hoppe-Seyler , vol.367 , pp. 473-481
    • Thomm, M.1    Madon, J.2    Stetter, K.O.3
  • 180
    • 0033538553 scopus 로고    scopus 로고
    • Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability
    • Thompson, M. J. and Eisenberg, D. 1999. Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability. J. Mol. Biol. 290: 595-604.
    • (1999) J. Mol. Biol. , vol.290 , pp. 595-604
    • Thompson, M.J.1    Eisenberg, D.2
  • 181
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff, S. N. 1993. The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22: 67-97.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 183
    • 0032142866 scopus 로고    scopus 로고
    • The essence of being extremophilic: The role of the unique archaeal membrane lipids
    • Van de Vossenberg, J. L. C. M., Driessen, A. J. M., and Konings, W. N. 1998. The essence of being extremophilic: the role of the unique archaeal membrane lipids. Extremophiles 2: 163-170.
    • (1998) Extremophiles , vol.2 , pp. 163-170
    • Van De Vossenberg, J.L.C.M.1    Driessen, A.J.M.2    Konings, W.N.3
  • 185
    • 0032079487 scopus 로고    scopus 로고
    • The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • Veinger, L., Diamant, S., Buchner, J., and Goloubinoff, P. 1998. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273: 11032-11037.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4
  • 189
    • 0030861309 scopus 로고    scopus 로고
    • Xylanase XynA from the hyperthermophilic bacterium Thermotoga maritima: Structure and stability of the recombinant enzyme and its isolated cellulose-binding domain
    • Wassenberg, D., Schurig, H., Liebl, W., and Jaenicke, R. 1997. Xylanase XynA from the hyperthermophilic bacterium Thermotoga maritima: Structure and stability of the recombinant enzyme and its isolated cellulose-binding domain. Prot. Sci. 6: 1718-1726.
    • (1997) Prot. Sci. , vol.6 , pp. 1718-1726
    • Wassenberg, D.1    Schurig, H.2    Liebl, W.3    Jaenicke, R.4
  • 190
    • 0034645778 scopus 로고    scopus 로고
    • Maltose-binding protein from the hyperthermophilic bacterium Thermotoga maritima: Stability and binding properties
    • Wassenberg, D., Liebl, W., and Jaenicke, R. 2000. Maltose-binding protein from the hyperthermophilic bacterium Thermotoga maritima: stability and binding properties. J. Mol. Biol. 295: 279-288.
    • (2000) J. Mol. Biol. , vol.295 , pp. 279-288
    • Wassenberg, D.1    Liebl, W.2    Jaenicke, R.3
  • 191
    • 0034724719 scopus 로고    scopus 로고
    • Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form
    • Watanabe, Y., Motohashi, K., Taguchi, H., and Yoshida, M. 2000. Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form. J. Biol. Chem. 275: 12388-12392.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12388-12392
    • Watanabe, Y.1    Motohashi, K.2    Taguchi, H.3    Yoshida, M.4
  • 192
    • 0033517351 scopus 로고    scopus 로고
    • Global unfolding of a substrate protein by the HsplOO chaperone ClpA
    • Weber-Ban, E. U., Reid, B. G., Miranker, A. D., and Horwich, A. L. 1999. Global unfolding of a substrate protein by the HsplOO chaperone ClpA. Nature 401: 90-93.
    • (1999) Nature , vol.401 , pp. 90-93
    • Weber-Ban, E.U.1    Reid, B.G.2    Miranker, A.D.3    Horwich, A.L.4
  • 193
    • 0032929094 scopus 로고    scopus 로고
    • Structural and mutagenesis studies of leishmania triosephosphate isomerase: A point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power
    • Williams, J. C., Zeelen, J. P., Neubauer, G., Vriend, G., Backmann, J., Michels, P. A., Lambeir, A. M., and Wierenga, R. K. 1999. Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power. Prot. Eng. 12: 243-250.
    • (1999) Prot. Eng. , vol.12 , pp. 243-250
    • Williams, J.C.1    Zeelen, J.P.2    Neubauer, G.3    Vriend, G.4    Backmann, J.5    Michels, P.A.6    Lambeir, A.M.7    Wierenga, R.K.8
  • 194
    • 0033536578 scopus 로고    scopus 로고
    • Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability
    • Wray, J. W., Baase, W. A., Lindstrom, J. D., Weaver, L. H., Poteete, A. R., and Matthews, B. W. 1999. Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. J. Mol. Biol. 292: 1111-1120.
    • (1999) J. Mol. Biol. , vol.292 , pp. 1111-1120
    • Wray, J.W.1    Baase, W.A.2    Lindstrom, J.D.3    Weaver, L.H.4    Poteete, A.R.5    Matthews, B.W.6
  • 195
    • 0026320363 scopus 로고
    • Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins
    • Wright, H. T. 1991. Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit. Rev. Biochem. Mol. Biol. 26: 1-52.
    • (1991) Crit. Rev. Biochem. Mol. Biol. , vol.26 , pp. 1-52
    • Wright, H.T.1
  • 196
    • 0033905714 scopus 로고    scopus 로고
    • 13C-labeling experiments and nuclear magnetic resonance analysis
    • 13C-labeling experiments and nuclear magnetic resonance analysis. J. Bacteriol. 182: 4632-4636.
    • (2000) J. Bacteriol. , vol.182 , pp. 4632-4636
    • Xavier, K.B.1    Da Costa, M.S.2    Santos, H.3
  • 197
    • 0033603392 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of hyperthermophilic proteins
    • Xiao, L. and Honig, B. 1999. Electrostatic contributions to the stability of hyperthermophilic proteins. J. Mol. Biol. 289: 1435-1444.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1435-1444
    • Xiao, L.1    Honig, B.2
  • 198
    • 0031833974 scopus 로고    scopus 로고
    • Phylogenetic evidence for the existence of novel thermophilic bacteria in hot spring sulfur-turf microbial mats in Japan
    • Yamamoto, H., Hiraishi, A., Kato, K., Chiura, H. X., Maki, Y., and Shimizu, A. 1998. Phylogenetic evidence for the existence of novel thermophilic bacteria in hot spring sulfur-turf microbial mats in Japan. Appl. Environ. Microbiol. 64: 1680-1687.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1680-1687
    • Yamamoto, H.1    Hiraishi, A.2    Kato, K.3    Chiura, H.X.4    Maki, Y.5    Shimizu, A.6
  • 199
    • 0030953876 scopus 로고    scopus 로고
    • In vitro stabilization and in vivo solubilization of foreign proteins by the beta subunit of a chaperonin from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1
    • Yan, Z., Fujiwara, S., Kohda, K., Takagi, M., and Imanaka, T. 1997. In vitro stabilization and in vivo solubilization of foreign proteins by the beta subunit of a chaperonin from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1. Appl. Environ. Microbiol. 63: 785-789.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 785-789
    • Yan, Z.1    Fujiwara, S.2    Kohda, K.3    Takagi, M.4    Imanaka, T.5
  • 200
    • 13244249836 scopus 로고
    • The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
    • Yip, K. S., Stillman, T. J., Britton, K. L., Artymiuk, P. J., Baker, P. J., Sedelnikova, S. E., Engel, P. C., Pasquo, A., Chiaraluce, R., and Consalvi, V. 1995. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 3: 1147-1158.
    • (1995) Structure , vol.3 , pp. 1147-1158
    • Yip, K.S.1    Stillman, T.J.2    Britton, K.L.3    Artymiuk, P.J.4    Baker, P.J.5    Sedelnikova, S.E.6    Engel, P.C.7    Pasquo, A.8    Chiaraluce, R.9    Consalvi, V.10
  • 201
    • 0031592944 scopus 로고    scopus 로고
    • Structural and functional characterization of homooligomeric complexes of α and β chaperonin subunits from the hyperthermophilic archaeon Thermococcus strain KS-1
    • Yoshida, T., Yohda, M., Iida, T., Maruyama, T., Taguchi, H., Yazaki, K., Ohta, T., Odaka, M., Endo, I., and Kagawa, Y. 1997. Structural and functional characterization of homooligomeric complexes of α and β chaperonin subunits from the hyperthermophilic archaeon Thermococcus strain KS-1. J. Mol. Biol. 273: 635-645.
    • (1997) J. Mol. Biol. , vol.273 , pp. 635-645
    • Yoshida, T.1    Yohda, M.2    Iida, T.3    Maruyama, T.4    Taguchi, H.5    Yazaki, K.6    Ohta, T.7    Odaka, M.8    Endo, I.9    Kagawa, Y.10
  • 202
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky, P., Kardos, J., Svingor, and Petsko, G. A. 1998. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc. Natl. Acad. Sci. USA 95: 7406-7411.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor3    Petsko, G.A.4
  • 203
    • 0032142867 scopus 로고    scopus 로고
    • Thermozymes: Biotechnoogy and structure-function relationships
    • Zeikus, J. G., Vieille, C., and Savchenko, A. 1998. Thermozymes: biotechnoogy and structure-function relationships. Extremophiles 2: 179-183.
    • (1998) Extremophiles , vol.2 , pp. 179-183
    • Zeikus, J.G.1    Vieille, C.2    Savchenko, A.3
  • 204
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao, H., Giver, L., Shao, Z., Affholter, J. A., and Arnold, F. H. 1998. Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat. Biotechnol. 16: 258-261.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Shao, Z.3    Affholter, J.A.4    Arnold, F.H.5
  • 205
    • 0027331573 scopus 로고
    • Both the Eschenchia coli chaperone systems, GroEL/GroES and Dnak/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same acitivity
    • Ziemienowicz, A., Skowyra, D., Zeilstra-Ryalls, J., Fayet, O., Georgopoulos, C., and Zylicz, M. Both the Eschenchia coli chaperone systems, GroEL/GroES and Dnak/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same acitivity. 1993. J. Biol. Chem. 268: 25425-25431.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25425-25431
    • Ziemienowicz, A.1    Skowyra, D.2    Zeilstra-Ryalls, J.3    Fayet, O.4    Georgopoulos, C.5    Zylicz, M.6


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