메뉴 건너뛰기




Volumn 189, Issue 19, 2007, Pages 7134-7144

Methionine sulfoxide reductase from the hyperthermophilic archaeon Thermococcus kodakaraensis, an enzyme designed to function at suboptimal growth temperatures

Author keywords

[No Author keywords available]

Indexed keywords

DISSOLVED OXYGEN; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE; METHIONINE SULFOXIDE REDUCTASE A; METHIONINE SULFOXIDE REDUCTASE B; RECOMBINANT PROTEIN; THIOREDOXIN;

EID: 34948861113     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00751-06     Document Type: Article
Times cited : (17)

References (49)
  • 1
    • 0035093350 scopus 로고    scopus 로고
    • Energetics of overall metabolic reactions of thermophilic and hyperthermophilic Archaea and Bacteria
    • Amend, J. P., and E. L. Shock. 2001. Energetics of overall metabolic reactions of thermophilic and hyperthermophilic Archaea and Bacteria. FEMS Microbiol. Rev. 25:175-243.
    • (2001) FEMS Microbiol. Rev , vol.25 , pp. 175-243
    • Amend, J.P.1    Shock, E.L.2
  • 2
    • 0242413235 scopus 로고    scopus 로고
    • Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis
    • Antoine, M., S. Boschi-Muller, and G. Branlant. 2003. Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis. J. Biol. Chem. 278:45352-45357.
    • (2003) J. Biol. Chem , vol.278 , pp. 45352-45357
    • Antoine, M.1    Boschi-Muller, S.2    Branlant, G.3
  • 3
    • 8444239349 scopus 로고    scopus 로고
    • Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1
    • Atomi, H., T. Fukui, T. Kanai, M. Morikawa, and T. Imanaka. 2004. Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1. Archaea 1:263-267.
    • (2004) Archaea , vol.1 , pp. 263-267
    • Atomi, H.1    Fukui, T.2    Kanai, T.3    Morikawa, M.4    Imanaka, T.5
  • 4
    • 0034680847 scopus 로고    scopus 로고
    • A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli
    • Boschi-Muller, S., S. Azza, S. Sanglier-Cianferani, F. Talfournier, A. Van Dorsselear, and G. Branlant. 2000. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. J. Biol. Chem. 275:35908-35913.
    • (2000) J. Biol. Chem , vol.275 , pp. 35908-35913
    • Boschi-Muller, S.1    Azza, S.2    Sanglier-Cianferani, S.3    Talfournier, F.4    Van Dorsselear, A.5    Branlant, G.6
  • 5
    • 12844275002 scopus 로고    scopus 로고
    • The enzymology and biochemistry of methionine sulfoxide reductases
    • Boschi-Muller, S., A. Olry, M. Antoine, and G. Branlant. 2005. The enzymology and biochemistry of methionine sulfoxide reductases. Biochim. Biophys. Acta 1703:231-238.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 231-238
    • Boschi-Muller, S.1    Olry, A.2    Antoine, M.3    Branlant, G.4
  • 9
    • 12844259524 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases in prokaryotes
    • Ezraty, B., L. Aussel, and F. Barras. 2005. Methionine sulfoxide reductases in prokaryotes. Biochim. Biophys. Acta 1703:221-229.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 221-229
    • Ezraty, B.1    Aussel, L.2    Barras, F.3
  • 10
    • 0022445886 scopus 로고
    • Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C
    • Fiala, G., and K. O. Stetter. 1986. Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C. Arch. Microbiol. 145:56-61.
    • (1986) Arch. Microbiol , vol.145 , pp. 56-61
    • Fiala, G.1    Stetter, K.O.2
  • 11
    • 13544250517 scopus 로고    scopus 로고
    • Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes
    • Fukui, T., H. Atomi, T. Kanai, R. Matsumi, S. Fujiwara, and T. Imanaka. 2005. Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. Genome Res. 15:352-363.
    • (2005) Genome Res , vol.15 , pp. 352-363
    • Fukui, T.1    Atomi, H.2    Kanai, T.3    Matsumi, R.4    Fujiwara, S.5    Imanaka, T.6
  • 13
    • 0032814950 scopus 로고    scopus 로고
    • Thermococcus waiotapuensis sp. nov., an extremely thermophilic archaeon isolated from a freshwater hot spring
    • González, J. M., D. Sheckells, M. Viebahn, D. Krupatkina, K. M. Borges, and F. T. Robb. 1999. Thermococcus waiotapuensis sp. nov., an extremely thermophilic archaeon isolated from a freshwater hot spring. Arch. Microbiol. 172:95-101.
    • (1999) Arch. Microbiol , vol.172 , pp. 95-101
    • González, J.M.1    Sheckells, D.2    Viebahn, M.3    Krupatkina, D.4    Borges, K.M.5    Robb, F.T.6
  • 14
    • 0024351039 scopus 로고
    • Phenotypic characterization of the archaebacterial genus Sulfolobus: Comparison of five wild-type strains
    • Grogan, D. W. 1989. Phenotypic characterization of the archaebacterial genus Sulfolobus: comparison of five wild-type strains. J. Bacteriol. 171:6710-6719.
    • (1989) J. Bacteriol , vol.171 , pp. 6710-6719
    • Grogan, D.W.1
  • 15
    • 12544251532 scopus 로고    scopus 로고
    • Halobacterium noricense sp. nov., an archaeal isolate from a bore core of an alpine Permian salt deposit, classification of Halobacterium sp. NRC-1 as a strain of H. salinarum and emended description of H. salinarum
    • Gruber, C., A. Legat, M. Pfaffenhuemer, C. Radax, G. Weidler, H. J. Busse, and H. Stan-Lotter. 2004. Halobacterium noricense sp. nov., an archaeal isolate from a bore core of an alpine Permian salt deposit, classification of Halobacterium sp. NRC-1 as a strain of H. salinarum and emended description of H. salinarum. Extremophiles 8:431-439.
    • (2004) Extremophiles , vol.8 , pp. 431-439
    • Gruber, C.1    Legat, A.2    Pfaffenhuemer, M.3    Radax, C.4    Weidler, G.5    Busse, H.J.6    Stan-Lotter, H.7
  • 16
    • 0035000622 scopus 로고    scopus 로고
    • Diversity among three novel groups of hyperthermophilic deep-sea Thermococcus species from three sites in the northeastern Pacific Ocean
    • Holden, J. F., K. Takai, M. Summit, S. Bolton, J. Zyskowski, and J. A. Baross. 2001. Diversity among three novel groups of hyperthermophilic deep-sea Thermococcus species from three sites in the northeastern Pacific Ocean. FEMS Microbiol. Ecol. 36:51-60.
    • (2001) FEMS Microbiol. Ecol , vol.36 , pp. 51-60
    • Holden, J.F.1    Takai, K.2    Summit, M.3    Bolton, S.4    Zyskowski, J.5    Baross, J.A.6
  • 17
    • 0037007636 scopus 로고    scopus 로고
    • A new phylum of Archaea represented by a nanosized hyperthermophilic symbiont
    • Huber, H., M. J. Hohn, R. Rachel, T. Fuchs, V. C. Wimmer, and K. O. Stetter. 2002. A new phylum of Archaea represented by a nanosized hyperthermophilic symbiont. Nature 417:63-67.
    • (2002) Nature , vol.417 , pp. 63-67
    • Huber, H.1    Hohn, M.J.2    Rachel, R.3    Fuchs, T.4    Wimmer, V.C.5    Stetter, K.O.6
  • 18
    • 0141957432 scopus 로고    scopus 로고
    • Taxonomy of nonmethanogenic hyperthermophilic and related thermophilic archaea
    • Itoh, T. 2003. Taxonomy of nonmethanogenic hyperthermophilic and related thermophilic archaea. J. Biosci. Bioeng. 96:203-212.
    • (2003) J. Biosci. Bioeng , vol.96 , pp. 203-212
    • Itoh, T.1
  • 19
    • 0021070752 scopus 로고
    • Methanococcus jannaschii sp. nov., an extremely thermophilic methanogen from a submarine hydrothermal vent
    • Jones, W. J., J. A. Leigh, F. Mayer, C. R. Woese, and R. S. Wolfe. 1983. Methanococcus jannaschii sp. nov., an extremely thermophilic methanogen from a submarine hydrothermal vent. Arch. Microbiol. 136:254-261.
    • (1983) Arch. Microbiol , vol.136 , pp. 254-261
    • Jones, W.J.1    Leigh, J.A.2    Mayer, F.3    Woese, C.R.4    Wolfe, R.S.5
  • 20
    • 12844273604 scopus 로고    scopus 로고
    • The three-dimensional structures of peptide methionine sulfoxide reductases: Current knowledge and open questions
    • Kauffmann, B., A. Aubry, and F. Favier. 2005. The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions. Biochim. Biophys. Acta 1703:249-260.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 249-260
    • Kauffmann, B.1    Aubry, A.2    Favier, F.3
  • 23
    • 0029564827 scopus 로고
    • Thermococcus alcaliphilus sp. nov., a new hyperthermophilic archaeum growing on polysulfide at alkalir e pH
    • Keller, M., F.-J. Braun, R. Dirmeier, D. Hafenbradl, S. Burggraf, R. Rachel, and K. O. Stetter. 1995. Thermococcus alcaliphilus sp. nov., a new hyperthermophilic archaeum growing on polysulfide at alkalir e pH. Arch. Microbiol. 164:390-395.
    • (1995) Arch. Microbiol , vol.164 , pp. 390-395
    • Keller, M.1    Braun, F.-J.2    Dirmeier, R.3    Hafenbradl, D.4    Burggraf, S.5    Rachel, R.6    Stetter, K.O.7
  • 24
    • 0031458333 scopus 로고    scopus 로고
    • Klenk, H.-P, R. A. Clayton, J.-F. Tomb, O. White, K. E. Nelson, K. A. Ketchum, R. J. Dodson, M. Gwinn, E. K. Hickey, J. D. Peterson, D. L. Richardson, A. R. Kerlavage, D. E. Graham, N. C. Kyrpides, R. D. Fleischmann, J. Quackenbush, N. H. Lee, G. G. Sutton, S. Gill, E. F. Kirkness, B. A. Dougherty, K. McKenney, M. D. Adams, B. Loftus, S. Peterson, C. I. Reich, L. K. McNeil, J. H. Badger, A. Glodek, L. Zhou, R. Overbeek, J. D. Gocayne, J. F. Weidman, L. McDonald, T. Utterback, M. D. Cotton, T. Spriggs, P. Artiach, B. P. Kaine, S. M. Sykes, P. W. Sadow, K. P. D'Andrea, C. Bowman, C. Fujii, S. A. Garland, T. M. Mason, G. J. Olsen, C. M. Fraser, H. O. Smith, C. R. Woese, and J. C. Venter. 1997. The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390:364-370
    • Klenk, H.-P., R. A. Clayton, J.-F. Tomb, O. White, K. E. Nelson, K. A. Ketchum, R. J. Dodson, M. Gwinn, E. K. Hickey, J. D. Peterson, D. L. Richardson, A. R. Kerlavage, D. E. Graham, N. C. Kyrpides, R. D. Fleischmann, J. Quackenbush, N. H. Lee, G. G. Sutton, S. Gill, E. F. Kirkness, B. A. Dougherty, K. McKenney, M. D. Adams, B. Loftus, S. Peterson, C. I. Reich, L. K. McNeil, J. H. Badger, A. Glodek, L. Zhou, R. Overbeek, J. D. Gocayne, J. F. Weidman, L. McDonald, T. Utterback, M. D. Cotton, T. Spriggs, P. Artiach, B. P. Kaine, S. M. Sykes, P. W. Sadow, K. P. D'Andrea, C. Bowman, C. Fujii, S. A. Garland, T. M. Mason, G. J. Olsen, C. M. Fraser, H. O. Smith, C. R. Woese, and J. C. Venter. 1997. The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390:364-370.
  • 25
    • 2542612966 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of aging
    • Koc, A., A. P. Gasch, J. C. Rutherford, H.-Y. Kim, and V. N. Gladyshev. 2004. Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of aging. Proc. Natl. Acad. Sci. USA 101:7999-8004.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7999-8004
    • Koc, A.1    Gasch, A.P.2    Rutherford, J.C.3    Kim, H.-Y.4    Gladyshev, V.N.5
  • 26
    • 0037020249 scopus 로고    scopus 로고
    • Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase
    • Kumar, R. A., A. Koc, R. L. Cerny, and V. N. Gladyshev. 2002. Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase. J. Biol. Chem. 277:37527-37535.
    • (2002) J. Biol. Chem , vol.277 , pp. 37527-37535
    • Kumar, R.A.1    Koc, A.2    Cerny, R.L.3    Gladyshev, V.N.4
  • 27
  • 28
    • 0028535189 scopus 로고
    • Reduction of DABS-L-methionine-dl-sulfoxide by protein methionine sulfoxide reductase from polymorphonuclear leukocytes: Stereospecificity towards the l-sulfoxide
    • Minetti, G., C. Balduini, and A. Brovelli. 1994. Reduction of DABS-L-methionine-dl-sulfoxide by protein methionine sulfoxide reductase from polymorphonuclear leukocytes: stereospecificity towards the l-sulfoxide. Ital. J. Biochem. 43:273-283.
    • (1994) Ital. J. Biochem , vol.43 , pp. 273-283
    • Minetti, G.1    Balduini, C.2    Brovelli, A.3
  • 30
    • 12844267504 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: Ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
    • Moskovitz, J. 2005. Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases. Biochim. Biophys. Acta 1703:213-219.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 213-219
    • Moskovitz, J.1
  • 32
    • 0034640506 scopus 로고    scopus 로고
    • Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
    • Moskovitz, J., J. M. Posten, B. S. Berlett, N. J. Nosworthy, R. Szczepanowski, and E. R. Stadtman. 2000. Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity. J. Biol. Chem. 275:14167-14172.
    • (2000) J. Biol. Chem , vol.275 , pp. 14167-14172
    • Moskovitz, J.1    Posten, J.M.2    Berlett, B.S.3    Nosworthy, N.J.4    Szczepanowski, R.5    Stadtman, E.R.6
  • 33
    • 4444284939 scopus 로고    scopus 로고
    • Kinetic characterization of the catalytic mechanism of methionine sulfoxide reductase B from Neisseria meningitidis
    • Olry, A., S. Boschi-Muller, and G. Branlant. 2004. Kinetic characterization of the catalytic mechanism of methionine sulfoxide reductase B from Neisseria meningitidis. Biochemistry 43:11616-11622.
    • (2004) Biochemistry , vol.43 , pp. 11616-11622
    • Olry, A.1    Boschi-Muller, S.2    Branlant, G.3
  • 34
    • 0025276332 scopus 로고
    • Haloarcula marismortui (Volcani) sp. nov., nom. rev., an extremely halophilic bacterium from the Dead Sea
    • Oren, A., M. Ginzburg, B. Z. Ginzburg, L. I. Hochstein, and B. E. Volcani. 1990. Haloarcula marismortui (Volcani) sp. nov., nom. rev., an extremely halophilic bacterium from the Dead Sea. Int. J. Syst. Bacteriol. 40:209-210.
    • (1990) Int. J. Syst. Bacteriol , vol.40 , pp. 209-210
    • Oren, A.1    Ginzburg, M.2    Ginzburg, B.Z.3    Hochstein, L.I.4    Volcani, B.E.5
  • 35
    • 0033952662 scopus 로고    scopus 로고
    • Culture-dependent and culture-independent characterization of microbial assemblages associated with high-temperature petroleum reservoirs
    • Orphan, V. J., L. T. Taylor, D. Hafenbradl, and E. F. Delong. 2000. Culture-dependent and culture-independent characterization of microbial assemblages associated with high-temperature petroleum reservoirs. Appl. Environ. Microbiol. 66:700-711.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 700-711
    • Orphan, V.J.1    Taylor, L.T.2    Hafenbradl, D.3    Delong, E.F.4
  • 36
    • 2442677663 scopus 로고    scopus 로고
    • A new intrinsic thermal parameter for enzymes reveals true temperature optima
    • Peterson, M. E., R. Eisenthal, M. J. Danson, A. Spence, and R. M. Daniel. 2004. A new intrinsic thermal parameter for enzymes reveals true temperature optima. J. Biol. Chem. 279:20717-20722.
    • (2004) J. Biol. Chem , vol.279 , pp. 20717-20722
    • Peterson, M.E.1    Eisenthal, R.2    Danson, M.J.3    Spence, A.4    Daniel, R.M.5
  • 39
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N., and M. Nei. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
    • (1987) Mol. Biol. Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 40
    • 0037215528 scopus 로고    scopus 로고
    • Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Sato, T., T. Fukui, H. Atomi, and T. Imanaka. 2003. Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Bacteriol. 185:210-220.
    • (2003) J. Bacteriol , vol.185 , pp. 210-220
    • Sato, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 41
    • 0028806517 scopus 로고
    • Picrophilus gen. nov., fam. nov.: A novel aerobic, heterotrophic, thermoacidophilic genus and family comprising archaea capable of growth around pH 0
    • Schleper, C., G. Puehler, I. Holz, A. Gambacorta, D. Janekovic, U. Santarius, H.-P. Klenk, and W. Zillig. 1995. Picrophilus gen. nov., fam. nov.: a novel aerobic, heterotrophic, thermoacidophilic genus and family comprising archaea capable of growth around pH 0. J. Bacteriol. 177:7050-7059.
    • (1995) J. Bacteriol , vol.177 , pp. 7050-7059
    • Schleper, C.1    Puehler, G.2    Holz, I.3    Gambacorta, A.4    Janekovic, D.5    Santarius, U.6    Klenk, H.-P.7    Zillig, W.8
  • 42
    • 11144313963 scopus 로고
    • Thermoplasma acidophilum and Thermplasma volcanium sp. nov. from solfatara fields
    • Segerer, A., T. A. Langworthy, and K. O. Stetter. 1988. Thermoplasma acidophilum and Thermplasma volcanium sp. nov. from solfatara fields. Syst. Appl. Microbiol. 10:161-171.
    • (1988) Syst. Appl. Microbiol , vol.10 , pp. 161-171
    • Segerer, A.1    Langworthy, T.A.2    Stetter, K.O.3
  • 43
    • 0034945083 scopus 로고    scopus 로고
    • She, Q., R. K. Singh, F. Confalonieri, Y. Zivanovic, G. Allard, M. J. Awayez, C. C.-Y. Chan-Weiher, I. G. Clausen, B. A. Curtis, A. De Moors, G. Erauso, C. Fletcher, P. M. K. Gordon, I. Heikamp-de Jong, A. C. Jeffries, C. J. Kozera, N. Medina, X. Peng, H. P. Thi-Ngoc, P. Redder, M. E. Schenk, C. Theriault, N. Tolstrup, R. L. Charlebois, W. F. Doolittle, M. Duguet, T. Gaasterland, R. A. Garrett, M. A. Ragan, C. W. Sensen, and J. Van der Oost. 2001. The complete genome of the crenarchaeon Sulfolobus solfataricus P2. Proc. Natl. Acad. Sci. USA 98:7835-7840.
    • She, Q., R. K. Singh, F. Confalonieri, Y. Zivanovic, G. Allard, M. J. Awayez, C. C.-Y. Chan-Weiher, I. G. Clausen, B. A. Curtis, A. De Moors, G. Erauso, C. Fletcher, P. M. K. Gordon, I. Heikamp-de Jong, A. C. Jeffries, C. J. Kozera, N. Medina, X. Peng, H. P. Thi-Ngoc, P. Redder, M. E. Schenk, C. Theriault, N. Tolstrup, R. L. Charlebois, W. F. Doolittle, M. Duguet, T. Gaasterland, R. A. Garrett, M. A. Ragan, C. W. Sensen, and J. Van der Oost. 2001. The complete genome of the crenarchaeon Sulfolobus solfataricus P2. Proc. Natl. Acad. Sci. USA 98:7835-7840.
  • 44
    • 15644383855 scopus 로고    scopus 로고
    • Smith, D. R., L. A. Doucette-Stamm, C. Deloughery, H. Lee, J. Dubois, T. Aldredge, R. Bashirzadeh, D. Blakely, R. Cook, K. Gilbert, D. Harrison, L. Hoang, P. Keagle, W. Lumm, B. Pothier, D. Qiu, R. Spadafora, R. Vicaire, Y. Wang, J. Wierzbowski, R. Gibson, N. Jiwani, A. Caruso, D. Bush, H. Safer, D. Patwell, S. Prabhakar, S. McDougall, G. Shimer, A. Goyal, S. Pietrokovski, G. M. Church, C. J. Daniels, J. Mao, P. Rice, J. Nölling, and J. N. Reeve. 1997. Complete genome sequence of Methanobacterium thermoautotrophicum ΔH: functional analysis and comparative genomics. J. Bacteriol. 179:7135-7155.
    • Smith, D. R., L. A. Doucette-Stamm, C. Deloughery, H. Lee, J. Dubois, T. Aldredge, R. Bashirzadeh, D. Blakely, R. Cook, K. Gilbert, D. Harrison, L. Hoang, P. Keagle, W. Lumm, B. Pothier, D. Qiu, R. Spadafora, R. Vicaire, Y. Wang, J. Wierzbowski, R. Gibson, N. Jiwani, A. Caruso, D. Bush, H. Safer, D. Patwell, S. Prabhakar, S. McDougall, G. Shimer, A. Goyal, S. Pietrokovski, G. M. Church, C. J. Daniels, J. Mao, P. Rice, J. Nölling, and J. N. Reeve. 1997. Complete genome sequence of Methanobacterium thermoautotrophicum ΔH: functional analysis and comparative genomics. J. Bacteriol. 179:7135-7155.
  • 45
    • 0036484726 scopus 로고    scopus 로고
    • Sulfolobus tokodaii sp. nov. (f. Sulfolobus sp. strain 7), a new member of the genus Sulfolobus isolated from Beppu Hot Springs, Japan
    • Suzuki, T., T. Iwasaki, T. Uzawa, K. Hara, N. Nemoto, T. Kon, T. Ueki, A. Yamagishi, and T. Oshima. 2002. Sulfolobus tokodaii sp. nov. (f. Sulfolobus sp. strain 7), a new member of the genus Sulfolobus isolated from Beppu Hot Springs, Japan. Extremophiles 6:39-44.
    • (2002) Extremophiles , vol.6 , pp. 39-44
    • Suzuki, T.1    Iwasaki, T.2    Uzawa, T.3    Hara, K.4    Nemoto, N.5    Kon, T.6    Ueki, T.7    Yamagishi, A.8    Oshima, T.9
  • 46
    • 0035108129 scopus 로고    scopus 로고
    • Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens
    • Thomas, T., N. Kumar, and R. Cavicchioli. 2001. Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens. J. Bacteriol. 183:1974-1982.
    • (2001) J. Bacteriol , vol.183 , pp. 1974-1982
    • Thomas, T.1    Kumar, N.2    Cavicchioli, R.3
  • 47
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.