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Volumn 30, Issue 6, 2006, Pages 872-905

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species

Author keywords

Functional genomics; Hyperthermophiles; Thermotoga

Indexed keywords

ARABINOSE; BACTERIAL PROTEIN; BETA 1,3 GLUCAN; BETA 1,6 GLUCAN; CARBOHYDRATE; CHITIN; GLUCOSE; IRON SULFUR PROTEIN; MANNAN; MANNOSE; PECTIN; POLYSACCHARIDE; RHAMNOSE; RIBOSE; XYLAN; XYLOSE;

EID: 33750041322     PISSN: 01686445     EISSN: 15746976     Source Type: Journal    
DOI: 10.1111/j.1574-6976.2006.00039.x     Document Type: Review
Times cited : (101)

References (288)
  • 1
    • 2442458877 scopus 로고    scopus 로고
    • The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases
    • Alberto F, Bignon C, Sulzenbacher G, Henrissat B & Czjzek M (2004) The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases. J Biol Chem 279: 18903-18910.
    • (2004) J Biol Chem , vol.279 , pp. 18903-18910
    • Alberto, F.1    Bignon, C.2    Sulzenbacher, G.3    Henrissat, B.4    Czjzek, M.5
  • 2
    • 34248390126 scopus 로고    scopus 로고
    • Physiological function of the maltose operon regulator, MalR, in Lactococcus lactis
    • Andersson U & Radstrom P (2002) Physiological function of the maltose operon regulator, MalR, in Lactococcus lactis. BMC Microbiol 2: 28.
    • (2002) BMC Microbiol , vol.2 , pp. 28
    • Andersson, U.1    Radstrom, P.2
  • 3
    • 3142765952 scopus 로고    scopus 로고
    • Crystal structure of an orphan protein (TM0875) from Thermotoga maritima at 2.00-Å resolution reveals a new fold
    • Bakolitsa C, Schwarzenbacher R, McMullan D et al. (2004) Crystal structure of an orphan protein (TM0875) from Thermotoga maritima at 2.00-Å resolution reveals a new fold. Proteins 56: 607-610.
    • (2004) Proteins , vol.56 , pp. 607-610
    • Bakolitsa, C.1    Schwarzenbacher, R.2    McMullan, D.3
  • 4
    • 0036021956 scopus 로고    scopus 로고
    • Thermotoga lettingae sp. nov., a novel thermophilic, methanol-degrading bacterium isolated from a thermophilic anaerobic reactor
    • Balk M, Weijma J & Stams AJ (2002) Thermotoga lettingae sp. nov., a novel thermophilic, methanol-degrading bacterium isolated from a thermophilic anaerobic reactor. Int J Syst Evol Microbiol 52: 1361-1368.
    • (2002) Int J Syst Evol Microbiol , vol.52 , pp. 1361-1368
    • Balk, M.1    Weijma, J.2    Stams, A.J.3
  • 5
    • 33644957243 scopus 로고    scopus 로고
    • Identification and characterization of a novel intracellular alkaline alpha-amylase from the hyperthermophilic bacterium Thermotoga maritima MSB8
    • Ballschmiter M, Futterer O & Liebl W (2006) Identification and characterization of a novel intracellular alkaline alpha-amylase from the hyperthermophilic bacterium Thermotoga maritima MSB8. Appl Environ Microbiol 72: 2206-2211.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 2206-2211
    • Ballschmiter, M.1    Futterer, O.2    Liebl, W.3
  • 6
    • 0037145330 scopus 로고    scopus 로고
    • Glucose-to-fructose conversion at high temperatures with xylose (glucose) isomerases from Streptomyces murinus and two hyperthermophilic Thermotoga species
    • Bandlish RK, Michael Hess J, Epting KL, Vieille C & Kelly RM (2002) Glucose-to-fructose conversion at high temperatures with xylose (glucose) isomerases from Streptomyces murinus and two hyperthermophilic Thermotoga species. Biotechnol Bioeng 80: 185-194.
    • (2002) Biotechnol Bioeng , vol.80 , pp. 185-194
    • Bandlish, R.K.1    Michael Hess, J.2    Epting, K.L.3    Vieille, C.4    Kelly, R.M.5
  • 7
    • 23344453820 scopus 로고    scopus 로고
    • Iron and Pseudomonas aeruginosa biofilm formation
    • Banin E, Vasil ML & Greenberg EP (2005) Iron and Pseudomonas aeruginosa biofilm formation. Proc Natl Acad Sci USA 102: 11076-11081.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11076-11081
    • Banin, E.1    Vasil, M.L.2    Greenberg, E.P.3
  • 8
    • 0027403763 scopus 로고
    • The sigma B-dependent promoter of the Bacillus subtilis sigB operon is induced by heat shock
    • Benson AK & Haldenwang WG (1993) The sigma B-dependent promoter of the Bacillus subtilis sigB operon is induced by heat shock. J Bacteriol 175: 1929-1935.
    • (1993) J Bacteriol , vol.175 , pp. 1929-1935
    • Benson, A.K.1    Haldenwang, W.G.2
  • 9
    • 1942475365 scopus 로고    scopus 로고
    • Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states
    • Bent CJ, Isaacs NW, Mitchell TJ & Riboldi-Tunnicliffe A (2004) Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states. J Bacteriol 186: 2872-2879.
    • (2004) J Bacteriol , vol.186 , pp. 2872-2879
    • Bent, C.J.1    Isaacs, N.W.2    Mitchell, T.J.3    Riboldi-Tunnicliffe, A.4
  • 10
    • 1542496458 scopus 로고    scopus 로고
    • Thermotoga neapolitana gene clusters participating in degradation of starch and maltodextins: Molecular structure of the locus
    • Berezina OV, Lunina NA, Zverlov VV, Naumov DG, Liebl W & Velikodvorskaia GA (2003) Thermotoga neapolitana gene clusters participating in degradation of starch and maltodextins: molecular structure of the locus. Mol Biol (Mosk) 37: 801-809.
    • (2003) Mol Biol (Mosk) , vol.37 , pp. 801-809
    • Berezina, O.V.1    Lunina, N.A.2    Zverlov, V.V.3    Naumov, D.G.4    Liebl, W.5    Velikodvorskaia, G.A.6
  • 11
    • 0042667020 scopus 로고    scopus 로고
    • Thermotoga maritima IscU. Structural characterization and dynamics of a new class of metallochaperone
    • Bertini I, Cowan JA, Del Bianco C, Luchinat C & Mansy SS (2003) Thermotoga maritima IscU. Structural characterization and dynamics of a new class of metallochaperone. J Mol Biol 331: 907-924.
    • (2003) J Mol Biol , vol.331 , pp. 907-924
    • Bertini, I.1    Cowan, J.A.2    Del Bianco, C.3    Luchinat, C.4    Mansy, S.S.5
  • 12
    • 0031934403 scopus 로고    scopus 로고
    • Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima
    • Bibel M, Brettl C, Gosslar U, Kriegshauser G & Liebl W (1998) Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima. FEMS Microbiol Lett 158: 9-15.
    • (1998) FEMS Microbiol Lett , vol.158 , pp. 9-15
    • Bibel, M.1    Brettl, C.2    Gosslar, U.3    Kriegshauser, G.4    Liebl, W.5
  • 14
    • 9144231355 scopus 로고    scopus 로고
    • Crystal structures of the antitermination factor NusB from Thermotoga maritima and implications for RNA binding
    • Bonin I, Robelek R, Benecke H, Urlaub H, Bacher A, Richter G & Wahl MC (2004) Crystal structures of the antitermination factor NusB from Thermotoga maritima and implications for RNA binding. Biochem J 383: 419-428.
    • (2004) Biochem J , vol.383 , pp. 419-428
    • Bonin, I.1    Robelek, R.2    Benecke, H.3    Urlaub, H.4    Bacher, A.5    Richter, G.6    Wahl, M.C.7
  • 15
    • 0035807792 scopus 로고    scopus 로고
    • beta-1,3-Glucan binding by a thermostable carbohydrate binding module from Thermotoga maritima
    • Boraston AB, Warren RA & Kilburn DG (2001) beta-1,3-Glucan binding by a thermostable carbohydrate binding module from Thermotoga maritima. Biochemistry (Moscow) 40: 14679-14685.
    • (2001) Biochemistry (Moscow) , vol.40 , pp. 14679-14685
    • Boraston, A.B.1    Warren, R.A.2    Kilburn, D.G.3
  • 16
    • 0037297578 scopus 로고    scopus 로고
    • Crystal structure of a zinc-containing glycerol dehydrogenase (TM0423) from Thermotoga maritima at 1.5 Å resolution
    • Brinen LS, Canaves JM, Dai X et al. (2003) Crystal structure of a zinc-containing glycerol dehydrogenase (TM0423) from Thermotoga maritima at 1.5 Å resolution. Proteins 50: 371-374.
    • (2003) Proteins , vol.50 , pp. 371-374
    • Brinen, L.S.1    Canaves, J.M.2    Dai, X.3
  • 17
    • 0028924376 scopus 로고
    • Purification of Thermotoga maritima enzymes for the degradation of cellulosic materials
    • Bronnenmeier K, Kern A, Liebl W & Staudenbauer WL (1995) Purification of Thermotoga maritima enzymes for the degradation of cellulosic materials. Appl Environ Microbiol 61: 1399-1407.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1399-1407
    • Bronnenmeier, K.1    Kern, A.2    Liebl, W.3    Staudenbauer, W.L.4
  • 18
    • 0036646105 scopus 로고    scopus 로고
    • Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG
    • Brown PN, Hill CP & Blair DF (2002) Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG. EMBO J 21: 3225-3234.
    • (2002) EMBO J , vol.21 , pp. 3225-3234
    • Brown, P.N.1    Hill, C.P.2    Blair, D.F.3
  • 19
    • 16844367441 scopus 로고    scopus 로고
    • Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima
    • Brown PN, Mathews MA, Joss LA, Hill CP & Blair DF (2005) Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima. J Bacteriol 187: 2890-2902.
    • (2005) J Bacteriol , vol.187 , pp. 2890-2902
    • Brown, P.N.1    Mathews, M.A.2    Joss, L.A.3    Hill, C.P.4    Blair, D.F.5
  • 20
    • 0031579663 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence and expression of a mannitol dehydrogenase gene from Pseudomonas fluorescens DSM 50106 in Escherichia coli
    • Brunker P, Altenbuchner J, Kulbe KD &Mattes R (1997) Cloning, nucleotide sequence and expression of a mannitol dehydrogenase gene from Pseudomonas fluorescens DSM 50106 in Escherichia coli. Biochim Biophys Acta 1351: 157-167.
    • (1997) Biochim Biophys Acta , vol.1351 , pp. 157-167
    • Brunker, P.1    Altenbuchner, J.2    Kulbe, K.D.3    Mattes, R.4
  • 22
    • 2642546571 scopus 로고    scopus 로고
    • Predicted role for the archease protein family based on structural and sequence analysis of TM1083 and MTH1598, two proteins structurally characterized through structural genomics efforts
    • Canaves JM (2004) Predicted role for the archease protein family based on structural and sequence analysis of TM1083 and MTH1598, two proteins structurally characterized through structural genomics efforts. Proteins 56: 19-27.
    • (2004) Proteins , vol.56 , pp. 19-27
    • Canaves, J.M.1
  • 24
    • 0036154307 scopus 로고    scopus 로고
    • Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- And mannan-based polysaccharides
    • Chhabra SR, Shockley KR, Ward DE & Kelly RM (2002) Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides. Appl Environ Microbiol 68: 545-554.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 545-554
    • Chhabra, S.R.1    Shockley, K.R.2    Ward, D.E.3    Kelly, R.M.4
  • 25
    • 0037470149 scopus 로고    scopus 로고
    • Carbohydrate-induced differential gene expression patterns in the hyperthermophilic bacterium Thermotoga maritima
    • Chhabra SR, Shockley KR, Conners SB, Scott KL, Wolfinger RD & Kelly RM (2003) Carbohydrate-induced differential gene expression patterns in the hyperthermophilic bacterium Thermotoga maritima. J Biol Chem 278: 7540-7552.
    • (2003) J Biol Chem , vol.278 , pp. 7540-7552
    • Chhabra, S.R.1    Shockley, K.R.2    Conners, S.B.3    Scott, K.L.4    Wolfinger, R.D.5    Kelly, R.M.6
  • 26
    • 0041821240 scopus 로고    scopus 로고
    • High-resolution X-ray structure of the DNA-binding protein HU from the hyper-thermophilic Thermotoga maritima and the determinants of its thermostability
    • Christodoulou E, Rypniewski WR & Vorgias CR (2003) High-resolution X-ray structure of the DNA-binding protein HU from the hyper-thermophilic Thermotoga maritima and the determinants of its thermostability. Extremophiles 7: 111-122.
    • (2003) Extremophiles , vol.7 , pp. 111-122
    • Christodoulou, E.1    Rypniewski, W.R.2    Vorgias, C.R.3
  • 27
    • 0022617696 scopus 로고
    • The nucleotide sequence of the malT gene encoding the positive regulator of the Escherichia coli maltose regulon
    • Cole ST & Raibaud O (1986) The nucleotide sequence of the malT gene encoding the positive regulator of the Escherichia coli maltose regulon. Gene 42: 201-208.
    • (1986) Gene , vol.42 , pp. 201-208
    • Cole, S.T.1    Raibaud, O.2
  • 28
    • 23044507033 scopus 로고    scopus 로고
    • NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima
    • Columbus L, Peti W, Etezady-Esfarjani T, Herrmann T & Wuthrich K (2005) NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima. Proteins 60: 552-557.
    • (2005) Proteins , vol.60 , pp. 552-557
    • Columbus, L.1    Peti, W.2    Etezady-Esfarjani, T.3    Herrmann, T.4    Wuthrich, K.5
  • 30
    • 27144509128 scopus 로고    scopus 로고
    • An expression-driven approach to the prediction of carbohydrate transport and utilization regulons in the hyperthermophilic bacterium Thermotoga maritima
    • Conners SB, Montero CI, Comfort DA, Shockley KR, Johnson MR, Chhabra SR & Kelly RM (2005) An expression-driven approach to the prediction of carbohydrate transport and utilization regulons in the hyperthermophilic bacterium Thermotoga maritima. J Bacteriol 187: 7267-7282.
    • (2005) J Bacteriol , vol.187 , pp. 7267-7282
    • Conners, S.B.1    Montero, C.I.2    Comfort, D.A.3    Shockley, K.R.4    Johnson, M.R.5    Chhabra, S.R.6    Kelly, R.M.7
  • 32
    • 0034737320 scopus 로고    scopus 로고
    • The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability
    • Dams T, Auerbach G, Bader G, Jacob U, Ploom T, Huber R & Jaenicke R (2000) The crystal structure of dihydrofolate reductase from Thermotoga maritima: molecular features of thermostability. J Mol Biol 297: 659-672.
    • (2000) J Mol Biol , vol.297 , pp. 659-672
    • Dams, T.1    Auerbach, G.2    Bader, G.3    Jacob, U.4    Ploom, T.5    Huber, R.6    Jaenicke, R.7
  • 33
    • 33645313846 scopus 로고    scopus 로고
    • Chromosome evolution in the Thermotogales: Large-scale inversions and strain diversification of CRISPR sequences
    • DeBoy RT, Mongodin EF, Emerson JB & Nelson KE (2006) Chromosome evolution in the Thermotogales: large-scale inversions and strain diversification of CRISPR sequences. J Bacteriol 188: 2364-2374.
    • (2006) J Bacteriol , vol.188 , pp. 2364-2374
    • DeBoy, R.T.1    Mongodin, E.F.2    Emerson, J.B.3    Nelson, K.E.4
  • 35
    • 3543070000 scopus 로고    scopus 로고
    • A scaleable and integrated crystallization pipeline applied to mining the Thermotoga maritima proteome
    • DiDonato M, Deacon AM, Klock HE, McMullan D & Lesley SA (2004) A scaleable and integrated crystallization pipeline applied to mining the Thermotoga maritima proteome. J Struct Funct Genomics 5: 133-146.
    • (2004) J Struct Funct Genomics , vol.5 , pp. 133-146
    • DiDonato, M.1    Deacon, A.M.2    Klock, H.E.3    McMullan, D.4    Lesley, S.A.5
  • 36
    • 0035158003 scopus 로고    scopus 로고
    • Thermotoga maritima phosphofructokinases: Expression and characterization of two unique enzymes
    • Ding YR, Ronimus RS & Morgan HW (2001) Thermotoga maritima phosphofructokinases: expression and characterization of two unique enzymes. J Bacteriol 183: 791-794.
    • (2001) J Bacteriol , vol.183 , pp. 791-794
    • Ding, Y.R.1    Ronimus, R.S.2    Morgan, H.W.3
  • 37
    • 18844478534 scopus 로고    scopus 로고
    • The hexokinase of the hyperthermophile Thermoproteus tenax. ATP-dependent hexokinases and ADP-dependent glucokinases, teo alternatives for glucose phosphorylation in Archaea
    • Dorr C, Zaparty M, Tjaden B, Brinkmann H & Siebers B (2003) The hexokinase of the hyperthermophile Thermoproteus tenax. ATP-dependent hexokinases and ADP-dependent glucokinases, teo alternatives for glucose phosphorylation in Archaea. J Biol Chem 278: 18744-18753.
    • (2003) J Biol Chem , vol.278 , pp. 18744-18753
    • Dorr, C.1    Zaparty, M.2    Tjaden, B.3    Brinkmann, H.4    Siebers, B.5
  • 38
    • 0031023550 scopus 로고    scopus 로고
    • Purification and characterization of extremely thermostable beta-mannanase, beta-mannosidase, and alpha-galactosidase from the hyperthermophilic eubacterium Thermotoga neapolitana 5068
    • Duffaud GD, McCutchen CM, Leduc P, Parker KN & Kelly RM (1997) Purification and characterization of extremely thermostable beta-mannanase, beta-mannosidase, and alpha-galactosidase from the hyperthermophilic eubacterium Thermotoga neapolitana 5068. Appl Environ Microbiol 63: 169-177.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 169-177
    • Duffaud, G.D.1    McCutchen, C.M.2    Leduc, P.3    Parker, K.N.4    Kelly, R.M.5
  • 39
    • 0037047102 scopus 로고    scopus 로고
    • The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium
    • Eisen JA, Nelson KE, Paulsen IT et al. (2002) The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium. Proc Natl Acad Sci USA 99: 9509-9514.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9509-9514
    • Eisen, J.A.1    Nelson, K.E.2    Paulsen, I.T.3
  • 40
    • 0035057117 scopus 로고    scopus 로고
    • Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters
    • Elferink MG, Albers SV, Konings WN & Driessen AJ (2001) Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters. Mol Microbiol 39: 1494-1503.
    • (2001) Mol Microbiol , vol.39 , pp. 1494-1503
    • Elferink, M.G.1    Albers, S.V.2    Konings, W.N.3    Driessen, A.J.4
  • 41
    • 10744227536 scopus 로고    scopus 로고
    • Crystal structure of an HEPN domain protein (TM0613) from Thermotoga maritima at 1.75 Å resolution
    • Erlandsen H, Canaves JM, Elsliger MA et al. (2004) Crystal structure of an HEPN domain protein (TM0613) from Thermotoga maritima at 1.75 Å resolution. Proteins 54: 806-809.
    • (2004) Proteins , vol.54 , pp. 806-809
    • Erlandsen, H.1    Canaves, J.M.2    Elsliger, M.A.3
  • 42
    • 6944253324 scopus 로고    scopus 로고
    • NMR assignment of TM1442, a putative anti-sigma factor antagonist from Thermotoga maritima
    • Etezady-Esfarjani T & Wuthrich K (2004) NMR assignment of TM1442, a putative anti-sigma factor antagonist from Thermotoga maritima. J Biomol NMR 29: 99-100.
    • (2004) J Biomol NMR , vol.29 , pp. 99-100
    • Etezady-Esfarjani, T.1    Wuthrich, K.2
  • 43
    • 0037328545 scopus 로고    scopus 로고
    • NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima
    • Etezady-Esfarjani T, Peti W & Wuthrich K (2003) NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima. J Biomol NMR 25: 167-168.
    • (2003) J Biomol NMR , vol.25 , pp. 167-168
    • Etezady-Esfarjani, T.1    Peti, W.2    Wuthrich, K.3
  • 44
    • 3042796495 scopus 로고    scopus 로고
    • NMR structure determination of the hypothetical protein TM1290 from Thermotoga maritima using automated NOESYanalysis
    • Etezady-Esfarjani T, Herrmann T, Peti W, Klock HE, Lesley SA & Wuthrich K (2004) NMR structure determination of the hypothetical protein TM1290 from Thermotoga maritima using automated NOESYanalysis. J Biomol NMR 29: 403-406.
    • (2004) J Biomol NMR , vol.29 , pp. 403-406
    • Etezady-Esfarjani, T.1    Herrmann, T.2    Peti, W.3    Klock, H.E.4    Lesley, S.A.5    Wuthrich, K.6
  • 46
    • 2442697909 scopus 로고    scopus 로고
    • Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinolphosphate aminotransferase
    • Fernandez FJ, Vega MC, Lehmann F, Sandmeier E, Gehring H, Christen P & Wilmanns M (2004) Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinolphosphate aminotransferase. J Biol Chem 279: 21478-21488.
    • (2004) J Biol Chem , vol.279 , pp. 21478-21488
    • Fernandez, F.J.1    Vega, M.C.2    Lehmann, F.3    Sandmeier, E.4    Gehring, H.5    Christen, P.6    Wilmanns, M.7
  • 47
    • 0037329109 scopus 로고    scopus 로고
    • Parallel evolution of ligand specificity between LacI/GalR family repressors and periplasmic sugar-binding proteins
    • Fukami-Kobayashi K, Tateno Y & Nishikawa K (2003) Parallel evolution of ligand specificity between LacI/GalR family repressors and periplasmic sugar-binding proteins. Mol Biol Evol 20: 267-277.
    • (2003) Mol Biol Evol , vol.20 , pp. 267-277
    • Fukami-Kobayashi, K.1    Tateno, Y.2    Nishikawa, K.3
  • 48
    • 0029778801 scopus 로고    scopus 로고
    • The glucose transport system of the hyperthermophilic anaerobic bacterium Thermotoga neapolitana
    • Galperin MY, Noll KM & Romano AH (1996) The glucose transport system of the hyperthermophilic anaerobic bacterium Thermotoga neapolitana. Appl Environ Microbiol 62: 2915-2918.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 2915-2918
    • Galperin, M.Y.1    Noll, K.M.2    Romano, A.H.3
  • 49
    • 0031030475 scopus 로고    scopus 로고
    • Coregulation of beta-galactoside uptake and hydrolysis by the hyperthermophilic bacterium Thermotoga neapolitana
    • Galperin MY, Noll KM & Romano AH (1997) Coregulation of beta-galactoside uptake and hydrolysis by the hyperthermophilic bacterium Thermotoga neapolitana. Appl Environ Microbiol 63: 969-972.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 969-972
    • Galperin, M.Y.1    Noll, K.M.2    Romano, A.H.3
  • 50
    • 0038317570 scopus 로고    scopus 로고
    • Growth of hyperthermophilic archaeon Pyrococcus furiosus on chitin involves two family 18 chitinases
    • Gao J, Bauer MW, Shockley KR, Pysz MA & Kelly RM (2003) Growth of hyperthermophilic archaeon Pyrococcus furiosus on chitin involves two family 18 chitinases. Appl Environ Microbiol 69: 3119-3128.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 3119-3128
    • Gao, J.1    Bauer, M.W.2    Shockley, K.R.3    Pysz, M.A.4    Kelly, R.M.5
  • 51
    • 4744349524 scopus 로고    scopus 로고
    • Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation
    • Garcia B, Latasa C, Solano C, Garcia-del Portillo F, Gamazo C & Lasa I (2004) Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation. Mol Microbiol 54: 264-277.
    • (2004) Mol Microbiol , vol.54 , pp. 264-277
    • Garcia, B.1    Latasa, C.2    Solano, C.3    Garcia-del Portillo, F.4    Gamazo, C.5    Lasa, I.6
  • 52
    • 19944428553 scopus 로고    scopus 로고
    • A novel member of the YchN-like fold: A novel member of the YchN-like fold: Solution structure of the hypothetical protein TM0979 from Thermotoga maritima
    • Gaspar JA, Liu C, Vassall KA et al. (2005) A novel member of the YchN-like fold: A novel member of the YchN-like fold: Solution structure of the hypothetical protein TM0979 from Thermotoga maritima. Protein Sci 14: 216-223.
    • (2005) Protein Sci , vol.14 , pp. 216-223
    • Gaspar, J.A.1    Liu, C.2    Vassall, K.A.3
  • 53
    • 0032146071 scopus 로고    scopus 로고
    • Molecular analysis of the malR gene of Clostridium butyricum NCIMB 7423, a member of the LacI-GalR family of repressor proteins
    • Goda SK, Eisa O, Akhter M & Minton NP (1998) Molecular analysis of the malR gene of Clostridium butyricum NCIMB 7423, a member of the LacI-GalR family of repressor proteins. FEMS Microbiol Lett 165: 193-200.
    • (1998) FEMS Microbiol Lett , vol.165 , pp. 193-200
    • Goda, S.K.1    Eisa, O.2    Akhter, M.3    Minton, N.P.4
  • 54
    • 0021225289 scopus 로고
    • The htpR gene product of E. coli is a sigma factor for heat-shock promoters
    • Grossman AD, Erickson JW & Gross CA (1984) The htpR gene product of E. coli is a sigma factor for heat-shock promoters. Cell 38: 383-390.
    • (1984) Cell , vol.38 , pp. 383-390
    • Grossman, A.D.1    Erickson, J.W.2    Gross, C.A.3
  • 55
    • 0036515152 scopus 로고    scopus 로고
    • The endopolysaccharide metabolism of the hyperthermophilic archeon Thermococcus hydrothermalis: Polymer structure and biosynthesis
    • Gruyer S, Legin E, Bliard C, Ball S & Duchiron F (2002) The endopolysaccharide metabolism of the hyperthermophilic archeon Thermococcus hydrothermalis: polymer structure and biosynthesis. Curr Microbiol 44: 206-211.
    • (2002) Curr Microbiol , vol.44 , pp. 206-211
    • Gruyer, S.1    Legin, E.2    Bliard, C.3    Ball, S.4    Duchiron, F.5
  • 56
    • 1042301374 scopus 로고    scopus 로고
    • Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic Thermotoga maritima and mechanism of product chain length determination
    • Guo RT, Kuo CJ, Chou CC, Ko TP, Shr HL, Liang PH & Wang AH (2004) Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic Thermotoga maritima and mechanism of product chain length determination. J Biol Chem 279: 4903-4912.
    • (2004) J Biol Chem , vol.279 , pp. 4903-4912
    • Guo, R.T.1    Kuo, C.J.2    Chou, C.C.3    Ko, T.P.4    Shr, H.L.5    Liang, P.H.6    Wang, A.H.7
  • 57
    • 0035121756 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of the TM1442 gene product from Thermotoga maritima, a homologue of Bacillus subtilis anti-anti-sigma factors
    • Ha KS, Kwak JE, Han BW, Lee JY, Moon J, Lee BI & Suh SW (2001) Crystallization and preliminary X-ray crystallographic analysis of the TM1442 gene product from Thermotoga maritima, a homologue of Bacillus subtilis anti-anti-sigma factors. Acta Crystallogr D Biol Crystallogr 57: 276-278.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 276-278
    • Ha, K.S.1    Kwak, J.E.2    Han, B.W.3    Lee, J.Y.4    Moon, J.5    Lee, B.I.6    Suh, S.W.7
  • 58
    • 0642285645 scopus 로고    scopus 로고
    • ATP-dependent glucokinase from the hyperthermophilic bacterium Thermotoga maritima represents an extremely thermophilic ROK glucokinase with high substrate specificity
    • Hansen T & Schonheit P (2003) ATP-dependent glucokinase from the hyperthermophilic bacterium Thermotoga maritima represents an extremely thermophilic ROK glucokinase with high substrate specificity. FEMS Microbiol Lett 226: 405-411.
    • (2003) FEMS Microbiol Lett , vol.226 , pp. 405-411
    • Hansen, T.1    Schonheit, P.2
  • 59
    • 0036837983 scopus 로고    scopus 로고
    • The first archaeal ATP-dependent glucokinase, from the hyperthermophilic crenarchaeon Aeropyrum pernix, represents a monomeric, extremely thermophilic ROK glucokinase with broad hexose specificity
    • Hansen T, Reichstein B, Schmid R & Schonheit P (2002) The first archaeal ATP-dependent glucokinase, from the hyperthermophilic crenarchaeon Aeropyrum pernix, represents a monomeric, extremely thermophilic ROK glucokinase with broad hexose specificity. J Bacteriol 184: 5955-5965.
    • (2002) J Bacteriol , vol.184 , pp. 5955-5965
    • Hansen, T.1    Reichstein, B.2    Schmid, R.3    Schonheit, P.4
  • 60
    • 0028278946 scopus 로고
    • A cryptic miniplasmid from the hyperthermophilic bacterium Thermotoga sp. strain RQ7
    • Harriott OT, Huber R, Stetter KO, Betts PW & Noll KM (1994) A cryptic miniplasmid from the hyperthermophilic bacterium Thermotoga sp. strain RQ7. J Bacteriol 176: 2759-2762.
    • (1994) J Bacteriol , vol.176 , pp. 2759-2762
    • Harriott, O.T.1    Huber, R.2    Stetter, K.O.3    Betts, P.W.4    Noll, K.M.5
  • 61
    • 3042848356 scopus 로고    scopus 로고
    • Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 Å resolution
    • Heine A, Canaves JM, von Delft F et al. (2004) Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 Å resolution. Proteins 56: 387-391.
    • (2004) Proteins , vol.56 , pp. 387-391
    • Heine, A.1    Canaves, J.M.2    Von Delft, F.3
  • 62
    • 0037040937 scopus 로고    scopus 로고
    • A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role
    • Hettwer S & Sterner R (2002) A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role. J Biol Chem 277: 8194-8201.
    • (2002) J Biol Chem , vol.277 , pp. 8194-8201
    • Hettwer, S.1    Sterner, R.2
  • 63
    • 0032989815 scopus 로고    scopus 로고
    • Post-transcriptional regulation of the Bacillus subtilis dnaK operon
    • Homuth G, Mogk A & Schumann W (1999) Post-transcriptional regulation of the Bacillus subtilis dnaK operon. Mol Microbiol 32: 1183-1197.
    • (1999) Mol Microbiol , vol.32 , pp. 1183-1197
    • Homuth, G.1    Mogk, A.2    Schumann, W.3
  • 64
    • 36849044887 scopus 로고    scopus 로고
    • (Dworkin MW, ed), Springer-Verlag, New York
    • Huber RW & Hannig M (2004) Thermotogales (Dworkin MW, ed), Springer-Verlag, New York (http://link.springer-ny.com/link/service/books/10125/ ).
    • (2004) Thermotogales
    • Huber, R.W.1    Hannig, M.2
  • 65
    • 0022522022 scopus 로고
    • Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C
    • Huber R, Langworthy TA, Konig H, Thomm M, Woese CR, Sleytr UB & Stetter KO (1986) Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C. Arch Microbiol 144: 324-333.
    • (1986) Arch Microbiol , vol.144 , pp. 324-333
    • Huber, R.1    Langworthy, T.A.2    Konig, H.3    Thomm, M.4    Woese, C.R.5    Sleytr, U.B.6    Stetter, K.O.7
  • 66
    • 0035788440 scopus 로고    scopus 로고
    • Two transporters, TogT and TogMNAB, are responsible for oligogalacturonide uptake in Erwinia chrysanthemi 3937
    • Hugouvieux-Cotte-Pattat N & Reverchon S (2001) Two transporters, TogT and TogMNAB, are responsible for oligogalacturonide uptake in Erwinia chrysanthemi 3937. Mol Microbiol 41: 1125-1132.
    • (2001) Mol Microbiol , vol.41 , pp. 1125-1132
    • Hugouvieux-Cotte-Pattat, N.1    Reverchon, S.2
  • 67
    • 0035788642 scopus 로고    scopus 로고
    • Identification of TogMNAB, an ABC transporter which mediates the uptake of pectic oligomers in Erwinia chrysanthemi 3937
    • Hugouvieux-Cotte-Pattat N, Blot N & Reverchon S (2001) Identification of TogMNAB, an ABC transporter which mediates the uptake of pectic oligomers in Erwinia chrysanthemi 3937. Mol Microbiol 41: 1113-1123.
    • (2001) Mol Microbiol , vol.41 , pp. 1113-1123
    • Hugouvieux-Cotte-Pattat, N.1    Blot, N.2    Reverchon, S.3
  • 69
    • 24744452693 scopus 로고    scopus 로고
    • Domain reorientation and induced fit upon RNA binding: Solution structure and dynamics of ribosomal protein L11 from Thermotoga maritima
    • Ilin S, Hoskins A, Ohlenschlager O, Jonker HR, Schwalbe H & Wohnert J (2005) Domain reorientation and induced fit upon RNA binding: solution structure and dynamics of ribosomal protein L11 from Thermotoga maritima. Chembiochem 6: 1611-1618.
    • (2005) Chembiochem , vol.6 , pp. 1611-1618
    • Ilin, S.1    Hoskins, A.2    Ohlenschlager, O.3    Jonker, H.R.4    Schwalbe, H.5    Wohnert, J.6
  • 70
    • 17144378531 scopus 로고    scopus 로고
    • Crystal structure of the tRNA 30 processing endoribonuclease tRNase Z from Thermotoga maritima
    • Ishii R, Minagawa A, Takaku H, Takagi M, Nashimoto M & Yokoyama S (2005) Crystal structure of the tRNA 30 processing endoribonuclease tRNase Z from Thermotoga maritima. J Biol Chem 280: 14138-14144.
    • (2005) J Biol Chem , vol.280 , pp. 14138-14144
    • Ishii, R.1    Minagawa, A.2    Takaku, H.3    Takagi, M.4    Nashimoto, M.5    Yokoyama, S.6
  • 71
    • 0001218383 scopus 로고
    • Thermotoga neapolitana sp. nov. of the extremely thermophilic, eubacterial genus Thermotoga
    • Jannasch HW, Huber R, Belkin S & Stetter KO (1988) Thermotoga neapolitana sp. nov. of the extremely thermophilic, eubacterial genus Thermotoga. Arch Microbiol 150: 103-104.
    • (1988) Arch Microbiol , vol.150 , pp. 103-104
    • Jannasch, H.W.1    Huber, R.2    Belkin, S.3    Stetter, K.O.4
  • 72
    • 0036267740 scopus 로고    scopus 로고
    • Identification of genes that are associated with DNA repeats in prokaryotes
    • Jansen R, Embden JD, Gaastra W & Schouls LM (2002) Identification of genes that are associated with DNA repeats in prokaryotes. Mol Microbiol 43: 1565-1575.
    • (2002) Mol Microbiol , vol.43 , pp. 1565-1575
    • Jansen, R.1    Embden, J.D.2    Gaastra, W.3    Schouls, L.M.4
  • 73
    • 3142755485 scopus 로고    scopus 로고
    • Crystal structure of a novel manganese-containing cupin (TM1459) from Thermotoga maritima at 1.65 Å resolution
    • Jaroszewski L, Schwarzenbacher R, von Delft F et al. (2004) Crystal structure of a novel manganese-containing cupin (TM1459) from Thermotoga maritima at 1.65 Å resolution. Proteins 56: 611-614.
    • (2004) Proteins , vol.56 , pp. 611-614
    • Jaroszewski, L.1    Schwarzenbacher, R.2    Von Delft, F.3
  • 75
    • 4644368800 scopus 로고    scopus 로고
    • Transglycosylation reaction of xylanase B from the hyperthermophilic Thermotoga maritima with the ability of synthesis of tertiary alkyl beta-D-xylobiosides and xylosides
    • Jiang Z, Zhu Y, Li L, Yu X, Kusakabe I, Kitaoka M & Hayashi K (2004) Transglycosylation reaction of xylanase B from the hyperthermophilic Thermotoga maritima with the ability of synthesis of tertiary alkyl beta-D-xylobiosides and xylosides. J Biotechnol 114: 125-134.
    • (2004) J Biotechnol , vol.114 , pp. 125-134
    • Jiang, Z.1    Zhu, Y.2    Li, L.3    Yu, X.4    Kusakabe, I.5    Kitaoka, M.6    Hayashi, K.7
  • 76
    • 32644449005 scopus 로고    scopus 로고
    • Biobleach boosting effect of recombinant xylanase B from the hyperthermophilic Thermotoga maritima on wheat straw pulp
    • Jiang ZQ, Li XT, Yang SQ, Li LT, Li Y & Feng WY (2006) Biobleach boosting effect of recombinant xylanase B from the hyperthermophilic Thermotoga maritima on wheat straw pulp. Appl Microbiol Biotechnol 70: 65-71.
    • (2006) Appl Microbiol Biotechnol , vol.70 , pp. 65-71
    • Jiang, Z.Q.1    Li, X.T.2    Yang, S.Q.3    Li, L.T.4    Li, Y.5    Feng, W.Y.6
  • 77
    • 28044432945 scopus 로고    scopus 로고
    • Iron-responsive regulation of biofilm formation in Staphylococcus aureus involves Fur-dependent and Fur-independent mechanisms
    • Johnson M, Cockayne A, Williams PH & Morrissey JA (2005a) Iron-responsive regulation of biofilm formation in Staphylococcus aureus involves Fur-dependent and Fur-independent mechanisms. J Bacteriol 187: 8211-8215.
    • (2005) J Bacteriol , vol.187 , pp. 8211-8215
    • Johnson, M.1    Cockayne, A.2    Williams, P.H.3    Morrissey, J.A.4
  • 78
    • 13444272004 scopus 로고    scopus 로고
    • Population density-dependent regulation of exopolysaccharide formation in the hyperthermophilic bacterium Thermotoga maritima
    • Johnson MR, Montero CI, Conners SB, Shockley KR, Bridger SL & Kelly RM (2005b) Population density-dependent regulation of exopolysaccharide formation in the hyperthermophilic bacterium Thermotoga maritima. Mol Microbiol 55: 664-674.
    • (2005) Mol Microbiol , vol.55 , pp. 664-674
    • Johnson, M.R.1    Montero, C.I.2    Conners, S.B.3    Shockley, K.R.4    Bridger, S.L.5    Kelly, R.M.6
  • 79
    • 33644865270 scopus 로고    scopus 로고
    • The Thermotoga maritima phenotype is impacted by syntrophic interaction with Methanococcus jannaschii in hyperthermophilic coculture
    • Johnson MR, Conners SB, Montero CI, Chou CJ, Shockley KR & Kelly RM (2006) The Thermotoga maritima phenotype is impacted by syntrophic interaction with Methanococcus jannaschii in hyperthermophilic coculture. Appl Environ Microbiol 72: 811-818.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 811-818
    • Johnson, M.R.1    Conners, S.B.2    Montero, C.I.3    Chou, C.J.4    Shockley, K.R.5    Kelly, R.M.6
  • 80
    • 0034708346 scopus 로고    scopus 로고
    • Crystal structure of a NifS-like protein from Thermotoga maritima: Implications for iron sulphur cluster assembly
    • Kaiser JT, Clausen T, Bourenkow GP, Bartunik HD, Steinbacher S & Huber R (2000) Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly. J Mol Biol 297: 451-464.
    • (2000) J Mol Biol , vol.297 , pp. 451-464
    • Kaiser, J.T.1    Clausen, T.2    Bourenkow, G.P.3    Bartunik, H.D.4    Steinbacher, S.5    Huber, R.6
  • 81
    • 0042061049 scopus 로고    scopus 로고
    • Detachment of Actinobacillus actinomycetemcomitans biofilm cells by an endogenous beta-hexosaminidase activity
    • Kaplan JB, Ragunath C, Ramasubbu N & Fine DH (2003) Detachment of Actinobacillus actinomycetemcomitans biofilm cells by an endogenous beta-hexosaminidase activity. J Bacteriol 185: 4693-4698.
    • (2003) J Bacteriol , vol.185 , pp. 4693-4698
    • Kaplan, J.B.1    Ragunath, C.2    Ramasubbu, N.3    Fine, D.H.4
  • 82
    • 13844262033 scopus 로고    scopus 로고
    • c-di-GMP (3′-5′-cyclic diguanylic acid) inhibits Staphylococcus aureus cell-cell interactions and biofilm formation
    • Karaolis DK, Rashid MH, Chythanya R, Luo W, Hyodo M & Hayakawa Y (2005) c-di-GMP (3′-5′-cyclic diguanylic acid) inhibits Staphylococcus aureus cell-cell interactions and biofilm formation. Antimicrob Agents Chemother 49: 1029-1038.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 1029-1038
    • Karaolis, D.K.1    Rashid, M.H.2    Chythanya, R.3    Luo, W.4    Hyodo, M.5    Hayakawa, Y.6
  • 83
    • 0037129833 scopus 로고    scopus 로고
    • Cloning, expression and characterization of L-arabinose isomerase from Thermotoga neapolitana: Bioconversion of Dgalactose to D-tagatose using the enzyme
    • Kim BC, Lee YH, Lee HS, Lee DW, Choe EA & Pyun YR (2002) Cloning, expression and characterization of L-arabinose isomerase from Thermotoga neapolitana: bioconversion of Dgalactose to D-tagatose using the enzyme. FEMS Microbiol Lett 212: 121-126.
    • (2002) FEMS Microbiol Lett , vol.212 , pp. 121-126
    • Kim, B.C.1    Lee, Y.H.2    Lee, H.S.3    Lee, D.W.4    Choe, E.A.5    Pyun, Y.R.6
  • 84
    • 0041344457 scopus 로고    scopus 로고
    • Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture
    • Kim MS, Shin J, Lee W, Lee HS & Oh BH (2003) Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture. J Biol Chem 278: 28173-28180.
    • (2003) J Biol Chem , vol.278 , pp. 28173-28180
    • Kim, M.S.1    Shin, J.2    Lee, W.3    Lee, H.S.4    Oh, B.H.5
  • 85
    • 6344268958 scopus 로고    scopus 로고
    • Characterization of a thermostable recombinant beta-galactosidase from Thermotoga maritima
    • Kim CS, Ji ES & Oh DK (2004) Characterization of a thermostable recombinant beta-galactosidase from Thermotoga maritima. J Appl Microbiol 97: 1006-1014.
    • (2004) J Appl Microbiol , vol.97 , pp. 1006-1014
    • Kim, C.S.1    Ji, E.S.2    Oh, D.K.3
  • 86
    • 4744337730 scopus 로고    scopus 로고
    • HmsP, a putative phosphodiesterase, and HmsT, a putative diguanylate cyclase, control Hms-dependent biofilm formation in Yersinia pestis
    • Kirillina O, Fetherston JD, Bobrov AG, Abney J & Perry RD (2004) HmsP, a putative phosphodiesterase, and HmsT, a putative diguanylate cyclase, control Hms-dependent biofilm formation in Yersinia pestis. Mol Microbiol 54: 75-88.
    • (2004) Mol Microbiol , vol.54 , pp. 75-88
    • Kirillina, O.1    Fetherston, J.D.2    Bobrov, A.G.3    Abney, J.4    Perry, R.D.5
  • 87
    • 0042063909 scopus 로고    scopus 로고
    • Fusion of family 2b carbohydrate-binding module increases the catalytic activity of a xylanase from Thermotoga maritima to soluble xylan
    • Kittur FS, Mangala SL, Rus'd AA, Kitaoka M, Tsujibo H & Hayashi K (2003) Fusion of family 2b carbohydrate-binding module increases the catalytic activity of a xylanase from Thermotoga maritima to soluble xylan. FEBS Lett 549: 147-151.
    • (2003) FEBS Lett , vol.549 , pp. 147-151
    • Kittur, F.S.1    Mangala, S.L.2    Rus'D, A.A.3    Kitaoka, M.4    Tsujibo, H.5    Hayashi, K.6
  • 88
    • 0242417644 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima
    • Kluskens LD, van Alebeek GJ, Voragen AG, de Vos WM & van der Oost J (2003) Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima. Biochem J 370: 651-659.
    • (2003) Biochem J , vol.370 , pp. 651-659
    • Kluskens, L.D.1    Van Alebeek, G.J.2    Voragen, A.G.3    De Vos, W.M.4    Van Der Oost, J.5
  • 89
    • 27644594650 scopus 로고    scopus 로고
    • Characterization and mode of action of an exopolygalacturonase from the hyperthermophilic bacterium Thermotoga maritima
    • Kluskens LD, van Alebeek GJ, Walther J, Voragen AG, de Vos WM & van der Oost J (2005) Characterization and mode of action of an exopolygalacturonase from the hyperthermophilic bacterium Thermotoga maritima. FEBS J 272: 5464-5473.
    • (2005) FEBS J , vol.272 , pp. 5464-5473
    • Kluskens, L.D.1    Van Alebeek, G.J.2    Walther, J.3    Voragen, A.G.4    De Vos, W.M.5    Van Der Oost, J.6
  • 90
    • 0037041035 scopus 로고    scopus 로고
    • The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges
    • Knochel T, Pappenberger A, Jansonius JN & Kirschner K (2002) The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges. J Biol Chem 277: 8626-8634.
    • (2002) J Biol Chem , vol.277 , pp. 8626-8634
    • Knochel, T.1    Pappenberger, A.2    Jansonius, J.N.3    Kirschner, K.4
  • 91
    • 0034885332 scopus 로고    scopus 로고
    • Cellobiose uptake in the hyperthermophilic archaeon Pyrococcus furiosus is mediated by an inducible, high-affinity ABC transporter
    • Koning SM, Elferink MG, Konings WN & Driessen AJ (2001) Cellobiose uptake in the hyperthermophilic archaeon Pyrococcus furiosus is mediated by an inducible, high-affinity ABC transporter. J Bacteriol 183: 4979-4984.
    • (2001) J Bacteriol , vol.183 , pp. 4979-4984
    • Koning, S.M.1    Elferink, M.G.2    Konings, W.N.3    Driessen, A.J.4
  • 93
    • 0342948726 scopus 로고    scopus 로고
    • Pullulanase from the hyperthermophilic bacterium Thermotoga maritima: Purification by beta-cyclodextrin affinity chromatography
    • Kriegshauser G & Liebl W (2000) Pullulanase from the hyperthermophilic bacterium Thermotoga maritima: purification by beta-cyclodextrin affinity chromatography. J Chromatogr B Biomed Sci Appl 737: 245-251.
    • (2000) J Chromatogr B Biomed Sci Appl , vol.737 , pp. 245-251
    • Kriegshauser, G.1    Liebl, W.2
  • 94
    • 0028223185 scopus 로고
    • Glucose kinase has a regulatory role in carbon catabolite repression in Streptomyces coelicolor
    • Kwakman JH & Postma PW (1994) Glucose kinase has a regulatory role in carbon catabolite repression in Streptomyces coelicolor. J Bacteriol 176: 2694-2698.
    • (1994) J Bacteriol , vol.176 , pp. 2694-2698
    • Kwakman, J.H.1    Postma, P.W.2
  • 95
    • 0034669517 scopus 로고    scopus 로고
    • Analysis of the Thermotoga maritima genome combining a variety of sequence similarity and genome context tools
    • Kyrpides NC, Ouzounis CA, Iliopoulos I, Vonstein V & Overbeek R (2000) Analysis of the Thermotoga maritima genome combining a variety of sequence similarity and genome context tools. Nucleic Acids Res 28: 4573-4576.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4573-4576
    • Kyrpides, N.C.1    Ouzounis, C.A.2    Iliopoulos, I.3    Vonstein, V.4    Overbeek, R.5
  • 96
    • 10644283902 scopus 로고    scopus 로고
    • Alpha-glucan recognition by a new family of carbohydrate-binding modules found primarily in bacterial pathogens
    • Lammerts van Bueren A, Finn R, Ausio J & Boraston AB (2004) Alpha-glucan recognition by a new family of carbohydrate-binding modules found primarily in bacterial pathogens. Biochemistry (Mosc) 43: 15633-15642.
    • (2004) Biochemistry (Mosc) , vol.43 , pp. 15633-15642
    • Lammerts Van Bueren, A.1    Finn, R.2    Ausio, J.3    Boraston, A.B.4
  • 98
    • 0021088623 scopus 로고
    • Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. the nucleotide sequence of the permease gene
    • Lee CA & Saier MH Jr (1983) Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. The nucleotide sequence of the permease gene. J Biol Chem 258: 10761-10767.
    • (1983) J Biol Chem , vol.258 , pp. 10761-10767
    • Lee, C.A.1    Saier Jr., M.H.2
  • 100
    • 0037041916 scopus 로고    scopus 로고
    • Cooperative action of alpha-glucanotransferase and maltogenic amylase for an improved process of isomaltooligosaccharide (IMO) production
    • Lee HS, Auh JH, Yoon HG et al. (2002a) Cooperative action of alpha-glucanotransferase and maltogenic amylase for an improved process of isomaltooligosaccharide (IMO) production. J Agric Food Chem 50: 2812-2817.
    • (2002) J Agric Food Chem , vol.50 , pp. 2812-2817
    • Lee, H.S.1    Auh, J.H.2    Yoon, H.G.3
  • 101
    • 0036374133 scopus 로고    scopus 로고
    • A novel amylolytic enzyme from Thermotoga maritima, resembling cyclodextrinase and alpha-glucosidase, that liberates glucose from the reducing end of the substrates
    • Lee MH, Kim YW, Kim TJ, Park CS, Kim JW, Moon TW & Park KH (2002b) A novel amylolytic enzyme from Thermotoga maritima, resembling cyclodextrinase and alpha-glucosidase, that liberates glucose from the reducing end of the substrates. Biochem Biophys Res Commun 295: 818-825.
    • (2002) Biochem Biophys Res Commun , vol.295 , pp. 818-825
    • Lee, M.H.1    Kim, Y.W.2    Kim, T.J.3    Park, C.S.4    Kim, J.W.5    Moon, T.W.6    Park, K.H.7
  • 102
    • 0037428467 scopus 로고    scopus 로고
    • TrmB, a sugar-specific transcriptional regulator of the trehalose/maltose ABC transporter from the hyperthermophilic archaeon Thermococcus litoralis
    • Lee SJ, Engelmann A, Horlacher R, Qu Q, Vierke G, Hebbeln C, Thomm M & Boos W (2003) TrmB, a sugar-specific transcriptional regulator of the trehalose/maltose ABC transporter from the hyperthermophilic archaeon Thermococcus litoralis. J Biol Chem 278: 983-990.
    • (2003) J Biol Chem , vol.278 , pp. 983-990
    • Lee, S.J.1    Engelmann, A.2    Horlacher, R.3    Qu, Q.4    Vierke, G.5    Hebbeln, C.6    Thomm, M.7    Boos, W.8
  • 103
    • 1642416740 scopus 로고    scopus 로고
    • Characterization of a thermostable Larabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima
    • Lee DW, Jang HJ, Choe EA, Kim BC, Lee SJ, Kim SB, Hong YH & Pyun YR (2004a) Characterization of a thermostable Larabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima. Appl Environ Microbiol 70: 1397-1404.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 1397-1404
    • Lee, D.W.1    Jang, H.J.2    Choe, E.A.3    Kim, B.C.4    Lee, S.J.5    Kim, S.B.6    Hong, Y.H.7    Pyun, Y.R.8
  • 104
    • 9644307855 scopus 로고    scopus 로고
    • Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia
    • Lee HH, Kim do J, Ahn HJ, Ha JY & Suh SW (2004b) Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia. J Biol Chem 279: 50514-50523.
    • (2004) J Biol Chem , vol.279 , pp. 50514-50523
    • Lee, H.H.1    Kim Do, J.2    Ahn, H.J.3    Ha, J.Y.4    Suh, S.W.5
  • 105
    • 2642577521 scopus 로고    scopus 로고
    • Crystal structure of the TM1442 protein from Thermotoga maritima, a homolog of the Bacillus subtilis general stress response anti-anti-sigma factor RsbV
    • Lee JY, Ahn HJ, Ha KS & Suh SW (2004c) Crystal structure of the TM1442 protein from Thermotoga maritima, a homolog of the Bacillus subtilis general stress response anti-anti-sigma factor RsbV. Proteins 56: 176-179.
    • (2004) Proteins , vol.56 , pp. 176-179
    • Lee, J.Y.1    Ahn, H.J.2    Ha, K.S.3    Suh, S.W.4
  • 106
    • 13844271823 scopus 로고    scopus 로고
    • A thermodynamic study of mesophilic, thermophilic, and hyperthermophilic L-arabinose isomerases: The effects of divalent metal ions on protein stability at elevated temperatures
    • Lee DW, Hong YH, Choe EA, Lee SJ, Kim SB, Lee HS, Oh JW, Shin HH & Pyun YR (2005a) A thermodynamic study of mesophilic, thermophilic, and hyperthermophilic L-arabinose isomerases: the effects of divalent metal ions on protein stability at elevated temperatures. FEBS Lett 579: 1261-1266.
    • (2005) FEBS Lett , vol.579 , pp. 1261-1266
    • Lee, D.W.1    Hong, Y.H.2    Choe, E.A.3    Lee, S.J.4    Kim, S.B.5    Lee, H.S.6    Oh, J.W.7    Shin, H.H.8    Pyun, Y.R.9
  • 107
    • 25144461083 scopus 로고    scopus 로고
    • TrmB, a sugar sensing regulator of ABC transporter genes in Pyrococcus furiosus exhibits dual promoter specificity and is controlled by different inducers
    • Lee SJ, Moulakakis C, Koning SM, Hausner W, Thomm M & Boos W (2005b) TrmB, a sugar sensing regulator of ABC transporter genes in Pyrococcus furiosus exhibits dual promoter specificity and is controlled by different inducers. Mol Microbiol 57: 1797-1807.
    • (2005) Mol Microbiol , vol.57 , pp. 1797-1807
    • Lee, S.J.1    Moulakakis, C.2    Koning, S.M.3    Hausner, W.4    Thomm, M.5    Boos, W.6
  • 108
    • 0037015054 scopus 로고    scopus 로고
    • Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline
    • Lesley SA, Kuhn P, Godzik A et al. (2002) Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline. Proc Natl Acad Sci USA 99: 11664-11669.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11664-11669
    • Lesley, S.A.1    Kuhn, P.2    Godzik, A.3
  • 109
    • 21044457208 scopus 로고    scopus 로고
    • Crystal structure of an indigoidine synthase a (IndA)-like protein (TM1464) from Thermotoga maritima at 1.90 A° resolution reveals a new fold
    • Levin I, Miller MD, Schwarzenbacher R et al. (2005) Crystal structure of an indigoidine synthase A (IndA)-like protein (TM1464) from Thermotoga maritima at 1.90 A° resolution reveals a new fold. Proteins 59: 864-868.
    • (2005) Proteins , vol.59 , pp. 864-868
    • Levin, I.1    Miller, M.D.2    Schwarzenbacher, R.3
  • 110
    • 8144225134 scopus 로고    scopus 로고
    • In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylase
    • Li D, Park SH, Shim JH, Lee HS, Tang SY, Park CS & Park KH (2004) In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylase. Carbohydr Res 339: 2789-2797.
    • (2004) Carbohydr Res , vol.339 , pp. 2789-2797
    • Li, D.1    Park, S.H.2    Shim, J.H.3    Lee, H.S.4    Tang, S.Y.5    Park, C.S.6    Park, K.H.7
  • 111
    • 0026660023 scopus 로고
    • Purification and characterization of a novel thermostable 4-alpha-glucanotransferase of Thermotoga maritima cloned in Escherichia coli
    • Liebl W, Feil R, Gabelsberger J, Kellermann J & Schleifer KH (1992) Purification and characterization of a novel thermostable 4-alpha- glucanotransferase of Thermotoga maritima cloned in Escherichia coli. Eur J Biochem 207: 81-88.
    • (1992) Eur J Biochem , vol.207 , pp. 81-88
    • Liebl, W.1    Feil, R.2    Gabelsberger, J.3    Kellermann, J.4    Schleifer, K.H.5
  • 112
    • 0028123353 scopus 로고
    • Comparative amino acid sequence analysis of Thermotoga maritima beta-glucosidase (BglA) deduced from the nucleotide sequence of the gene indicates distant relationship between beta-glucosidases of the BGA family and other families of beta-1,4-glycosyl hydrolases
    • Liebl W, Gabelsberger J & Schleifer KH (1994) Comparative amino acid sequence analysis of Thermotoga maritima beta-glucosidase (BglA) deduced from the nucleotide sequence of the gene indicates distant relationship between beta-glucosidases of the BGA family and other families of beta-1,4-glycosyl hydrolases. Mol Gen Genet 242: 111-115.
    • (1994) Mol Gen Genet , vol.242 , pp. 111-115
    • Liebl, W.1    Gabelsberger, J.2    Schleifer, K.H.3
  • 113
    • 0029774346 scopus 로고    scopus 로고
    • Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes
    • Liebl W, Ruile P, Bronnenmeier K, Riedel K, Lottspeich F & Greif I (1996) Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes. Microbiology 142: 2533-2542.
    • (1996) Microbiology , vol.142 , pp. 2533-2542
    • Liebl, W.1    Ruile, P.2    Bronnenmeier, K.3    Riedel, K.4    Lottspeich, F.5    Greif, I.6
  • 114
    • 0031028407 scopus 로고    scopus 로고
    • Properties and gene structure of the Thermotoga maritima alpha-amylase AmyA, a putative lipoprotein of a hyperthermophilic bacterium
    • Liebl W, Stemplinger I & Ruile P (1997) Properties and gene structure of the Thermotoga maritima alpha-amylase AmyA, a putative lipoprotein of a hyperthermophilic bacterium. J Bacteriol 179: 941-948.
    • (1997) J Bacteriol , vol.179 , pp. 941-948
    • Liebl, W.1    Stemplinger, I.2    Ruile, P.3
  • 115
    • 0031855806 scopus 로고    scopus 로고
    • Analysis of the gene for beta-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima, and characterisation of the enzyme expressed in Escherichia coli
    • Liebl W, Brem D & Gotschlich A (1998a) Analysis of the gene for beta-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima, and characterisation of the enzyme expressed in Escherichia coli. Appl Microbiol Biotechnol 50: 55-64.
    • (1998) Appl Microbiol Biotechnol , vol.50 , pp. 55-64
    • Liebl, W.1    Brem, D.2    Gotschlich, A.3
  • 116
    • 0031894595 scopus 로고    scopus 로고
    • Properties of an alpha-galactosidase, and structure of its gene galA, within an alpha- And beta-galactoside utilization gene cluster of the hyperthermophilic bacterium Thermotoga maritima
    • Liebl W, Wagner B & Schellhase J (1998b) Properties of an alpha-galactosidase, and structure of its gene galA, within an alpha- and beta-galactoside utilization gene cluster of the hyperthermophilic bacterium Thermotoga maritima. Syst Appl Microbiol 21: 1-11.
    • (1998) Syst Appl Microbiol , vol.21 , pp. 1-11
    • Liebl, W.1    Wagner, B.2    Schellhase, J.3
  • 117
    • 10744220908 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable intracellular alpha-amylase gene from the hyperthermophilic bacterium Thermotoga maritima MSB8
    • Lim WJ, Park SR, An CL, Lee JY, Hong SY, Shin EC, Kim EJ, Kim JO, Kim H & Yun HD (2003) Cloning and characterization of a thermostable intracellular alpha-amylase gene from the hyperthermophilic bacterium Thermotoga maritima MSB8. Res Microbiol 154: 681-687.
    • (2003) Res Microbiol , vol.154 , pp. 681-687
    • Lim, W.J.1    Park, S.R.2    An, C.L.3    Lee, J.Y.4    Hong, S.Y.5    Shin, E.C.6    Kim, E.J.7    Kim, J.O.8    Kim, H.9    Yun, H.D.10
  • 118
    • 21744456875 scopus 로고    scopus 로고
    • Crystal structure of a heat-inducible transcriptional repressor HrcA from Thermotoga maritima: Structural insight into DNA binding and dimerization
    • Liu J, Huang C, Shin DH, Yokota H, Jancarik J, Kim JS, Adams PD, Kim R & Kim SH (2005a) Crystal structure of a heat-inducible transcriptional repressor HrcA from Thermotoga maritima: structural insight into DNA binding and dimerization. J Mol Biol 350: 987-996.
    • (2005) J Mol Biol , vol.350 , pp. 987-996
    • Liu, J.1    Huang, C.2    Shin, D.H.3    Yokota, H.4    Jancarik, J.5    Kim, J.S.6    Adams, P.D.7    Kim, R.8    Kim, S.H.9
  • 119
    • 18144379106 scopus 로고    scopus 로고
    • Crystal structure of a PhoU protein homologue: A new class of metalloprotein containing multinuclear iron clusters
    • Liu J, Lou Y, Yokota H, Adams PD, Kim R & Kim SH (2005b) Crystal structure of a PhoU protein homologue: a new class of metalloprotein containing multinuclear iron clusters. J Biol Chem 280: 15960-15966.
    • (2005) J Biol Chem , vol.280 , pp. 15960-15966
    • Liu, J.1    Lou, Y.2    Yokota, H.3    Adams, P.D.4    Kim, R.5    Kim, S.H.6
  • 120
    • 18844400852 scopus 로고    scopus 로고
    • Cloning, expression, purification, and analysis of mannitol dehydrogenase gene mtlK from Lactobacillus brevis
    • Liu S, Saha B & Cotta M (2005c) Cloning, expression, purification, and analysis of mannitol dehydrogenase gene mtlK from Lactobacillus brevis. Appl Biochem Biotechnol 121-124: 391-401.
    • (2005) Appl Biochem Biotechnol , vol.121-124 , pp. 391-401
    • Liu, S.1    Saha, B.2    Cotta, M.3
  • 121
    • 0033614958 scopus 로고    scopus 로고
    • Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor
    • Lloyd SA, Whitby FG, Blair DF & Hill CP (1999) Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor. Nature 400: 472-475.
    • (1999) Nature , vol.400 , pp. 472-475
    • Lloyd, S.A.1    Whitby, F.G.2    Blair, D.F.3    Hill, C.P.4
  • 122
    • 0038820035 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases
    • Lodge JA, Maier T, Liebl W, Hoffmann V & Strater N (2003) Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases. J Biol Chem 278: 19151-19158.
    • (2003) J Biol Chem , vol.278 , pp. 19151-19158
    • Lodge, J.A.1    Maier, T.2    Liebl, W.3    Hoffmann, V.4    Strater, N.5
  • 123
    • 4544305681 scopus 로고    scopus 로고
    • Peptide signaling in Staphylococcus aureus and other Gram-positive bacteria
    • Lyon GJ & Novick RP (2004) Peptide signaling in Staphylococcus aureus and other Gram-positive bacteria. Peptides 25: 1389-1403.
    • (2004) Peptides , vol.25 , pp. 1389-1403
    • Lyon, G.J.1    Novick, R.P.2
  • 124
    • 0032709104 scopus 로고    scopus 로고
    • The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparative thermostability structural analysis of ten different TIM structures
    • Maes D, Zeelen JP, Thanki N et al. (1999) The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures. Proteins 37: 441-453.
    • (1999) Proteins , vol.37 , pp. 441-453
    • Maes, D.1    Zeelen, J.P.2    Thanki, N.3
  • 125
    • 0037079680 scopus 로고    scopus 로고
    • A DNA repair system specific for thermophilic Archaea and bacteria predicted by genomic context analysis
    • Makarova KS, Aravind L, Grishin NV, Rogozin IB & Koonin EV (2002) A DNA repair system specific for thermophilic Archaea and bacteria predicted by genomic context analysis. Nucleic Acids Res 30: 482-496.
    • (2002) Nucleic Acids Res , vol.30 , pp. 482-496
    • Makarova, K.S.1    Aravind, L.2    Grishin, N.V.3    Rogozin, I.B.4    Koonin, E.V.5
  • 126
    • 1642274382 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: Biochemical characterization of the conformational dynamics of Thermotoga maritima IscU and the relevance for cellular cluster assembly
    • Mansy SS, Wu SP & Cowan JA (2004) Iron-sulfur cluster biosynthesis: biochemical characterization of the conformational dynamics of Thermotoga maritima IscU and the relevance for cellular cluster assembly. J Biol Chem 279: 10469-10475.
    • (2004) J Biol Chem , vol.279 , pp. 10469-10475
    • Mansy, S.S.1    Wu, S.P.2    Cowan, J.A.3
  • 127
    • 0029838122 scopus 로고    scopus 로고
    • New compatible solutes related to Di-myo-inositol-phosphate in members of the order Thermotogales
    • Martins LO, Carreto LS, Da Costa MS & 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
  • 128
    • 26444505976 scopus 로고    scopus 로고
    • Effect of RyhB small RNA on global iron use in Escherichia coli
    • Masse E, Vanderpool CK & Gottesman S (2005) Effect of RyhB small RNA on global iron use in Escherichia coli. J Bacteriol 187: 6962-6971.
    • (2005) J Bacteriol , vol.187 , pp. 6962-6971
    • Masse, E.1    Vanderpool, C.K.2    Gottesman, S.3
  • 129
    • 21044441789 scopus 로고    scopus 로고
    • Crystal structure of S-adenosylmethionine: TRNA ribosyltransferase- isomerase (QueA) from Thermotoga maritima at 2.0 Å resolution reveals a new fold
    • Mathews I, Schwarzenbacher R, McMullan D et al. (2005) Crystal structure of S-adenosylmethionine: tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 Å resolution reveals a new fold. Proteins 59: 869-874.
    • (2005) Proteins , vol.59 , pp. 869-874
    • Mathews, I.1    Schwarzenbacher, R.2    McMullan, D.3
  • 130
    • 1642445607 scopus 로고    scopus 로고
    • Improved catalytic efficiency and active site modification of 1,4-beta-D-glucan glucohydrolase a from Thermotoga neapolitana by directed evolution
    • McCarthy JK, Uzelac A, Davis DF & Eveleigh DE (2004) Improved catalytic efficiency and active site modification of 1,4-beta-D-glucan glucohydrolase A from Thermotoga neapolitana by directed evolution. J Biol Chem 279: 11495-11502.
    • (2004) J Biol Chem , vol.279 , pp. 11495-11502
    • McCarthy, J.K.1    Uzelac, A.2    Davis, D.F.3    Eveleigh, D.E.4
  • 132
    • 3142758487 scopus 로고    scopus 로고
    • Crystal structure of a novel Thermotoga maritima enzyme (TM1112) from the cupin family at 1.83 Å resolution
    • McMullan D, Schwarzenbacher R, Jaroszewski L et al. (2004) Crystal structure of a novel Thermotoga maritima enzyme (TM1112) from the cupin family at 1.83 Å resolution. Proteins 56: 615-618.
    • (2004) Proteins , vol.56 , pp. 615-618
    • McMullan, D.1    Schwarzenbacher, R.2    Jaroszewski, L.3
  • 133
    • 0032535155 scopus 로고    scopus 로고
    • Thermotoga maritima maltosyltransferase, a novel type of maltodextrin glycosyltransferase acting on starch and maltooligosaccharides
    • Meissner H & Liebl W (1998) Thermotoga maritima maltosyltransferase, a novel type of maltodextrin glycosyltransferase acting on starch and maltooligosaccharides. Eur J Biochem 258: 1050-1058.
    • (1998) Eur J Biochem , vol.258 , pp. 1050-1058
    • Meissner, H.1    Liebl, W.2
  • 134
    • 0034127278 scopus 로고    scopus 로고
    • The thermostabilizing domain of the modular xylanase XynA of Thermotoga maritima represents a novel type of binding domain with affinity for soluble xylan and mixed-linkage beta-1,3/beta-1, 4-glucan
    • Meissner K, Wassenberg D & Liebl W (2000) The thermostabilizing domain of the modular xylanase XynA of Thermotoga maritima represents a novel type of binding domain with affinity for soluble xylan and mixed-linkage beta-1,3/beta-1, 4-glucan. Mol Microbiol 36: 898-912.
    • (2000) Mol Microbiol , vol.36 , pp. 898-912
    • Meissner, K.1    Wassenberg, D.2    Liebl, W.3
  • 136
    • 23944509113 scopus 로고    scopus 로고
    • Characterization of Vibrio cholerae RyhB: The RyhB regulon and role of RyhB in biofilm formation
    • Mey AR, Craig SA & Payne SM (2005) Characterization of Vibrio cholerae RyhB: the RyhB regulon and role of RyhB in biofilm formation. Infect Immun 73: 5706-5719.
    • (2005) Infect Immun , vol.73 , pp. 5706-5719
    • Mey, A.R.1    Craig, S.A.2    Payne, S.M.3
  • 137
    • 0038309557 scopus 로고    scopus 로고
    • Crystal complexes of a predicted S-adenosylmethionine-dependent methyltransferase reveal a typical AdoMet binding domain and a substrate recognition domain
    • Miller DJ, Ouellette N, Evdokimova E, Savchenko A, Edwards A & Anderson WF (2003) Crystal complexes of a predicted S-adenosylmethionine- dependent methyltransferase reveal a typical AdoMet binding domain and a substrate recognition domain. Protein Sci 12: 1432-1442.
    • (2003) Protein Sci , vol.12 , pp. 1432-1442
    • Miller, D.J.1    Ouellette, N.2    Evdokimova, E.3    Savchenko, A.4    Edwards, A.5    Anderson, W.F.6
  • 138
    • 4444256467 scopus 로고    scopus 로고
    • Crystal structure of a tandem cystathionine-beta-synthase (CBS) domain protein (TM0935) from Thermotoga maritima at 1.87 Å resolution
    • Miller MD, Schwarzenbacher R, von Delft F et al. (2004) Crystal structure of a tandem cystathionine-beta-synthase (CBS) domain protein (TM0935) from Thermotoga maritima at 1.87 Å resolution. Proteins 57: 213-217.
    • (2004) Proteins , vol.57 , pp. 213-217
    • Miller, M.D.1    Schwarzenbacher, R.2    Von Delft, F.3
  • 139
    • 26444500989 scopus 로고    scopus 로고
    • Hyperthermophilic alpha-L-arabinofuranosidase from Thermotoga maritima MSB8: Molecular cloning, gene expression, and characterization of the recombinant protein
    • Miyazaki K (2005) Hyperthermophilic alpha-L-arabinofuranosidase from Thermotoga maritima MSB8: molecular cloning, gene expression, and characterization of the recombinant protein. Extremophiles 9: 399-406.
    • (2005) Extremophiles , vol.9 , pp. 399-406
    • Miyazaki, K.1
  • 140
    • 0030849142 scopus 로고    scopus 로고
    • The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis
    • Mogk A, Homuth G, Scholz C, Kim L, Schmid FX & Schumann W(1997) The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis. EMBO J 16: 4579-4590.
    • (1997) EMBO J , vol.16 , pp. 4579-4590
    • Mogk, A.1    Homuth, G.2    Scholz, C.3    Kim, L.4    Schmid, F.X.5    Schumann, W.6
  • 141
    • 0034034401 scopus 로고    scopus 로고
    • Biological significance of a family of regularly spaced repeats in the genomes of Archaea, Bacteria and mitochondria
    • Mojica FJ, Diez-Villasenor C, Soria E & Juez G (2000) Biological significance of a family of regularly spaced repeats in the genomes of Archaea, Bacteria and mitochondria. Mol Microbiol 36: 244-246.
    • (2000) Mol Microbiol , vol.36 , pp. 244-246
    • Mojica, F.J.1    Diez-Villasenor, C.2    Soria, E.3    Juez, G.4
  • 142
    • 16444385662 scopus 로고    scopus 로고
    • Intervening sequences of regularly spaced prokaryotic repeats derive from foreign genetic elements
    • Mojica FJ, Diez-Villasenor C, Garcia-Martinez J & Soria E (2005) Intervening sequences of regularly spaced prokaryotic repeats derive from foreign genetic elements. J Mol Evol 60: 174-182.
    • (2005) J Mol Evol , vol.60 , pp. 174-182
    • Mojica, F.J.1    Diez-Villasenor, C.2    Garcia-Martinez, J.3    Soria, E.4
  • 144
    • 0031555167 scopus 로고    scopus 로고
    • Hydrogen transfer between methanogens and fermentative heterotrophs in hyperthermophilic cocultures
    • Muralidharan V, Rinker KD, Hirsh IS, Bouwer EJ & Kelly RM (1997) Hydrogen transfer between methanogens and fermentative heterotrophs in hyperthermophilic cocultures. Biotechnol Bioeng 56: 268-278.
    • (1997) Biotechnol Bioeng , vol.56 , pp. 268-278
    • Muralidharan, V.1    Rinker, K.D.2    Hirsh, I.S.3    Bouwer, E.J.4    Kelly, R.M.5
  • 145
    • 22544441350 scopus 로고    scopus 로고
    • Iron salts perturb biofilm formation and disrupt existing biofilms of Pseudomonas aeruginosa
    • Musk DJ, Banko DA & Hergenrother PJ (2005) Iron salts perturb biofilm formation and disrupt existing biofilms of Pseudomonas aeruginosa. Chem Biol 12: 789-796.
    • (2005) Chem Biol , vol.12 , pp. 789-796
    • Musk, D.J.1    Banko, D.A.2    Hergenrother, P.J.3
  • 146
    • 0038511329 scopus 로고    scopus 로고
    • Unique metal dependency of cytosolic alpha-mannosidase from Thermotoga maritima, a hyperthermophilic bacterium
    • Nakajima M, Imamura H, Shoun H & Wakagi T (2003) Unique metal dependency of cytosolic alpha-mannosidase from Thermotoga maritima, a hyperthermophilic bacterium. Arch Biochem Biophys 415: 87-93.
    • (2003) Arch Biochem Biophys , vol.415 , pp. 87-93
    • Nakajima, M.1    Imamura, H.2    Shoun, H.3    Wakagi, T.4
  • 148
    • 0036856399 scopus 로고    scopus 로고
    • Periplasmic maltose- And glucose-binding protein activities in cell-free extracts of Thermotoga maritima
    • Nanavati D, Noll KM & Romano AH (2002) Periplasmic maltose- and glucose-binding protein activities in cell-free extracts of Thermotoga maritima. Microbiology 148: 3531-3537.
    • (2002) Microbiology , vol.148 , pp. 3531-3537
    • Nanavati, D.1    Noll, K.M.2    Romano, A.H.3
  • 149
    • 14644403014 scopus 로고    scopus 로고
    • Substrate specificities and expression patterns reflect the evolutionary divergence of maltose ABC transporters in Thermotoga maritima
    • Nanavati DM, Nguyen TN & Noll KM (2005) Substrate specificities and expression patterns reflect the evolutionary divergence of maltose ABC transporters in Thermotoga maritima. J Bacteriol 187: 2002-2009.
    • (2005) J Bacteriol , vol.187 , pp. 2002-2009
    • Nanavati, D.M.1    Nguyen, T.N.2    Noll, K.M.3
  • 150
    • 33144472334 scopus 로고    scopus 로고
    • Several archaeal homologs of putative oligopeptide-binding proteins encoded by Thermotoga maritima bind sugars
    • Nanavati DM, Thirangoon K & Noll KM (2006) Several archaeal homologs of putative oligopeptide-binding proteins encoded by Thermotoga maritima bind sugars. Appl Environ Microbiol 72: 1336-1345.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 1336-1345
    • Nanavati, D.M.1    Thirangoon, K.2    Noll, K.M.3
  • 151
    • 0026595001 scopus 로고
    • Purification and functional characterization of the KdgR protein, a major
    • Nasser W, Reverchon S & Robert-Baudouy J (1992) Purification and functional characterization of the KdgR protein, a major repressor of pectinolysis genes of Erwinia chrysanthemi. Mol Microbiol 6: 257-265.
    • (1992) Mol Microbiol , vol.6 , pp. 257-265
    • Nasser, W.1    Reverchon, S.2    Robert-Baudouy, J.3
  • 152
    • 0033609333 scopus 로고    scopus 로고
    • Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima
    • Nelson KE, Clayton RA, Gill SR et al. (1999) Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature 399: 323-329.
    • (1999) Nature , vol.399 , pp. 323-329
    • Nelson, K.E.1    Clayton, R.A.2    Gill, S.R.3
  • 153
    • 0242424342 scopus 로고    scopus 로고
    • Targeting clusters of transferred genes in Thermotoga maritima
    • Nesbo CL & Doolittle WF (2003) Targeting clusters of transferred genes in Thermotoga maritima. Environ Microbiol 5: 1144-1154.
    • (2003) Environ Microbiol , vol.5 , pp. 1144-1154
    • Nesbo, C.L.1    Doolittle, W.F.2
  • 154
    • 0035106010 scopus 로고    scopus 로고
    • Phylogenetic analyses of two "archaeal" genes in Thermotoga maritima reveal multiple transfers between archaea and bacteria
    • Nesbo CL, L'Haridon S, Stetter KO & Doolittle WF (2001) Phylogenetic analyses of two "archaeal" genes in Thermotoga maritima reveal multiple transfers between archaea and bacteria. Mol Biol Evol 18: 362-375.
    • (2001) Mol Biol Evol , vol.18 , pp. 362-375
    • Nesbo, C.L.1    L'Haridon, S.2    Stetter, K.O.3    Doolittle, W.F.4
  • 155
    • 0036335361 scopus 로고    scopus 로고
    • Suppressive subtractive hybridization detects extensive genomic diversity in Thermotoga maritima
    • Nesbo CL, Nelson KE & Doolittle WF (2002) Suppressive subtractive hybridization detects extensive genomic diversity in Thermotoga maritima. J Bacteriol 184: 4475-4488.
    • (2002) J Bacteriol , vol.184 , pp. 4475-4488
    • Nesbo, C.L.1    Nelson, K.E.2    Doolittle, W.F.3
  • 156
    • 33644749286 scopus 로고    scopus 로고
    • Recombination in Thermotoga: Implications for species concepts and biogeography
    • Nesbo CL, Dlutek M & Doolittle WF (2006) Recombination in Thermotoga: implications for species concepts and biogeography. Genetics 172: 759-769.
    • (2006) Genetics , vol.172 , pp. 759-769
    • Nesbo, C.L.1    Dlutek, M.2    Doolittle, W.F.3
  • 157
    • 3042735789 scopus 로고    scopus 로고
    • Whole-genome expression profiling of Thermotoga maritima in response to growth on sugars in a chemostat
    • Nguyen TN, Ejaz AD, Brancieri MA, Mikula AM, Nelson KE, Gill SR & Noll KM (2004) Whole-genome expression profiling of Thermotoga maritima in response to growth on sugars in a chemostat. J Bacteriol 186: 4824-4828.
    • (2004) J Bacteriol , vol.186 , pp. 4824-4828
    • Nguyen, T.N.1    Ejaz, A.D.2    Brancieri, M.A.3    Mikula, A.M.4    Nelson, K.E.5    Gill, S.R.6    Noll, K.M.7
  • 158
    • 0030667158 scopus 로고    scopus 로고
    • The maltose/maltodextrin regulon of Streptococcus pneumoniae Differential promoter regulation by the transcriptional repressor MalR
    • Nieto C, Espinosa M & Puyet A (1997) The maltose/maltodextrin regulon of Streptococcus pneumoniae Differential promoter regulation by the transcriptional repressor MalR. J Biol Chem 272: 30860-30865.
    • (1997) J Biol Chem , vol.272 , pp. 30860-30865
    • Nieto, C.1    Espinosa, M.2    Puyet, A.3
  • 159
    • 0030849307 scopus 로고    scopus 로고
    • Recent advances in genetic analyses of hyperthermophilic archaea and bacteria
    • Noll KM & Vargas M (1997) Recent advances in genetic analyses of hyperthermophilic archaea and bacteria. Arch Microbiol 168: 73-80.
    • (1997) Arch Microbiol , vol.168 , pp. 73-80
    • Noll, K.M.1    Vargas, M.2
  • 160
    • 9144274340 scopus 로고    scopus 로고
    • Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 Å resolution
    • Page R, Nelson MS, von Delft F et al. (2004) Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 Å resolution. Proteins 54: 157-161.
    • (2004) Proteins , vol.54 , pp. 157-161
    • Page, R.1    Nelson, M.S.2    Von Delft, F.3
  • 161
    • 0023316642 scopus 로고
    • E. coli maltodextrin phosphorylase: Primary structure and deletion mapping of the C-terminal site
    • Palm D, Goerl R, Weidinger G, Zeier R, Fischer B & Schinzel R (1987) E. coli maltodextrin phosphorylase: primary structure and deletion mapping of the C-terminal site. Z Naturforsch [C] 42: 394-400.
    • (1987) Z Naturforsch [C] , vol.42 , pp. 394-400
    • Palm, D.1    Goerl, R.2    Weidinger, G.3    Zeier, R.4    Fischer, B.5    Schinzel, R.6
  • 162
    • 0037950633 scopus 로고    scopus 로고
    • Characterization of a [2Fe-2S] protein encoded in the iron-hydrogenase operon of Thermotoga maritima
    • Pan G, Menon AL & Adams MW (2003) Characterization of a [2Fe-2S] protein encoded in the iron-hydrogenase operon of Thermotoga maritima. J Biol Inorg Chem 8: 469-474.
    • (2003) J Biol Inorg Chem , vol.8 , pp. 469-474
    • Pan, G.1    Menon, A.L.2    Adams, M.W.3
  • 163
    • 0037047795 scopus 로고    scopus 로고
    • Exopolygalacturonate lyase from Thermotoga maritima: Cloning, characterization and organic synthesis application
    • Parisot J, Ghochikyan A, Langlois V, Sakanyan V & Rabiller C (2002) Exopolygalacturonate lyase from Thermotoga maritima: cloning, characterization and organic synthesis application. Carbohydr Res 337: 1427-1433.
    • (2002) Carbohydr Res , vol.337 , pp. 1427-1433
    • Parisot, J.1    Ghochikyan, A.2    Langlois, V.3    Sakanyan, V.4    Rabiller, C.5
  • 164
    • 0038021209 scopus 로고    scopus 로고
    • Cloning expression and characterization of a thermostable exopolygalacturonase from Thermotoga maritima
    • Parisot J, Langlois V, Sakanyan V & Rabiller C (2003) Cloning expression and characterization of a thermostable exopolygalacturonase from Thermotoga maritima. Carbohydr Res 338: 1333-1337.
    • (2003) Carbohydr Res , vol.338 , pp. 1333-1337
    • Parisot, J.1    Langlois, V.2    Sakanyan, V.3    Rabiller, C.4
  • 165
    • 4143085007 scopus 로고    scopus 로고
    • In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved
    • Park SY, Beel BD, Simon MI, Bilwes AM & Crane BR (2004a) In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved. Proc Natl Acad Sci USA 101: 11646-11651.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11646-11651
    • Park, S.Y.1    Beel, B.D.2    Simon, M.I.3    Bilwes, A.M.4    Crane, B.R.5
  • 166
    • 2942659743 scopus 로고    scopus 로고
    • The 1.59 Å resolution crystal structure of TM0096, a flavin mononucleotide binding protein from Thermotoga maritima
    • Park F, Gajiwala K, Noland B et al. (2004b) The 1.59 Å resolution crystal structure of TM0096, a flavin mononucleotide binding protein from Thermotoga maritima. Proteins 55: 772-774.
    • (2004) Proteins , vol.55 , pp. 772-774
    • Park, F.1    Gajiwala, K.2    Noland, B.3
  • 167
    • 1442300985 scopus 로고    scopus 로고
    • Subunit exchange by CheA histidine kinases from the mesophile Escherichia coli and the thermophile Thermotoga maritima
    • Park SY, Quezada CM, Bilwes AM & Crane BR (2004c) Subunit exchange by CheA histidine kinases from the mesophile Escherichia coli and the thermophile Thermotoga maritima. Biochemistry (Moscow) 43: 2228-2240.
    • (2004) Biochemistry (Moscow) , vol.43 , pp. 2228-2240
    • Park, S.Y.1    Quezada, C.M.2    Bilwes, A.M.3    Crane, B.R.4
  • 168
    • 0035813450 scopus 로고    scopus 로고
    • Galactomannanases Man2 and Man5 from Thermotoga species: Growth physiology on galactomannans, gene sequence analysis, and biochemical properties of recombinant enzymes
    • Parker KN, Chhabra SR, Lam D, Callen W, Duffaud GD, Snead MA, Short JM, Mathur EJ & Kelly RM (2001) Galactomannanases Man2 and Man5 from Thermotoga species: growth physiology on galactomannans, gene sequence analysis, and biochemical properties of recombinant enzymes. Biotechnol Bioeng 75: 322-333.
    • (2001) Biotechnol Bioeng , vol.75 , pp. 322-333
    • Parker, K.N.1    Chhabra, S.R.2    Lam, D.3    Callen, W.4    Duffaud, G.D.5    Snead, M.A.6    Short, J.M.7    Mathur, E.J.8    Kelly, R.M.9
  • 170
    • 2442544313 scopus 로고    scopus 로고
    • Biomolecular NMR using a microcoil NMR probe - New technique for the chemical shift assignment of aromatic side chains in proteins
    • Peti W, Norcross J, Eldridge G & O'Neil-Johnson M (2004) Biomolecular NMR using a microcoil NMR probe - new technique for the chemical shift assignment of aromatic side chains in proteins. J Am Chem Soc 126: 5873-5878.
    • (2004) J Am Chem Soc , vol.126 , pp. 5873-5878
    • Peti, W.1    Norcross, J.2    Eldridge, G.3    O'Neil-Johnson, M.4
  • 171
    • 0142155219 scopus 로고    scopus 로고
    • CspB and CspL, thermostable cold-shock proteins from Thermotoga maritima
    • Phadtare S, Hwang J, Severinov K & Inouye M (2003) CspB and CspL, thermostable cold-shock proteins from Thermotoga maritima. Genes Cells 8: 801-810.
    • (2003) Genes Cells , vol.8 , pp. 801-810
    • Phadtare, S.1    Hwang, J.2    Severinov, K.3    Inouye, M.4
  • 172
    • 0043032766 scopus 로고    scopus 로고
    • MiaB protein from Thermotoga maritima. Characterization of an extremely thermophilic tRNA-methylthiotransferase
    • Pierrel F, Hernandez HL, Johnson MK, Fontecave M & Atta M (2003) MiaB protein from Thermotoga maritima. Characterization of an extremely thermophilic tRNA-methylthiotransferase. J Biol Chem 278: 29515-29524.
    • (2003) J Biol Chem , vol.278 , pp. 29515-29524
    • Pierrel, F.1    Hernandez, H.L.2    Johnson, M.K.3    Fontecave, M.4    Atta, M.5
  • 173
    • 0019148881 scopus 로고
    • Regulation of Escherichia coli K-12 hexuronate system genes: Exu regulon
    • Portalier R, Robert-Baudouy J & Stoeber F (1980) Regulation of Escherichia coli K-12 hexuronate system genes: exu regulon. J Bacteriol 143: 1095-1107.
    • (1980) J Bacteriol , vol.143 , pp. 1095-1107
    • Portalier, R.1    Robert-Baudouy, J.2    Stoeber, F.3
  • 174
    • 15844390228 scopus 로고    scopus 로고
    • CRISPR elements in Yersinia pestis acquire new repeats by preferential uptake of bacteriophage DNA, and provide additional tools for evolutionary studies
    • Pourcel C, Salvignol G & Vergnaud G (2005) CRISPR elements in Yersinia pestis acquire new repeats by preferential uptake of bacteriophage DNA, and provide additional tools for evolutionary studies. Microbiology 151: 653-663.
    • (2005) Microbiology , vol.151 , pp. 653-663
    • Pourcel, C.1    Salvignol, G.2    Vergnaud, G.3
  • 175
    • 10744220291 scopus 로고    scopus 로고
    • The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533
    • Pridmore RD, Berger B, Desiere F et al. (2004) The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533. Proc Natl Acad Sci USA 101: 2512-2517.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2512-2517
    • Pridmore, R.D.1    Berger, B.2    Desiere, F.3
  • 176
    • 0024042231 scopus 로고
    • Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase
    • Pugsley AP & Dubreuil C (1988) Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase. Mol Microbiol 2: 473-479.
    • (1988) Mol Microbiol , vol.2 , pp. 473-479
    • Pugsley, A.P.1    Dubreuil, C.2
  • 177
    • 0031793117 scopus 로고    scopus 로고
    • The kdgRKAT operon of Bacillus subtilis: Detection of the transcript and regulation by the kdgR and ccpA genes
    • Pujic P, Dervyn R, Sorokin A & Ehrlich SD (1998) The kdgRKAT operon of Bacillus subtilis: detection of the transcript and regulation by the kdgR and ccpA genes. Microbiology 144: 3111-3118.
    • (1998) Microbiology , vol.144 , pp. 3111-3118
    • Pujic, P.1    Dervyn, R.2    Sorokin, A.3    Ehrlich, S.D.4
  • 181
    • 4143077357 scopus 로고    scopus 로고
    • Helical shifts generate two distinct conformers in the atomic resolution structure of the CheA phosphotransferase domain from Thermotoga maritima
    • Quezada CM, Gradinaru C, Simon MI, Bilwes AM & Crane BR (2004) Helical shifts generate two distinct conformers in the atomic resolution structure of the CheA phosphotransferase domain from Thermotoga maritima. J Mol Biol 341: 1283-1294.
    • (2004) J Mol Biol , vol.341 , pp. 1283-1294
    • Quezada, C.M.1    Gradinaru, C.2    Simon, M.I.3    Bilwes, A.M.4    Crane, B.R.5
  • 182
    • 0034242764 scopus 로고    scopus 로고
    • Thermotoga maritima AglA, an extremely thermostable NAD+-, Mn2+-, and thiol-dependent alpha-glucosidase
    • Raasch C, Streit W, Schanzer J, Bibel M, Gosslar U & Liebl W (2000) Thermotoga maritima AglA, an extremely thermostable NAD+-, Mn2+-, and thiol-dependent alpha-glucosidase. Extremophiles 4: 189-200.
    • (2000) Extremophiles , vol.4 , pp. 189-200
    • Raasch, C.1    Streit, W.2    Schanzer, J.3    Bibel, M.4    Gosslar, U.5    Liebl, W.6
  • 183
    • 0037165653 scopus 로고    scopus 로고
    • Identification of residues important for NAD+binding by the Thermotoga maritima alpha-glucosidase AglA, a member of glycoside hydrolase family 4
    • Raasch C, Armbrecht M, Streit W, Hocker B, Strater N & Liebl W (2002) Identification of residues important for NAD+binding by the Thermotoga maritima alpha-glucosidase AglA, a member of glycoside hydrolase family 4. FEBS Lett 517: 267-271.
    • (2002) FEBS Lett , vol.517 , pp. 267-271
    • Raasch, C.1    Armbrecht, M.2    Streit, W.3    Hocker, B.4    Strater, N.5    Liebl, W.6
  • 184
    • 0042201948 scopus 로고    scopus 로고
    • Characterization of a cellobiose phosphorylase from a hyperthermophilic eubacterium, Thermotoga maritima MSB8
    • Rajashekhara E, Kitaoka M, Kim YK & Hayashi K (2002) Characterization of a cellobiose phosphorylase from a hyperthermophilic eubacterium, Thermotoga maritima MSB8. Biosci Biotechnol Biochem 66: 2578-2586.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 2578-2586
    • Rajashekhara, E.1    Kitaoka, M.2    Kim, Y.K.3    Hayashi, K.4
  • 187
    • 0024729941 scopus 로고
    • MalI, a novel protein involved in regulation of the maltose system of Escherichia coli, is highly homologous to the repressor proteins GalR, CytR, and LacI
    • Reidl J, Romisch K, Ehrmann M & Boos W (1989) MalI, a novel protein involved in regulation of the maltose system of Escherichia coli, is highly homologous to the repressor proteins GalR, CytR, and LacI. J Bacteriol 171: 4888-4899.
    • (1989) J Bacteriol , vol.171 , pp. 4888-4899
    • Reidl, J.1    Romisch, K.2    Ehrmann, M.3    Boos, W.4
  • 188
    • 0025761081 scopus 로고
    • Characterization of kdgR, a gene of Erwinia chrysanthemi that regulates pectin degradation
    • Reverchon S, Nasser W & Robert-Baudouy J (1991) Characterization of kdgR, a gene of Erwinia chrysanthemi that regulates pectin degradation. Mol Microbiol 5: 2203-2216.
    • (1991) Mol Microbiol , vol.5 , pp. 2203-2216
    • Reverchon, S.1    Nasser, W.2    Robert-Baudouy, J.3
  • 189
    • 10044261004 scopus 로고    scopus 로고
    • A genetic locus necessary for rhamnose uptake and catabolism in Rhizobium leguminosarum bv. trifolli
    • Richardson JS, Hynes MF & Oresnik IJ (2004) A genetic locus necessary for rhamnose uptake and catabolism in Rhizobium leguminosarum bv. trifolli. J Bacteriol 186: 8433-8442.
    • (2004) J Bacteriol , vol.186 , pp. 8433-8442
    • Richardson, J.S.1    Hynes, M.F.2    Oresnik, I.J.3
  • 190
    • 26444531033 scopus 로고    scopus 로고
    • Crystal structure of a putative modulator of DNA gyrase (pmbA) from Thermotoga maritima at 1.95 Å resolution reveals a new fold
    • Rife C, Schwarzenbacher R, McMullan D et al. (2005) Crystal structure of a putative modulator of DNA gyrase (pmbA) from Thermotoga maritima at 1.95 Å resolution reveals a new fold. Proteins 61: 444-448.
    • (2005) Proteins , vol.61 , pp. 444-448
    • Rife, C.1    Schwarzenbacher, R.2    McMullan, D.3
  • 191
    • 0033027267 scopus 로고    scopus 로고
    • Continuous culture as a tool for investigating the growth physiology of heterotrophic hyperthermophiles and extreme thermoacidophiles
    • Rinker KD, Han CJ & Kelly RM (1999) Continuous culture as a tool for investigating the growth physiology of heterotrophic hyperthermophiles and extreme thermoacidophiles. J Appl Microbiol 85: 118-127.
    • (1999) J Appl Microbiol , vol.85 , pp. 118-127
    • Rinker, K.D.1    Han, C.J.2    Kelly, R.M.3
  • 192
    • 0031955932 scopus 로고    scopus 로고
    • A 35.7 kb DNA fragment from the Bacillus subtilis chromosome containing a putative 12.3 kb operon involved in hexuronate catabolism and a perfectly symmetrical hypothetical catabolite-responsive element
    • Rivolta C, Soldo B, Lazarevic V, Joris B, Mauel C & Karamata D (1998) A 35.7 kb DNA fragment from the Bacillus subtilis chromosome containing a putative 12.3 kb operon involved in hexuronate catabolism and a perfectly symmetrical hypothetical catabolite-responsive element. Microbiology 144: 877-884.
    • (1998) Microbiology , vol.144 , pp. 877-884
    • Rivolta, C.1    Soldo, B.2    Lazarevic, V.3    Joris, B.4    Mauel, C.5    Karamata, D.6
  • 193
    • 0038154011 scopus 로고    scopus 로고
    • Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily
    • Robinson VL, Wu T & Stock AM (2003) Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily. J Bacteriol 185: 4186-4194.
    • (2003) J Bacteriol , vol.185 , pp. 4186-4194
    • Robinson, V.L.1    Wu, T.2    Stock, A.M.3
  • 194
    • 20444389830 scopus 로고    scopus 로고
    • Structural genomics of Thermotoga maritima proteins shows that contact order is a major determinant of protein thermostability
    • Robinson-Rechavi M & Godzik A (2005) Structural genomics of Thermotoga maritima proteins shows that contact order is a major determinant of protein thermostability. Structure (Cambridge) 13: 857-860.
    • (2005) Structure (Cambridge) , vol.13 , pp. 857-860
    • Robinson-Rechavi, M.1    Godzik, A.2
  • 195
    • 0035823253 scopus 로고    scopus 로고
    • The crystal structure of Thermotoga maritima maltosyltransferase and its implications for the molecular basis of the novel transfer specificity
    • Roujeinikova A, Raasch C, Burke J, Baker PJ, Liebl W & Rice DW (2001a) The crystal structure of Thermotoga maritima maltosyltransferase and its implications for the molecular basis of the novel transfer specificity. J Mol Biol 312: 119-131.
    • (2001) J Mol Biol , vol.312 , pp. 119-131
    • Roujeinikova, A.1    Raasch, C.2    Burke, J.3    Baker, P.J.4    Liebl, W.5    Rice, D.W.6
  • 196
    • 0034929048 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies on 4-alpha-glucanotransferase from Thermotoga maritima
    • Roujeinikova A, Raasch C, Sedelnikova S, Liebl W & Rice DW (2001b) Crystallization and preliminary X-ray crystallographic studies on 4-alpha-glucanotransferase from Thermotoga maritima. Acta Crystallogr D Biol Crystallogr 57: 1046-1047.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 1046-1047
    • Roujeinikova, A.1    Raasch, C.2    Sedelnikova, S.3    Liebl, W.4    Rice, D.W.5
  • 197
    • 0036354161 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima 4-alpha-glucanotransferase and its acarbose complex: Implications for substrate specificity and catalysis
    • Roujeinikova A, Raasch C, Sedelnikova S, Liebl W & Rice DW (2002) Crystal structure of Thermotoga maritima 4-alpha-glucanotransferase and its acarbose complex: implications for substrate specificity and catalysis. J Mol Biol 321: 149-162.
    • (2002) J Mol Biol , vol.321 , pp. 149-162
    • Roujeinikova, A.1    Raasch, C.2    Sedelnikova, S.3    Liebl, W.4    Rice, D.W.5
  • 198
    • 24144494192 scopus 로고    scopus 로고
    • Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima
    • Rubach JK, Brazzolotto X, Gaillard J & Fontecave M (2005) Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima. FEBS Lett 579: 5055-5060.
    • (2005) FEBS Lett , vol.579 , pp. 5055-5060
    • Rubach, J.K.1    Brazzolotto, X.2    Gaillard, J.3    Fontecave, M.4
  • 199
    • 0027483030 scopus 로고
    • Thermostable beta-glucosidase and beta-xylosidase from Thermotoga sp. strain FjSS3-B.1
    • Ruttersmith LD & Daniel RM (1993) Thermostable beta-glucosidase and beta-xylosidase from Thermotoga sp. strain FjSS3-B.1. Biochim Biophys Acta 1156: 167-172.
    • (1993) Biochim Biophys Acta , vol.1156 , pp. 167-172
    • Ruttersmith, L.D.1    Daniel, R.M.2
  • 200
    • 14244254898 scopus 로고    scopus 로고
    • Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: Insights into biochemistry of the GGDEF protein domain
    • Ryjenkov DA, Tarutina M, Moskvin OV & Gomelsky M (2005) Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain. J Bacteriol 187: 1792-1798.
    • (2005) J Bacteriol , vol.187 , pp. 1792-1798
    • Ryjenkov, D.A.1    Tarutina, M.2    Moskvin, O.V.3    Gomelsky, M.4
  • 201
    • 1842763734 scopus 로고    scopus 로고
    • Purification and characterization of a novel mannitol dehydrogenase from Lactobacillus intermedius
    • Saha BC (2004) Purification and characterization of a novel mannitol dehydrogenase from Lactobacillus intermedius. Biotechnol Prog 20: 537-542.
    • (2004) Biotechnol Prog , vol.20 , pp. 537-542
    • Saha, B.C.1
  • 203
    • 2642514010 scopus 로고    scopus 로고
    • Crystal structure of a glycerophosphodiester phosphodiesterase (GDPD) from Thermotoga maritima (TM1621) at 1.60 Å resolution
    • Santelli E, Schwarzenbacher R, McMullan D et al. (2004) Crystal structure of a glycerophosphodiester phosphodiesterase (GDPD) from Thermotoga maritima (TM1621) at 1.60 Å resolution. Proteins 56: 167-170.
    • (2004) Proteins , vol.56 , pp. 167-170
    • Santelli, E.1    Schwarzenbacher, R.2    McMullan, D.3
  • 204
    • 24044477519 scopus 로고    scopus 로고
    • Lactobacillus reuteri ATCC 53608 mdh gene cloning and recombinant mannitol dehydrogenase characterization
    • Sasaki Y, Laivenieks M & Zeikus JG (2005) Lactobacillus reuteri ATCC 53608 mdh gene cloning and recombinant mannitol dehydrogenase characterization. Appl Microbiol Biotechnol 68: 36-41.
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 36-41
    • Sasaki, Y.1    Laivenieks, M.2    Zeikus, J.G.3
  • 205
    • 0028786876 scopus 로고
    • Sequence and expression of a xylanase gene from the hyperthermophile Thermotoga sp. strain FjSS3-B.1 and characterization of the recombinant enzyme and its activity on kraft pulp
    • Saul DJ, Williams LC, Reeves RA, Gibbs MD & Bergquist PL (1995) Sequence and expression of a xylanase gene from the hyperthermophile Thermotoga sp. strain FjSS3-B.1 and characterization of the recombinant enzyme and its activity on kraft pulp. Appl Environ Microbiol 61: 4110-4113.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 4110-4113
    • Saul, D.J.1    Williams, L.C.2    Reeves, R.A.3    Gibbs, M.D.4    Bergquist, P.L.5
  • 207
    • 0037384574 scopus 로고    scopus 로고
    • Global gene expression in Escherichia coli biofilms
    • Schembri MA, Kjaergaard K & Klemm P (2003) Global gene expression in Escherichia coli biofilms. Mol Microbiol 48: 253-267.
    • (2003) Mol Microbiol , vol.48 , pp. 253-267
    • Schembri, M.A.1    Kjaergaard, K.2    Klemm, P.3
  • 208
    • 0030896572 scopus 로고    scopus 로고
    • The Streptomyces ATP-binding component MsiK assists in cellobiose and maltose transport
    • Schlosser A, Kampers T & Schrempf H (1997) The Streptomyces ATP-binding component MsiK assists in cellobiose and maltose transport. J Bacteriol 179: 2092-2095.
    • (1997) J Bacteriol , vol.179 , pp. 2092-2095
    • Schlosser, A.1    Kampers, T.2    Schrempf, H.3
  • 209
    • 0035010435 scopus 로고    scopus 로고
    • ABC transporters catalyzing carbohydrate uptake
    • Schneider E (2001) ABC transporters catalyzing carbohydrate uptake. Res Microbiol 152: 303-310.
    • (2001) Res Microbiol , vol.152 , pp. 303-310
    • Schneider, E.1
  • 210
    • 0037236212 scopus 로고    scopus 로고
    • Comparative genotyping of Campylobacter jejuni by amplified fragment length polymorphism, multilocus sequence typing, and short repeat sequencing: Strain diversity, host range, and recombination
    • Schouls LM, Reulen S, Duim B, Wagenaar JA, Willems RJ, Dingle KE, Colles FM & Van Embden JD (2003) Comparative genotyping of Campylobacter jejuni by amplified fragment length polymorphism, multilocus sequence typing, and short repeat sequencing: strain diversity, host range, and recombination. J Clin Microbiol 41: 15-26.
    • (2003) J Clin Microbiol , vol.41 , pp. 15-26
    • Schouls, L.M.1    Reulen, S.2    Duim, B.3    Wagenaar, J.A.4    Willems, R.J.5    Dingle, K.E.6    Colles, F.M.7    Van Embden, J.D.8
  • 211
    • 0037343179 scopus 로고    scopus 로고
    • Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as a fatty acid-binding protein
    • Schulze-Gahmen U, Pelaschier J, Yokota H, Kim R & Kim SH (2003) Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as a fatty acid-binding protein. Proteins 50: 526-530.
    • (2003) Proteins , vol.50 , pp. 526-530
    • Schulze-Gahmen, U.1    Pelaschier, J.2    Yokota, H.3    Kim, R.4    Kim, S.H.5
  • 212
    • 0025818996 scopus 로고
    • Topographical and enzymatic characterization of amylases from the extremely thermophilic eubacterium Thermotoga maritima
    • Schumann J, Wrba A, Jaenicke R & Stetter KO (1991) Topographical and enzymatic characterization of amylases from the extremely thermophilic eubacterium Thermotoga maritima. FEBS Lett 282: 122-126.
    • (1991) FEBS Lett , vol.282 , pp. 122-126
    • Schumann, J.1    Wrba, A.2    Jaenicke, R.3    Stetter, K.O.4
  • 213
    • 0041319016 scopus 로고    scopus 로고
    • Crystal structure of uronate isomerase (TM0064) from Thermotoga maritima at 2.85 A resolution
    • Schwarzenbacher R, Canaves JM, Brinen LS et al. (2003) Crystal structure of uronate isomerase (TM0064) from Thermotoga maritima at 2.85 A resolution. Proteins 53: 142-145.
    • (2003) Proteins , vol.53 , pp. 142-145
    • Schwarzenbacher, R.1    Canaves, J.M.2    Brinen, L.S.3
  • 214
    • 10744224011 scopus 로고    scopus 로고
    • Crystal structure of a putative glutamine amido transferase (TM1158) from Thermotoga maritima at 1.7 a resolution
    • Scwarzenbacher R, Deacon AM, Jaroszewski L et al. (2004a) Crystal structure of a putative glutamine amido transferase (TM1158) from Thermotoga maritima at 1.7 A resolution. Proteins 54: 801-805.
    • (2004) Proteins , vol.54 , pp. 801-805
    • Scwarzenbacher, R.1    Deacon, A.M.2    Jaroszewski, L.3
  • 215
    • 12144288747 scopus 로고    scopus 로고
    • Crystal structure of a phosphoribosylaminoimidazole mutase PurE (TM0446) from Thermotoga maritima at 1.77-A resolution
    • Schwarzenbacher R, Jaroszewski L, von Delft F et al. (2004b) Crystal structure of a phosphoribosylaminoimidazole mutase PurE (TM0446) from Thermotoga maritima at 1.77-A resolution. Proteins 55: 474-478.
    • (2004) Proteins , vol.55 , pp. 474-478
    • Schwarzenbacher, R.1    Jaroszewski, L.2    Von Delft, F.3
  • 216
    • 2442621521 scopus 로고    scopus 로고
    • Crystal structure of an aspartate aminotransferase (TM1255) from Thermotoga maritima at 1.90 a resolution
    • Schwarzenbacher R, Jaroszewski L, von Delft F et al. (2004c) Crystal structure of an aspartate aminotransferase (TM1255) from Thermotoga maritima at 1.90 A resolution. Proteins 55: 759-763.
    • (2004) Proteins , vol.55 , pp. 759-763
    • Schwarzenbacher, R.1    Jaroszewski, L.2    Von Delft, F.3
  • 217
    • 2442472266 scopus 로고    scopus 로고
    • Crystal structure of a type II quinolic acid phosphoribosyltransferase (TM1645) from Thermotoga maritima at 2.50 a resolution
    • Schwarzenbacher R, Jaroszewski L, von Delft F et al. (2004d) Crystal structure of a type II quinolic acid phosphoribosyltransferase (TM1645) from Thermotoga maritima at 2.50 A resolution. Proteins 55: 768-771.
    • (2004) Proteins , vol.55 , pp. 768-771
    • Schwarzenbacher, R.1    Jaroszewski, L.2    Von Delft, F.3
  • 218
    • 10744220954 scopus 로고    scopus 로고
    • Crystal structure of a putative PII-like signaling protein (TM0021) from Thermotoga maritima at 2.5 a resolution
    • Schwarzenbacher R, von Delft F, Abdubek P et al. (2004e) Crystal structure of a putative PII-like signaling protein (TM0021) from Thermotoga maritima at 2.5 A resolution. Proteins 54: 810-813.
    • (2004) Proteins , vol.54 , pp. 810-813
    • Schwarzenbacher, R.1    Von Delft, F.2    Abdubek, P.3
  • 219
    • 9144261115 scopus 로고    scopus 로고
    • Crystal structure of an iron-containing 1,3-propanediol dehydrogenase (TM0920) from Thermotoga maritima at 1.3 a resolution
    • Schwarzenbacher R, von Delft F, Canaves JM et al. (2004f) Crystal structure of an iron-containing 1,3-propanediol dehydrogenase (TM0920) from Thermotoga maritima at 1.3 A resolution. Proteins 54: 174-177.
    • (2004) Proteins , vol.54 , pp. 174-177
    • Schwarzenbacher, R.1    Von Delft, F.2    Canaves, J.M.3
  • 220
    • 3042762410 scopus 로고    scopus 로고
    • Crystal structure of a putative oxalate decarboxylase (TM1287) from Thermotoga maritima at 1.95 A resolution
    • Schwarzenbacher R, von Delft F, Jaroszewski L et al. (2004g) Crystal structure of a putative oxalate decarboxylase (TM1287) from Thermotoga maritima at 1.95 A resolution. Proteins 56: 392-395.
    • (2004) Proteins , vol.56 , pp. 392-395
    • Schwarzenbacher, R.1    Von Delft, F.2    Jaroszewski, L.3
  • 221
    • 0031002263 scopus 로고    scopus 로고
    • Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga
    • Selig M, Xavier KB, Santos H & Schonheit P (1997) Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga. Arch Microbiol 167: 217-232.
    • (1997) Arch Microbiol , vol.167 , pp. 217-232
    • Selig, M.1    Xavier, K.B.2    Santos, H.3    Schonheit, P.4
  • 222
    • 0033579365 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima ribosome recycling factor: A tRNA mimic
    • Selmer M, Al-Karadaghi S, Hirokawa G, Kaji A & Liljas A (1999a) Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic. Science 286: 2349-2352.
    • (1999) Science , vol.286 , pp. 2349-2352
    • Selmer, M.1    Al-Karadaghi, S.2    Hirokawa, G.3    Kaji, A.4    Liljas, A.5
  • 224
    • 0345254951 scopus 로고    scopus 로고
    • Crystal structure of NusA from Thermotoga maritima and functional implication of the N-terminal domain
    • Shin DH, Nguyen HH, Jancarik J, Yokota H, Kim R & Kim SH (2003a) Crystal structure of NusA from Thermotoga maritima and functional implication of the N-terminal domain. Biochemistry (Moscow) 42: 13429-13437.
    • (2003) Biochemistry (Moscow) , vol.42 , pp. 13429-13437
    • Shin, D.H.1    Nguyen, H.H.2    Jancarik, J.3    Yokota, H.4    Kim, R.5    Kim, S.H.6
  • 225
    • 0037633997 scopus 로고    scopus 로고
    • Crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima
    • Shin DH, Roberts A, Jancarik J, Yokota H, Kim R, Wemmer DE & Kim SH (2003b) Crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima. Protein Sci 12: 1464-1472.
    • (2003) Protein Sci , vol.12 , pp. 1464-1472
    • Shin, D.H.1    Roberts, A.2    Jancarik, J.3    Yokota, H.4    Kim, R.5    Wemmer, D.E.6    Kim, S.H.7
  • 226
    • 4143064788 scopus 로고    scopus 로고
    • Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome
    • Shin DH, Brandsen J, Jancarik J, Yokota H, Kim R & Kim SH (2004a) Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome. J Mol Biol 341: 227-239.
    • (2004) J Mol Biol , vol.341 , pp. 227-239
    • Shin, D.H.1    Brandsen, J.2    Jancarik, J.3    Yokota, H.4    Kim, R.5    Kim, S.H.6
  • 227
    • 4444285829 scopus 로고    scopus 로고
    • Crystal structure of YjeQ from Thermotoga maritima contains a circularly permuted GTPase domain
    • Shin DH, Lou Y, Jancarik J, Yokota H, Kim R & Kim SH (2004b) Crystal structure of YjeQ from Thermotoga maritima contains a circularly permuted GTPase domain. Proc Natl Acad Sci USA 101: 13198-13203.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13198-13203
    • Shin, D.H.1    Lou, Y.2    Jancarik, J.3    Yokota, H.4    Kim, R.5    Kim, S.H.6
  • 230
    • 3342952192 scopus 로고    scopus 로고
    • Crystal structure of the reaction complex of 3-deoxy-D-arabino- heptulosonate-7-phosphate synthase from Thermotoga maritima refines the catalytic mechanism and indicates a new mechanism of allosteric regulation
    • Shumilin IA, Bauerle R, Wu J, Woodard RW & Kretsinger RH (2004) Crystal structure of the reaction complex of 3-deoxy-D-arabino-heptulosonate-7- phosphate synthase from Thermotoga maritima refines the catalytic mechanism and indicates a new mechanism of allosteric regulation. J Mol Biol 341: 455-466.
    • (2004) J Mol Biol , vol.341 , pp. 455-466
    • Shumilin, I.A.1    Bauerle, R.2    Wu, J.3    Woodard, R.W.4    Kretsinger, R.H.5
  • 231
    • 0025870894 scopus 로고
    • An extremely thermostable xylanase from the thermophilic eubacterium Thermotoga
    • Simpson HD, Haufler UR & Daniel RM (1991) An extremely thermostable xylanase from the thermophilic eubacterium Thermotoga. Biochem J 277: 413-417.
    • (1991) Biochem J , vol.277 , pp. 413-417
    • Simpson, H.D.1    Haufler, U.R.2    Daniel, R.M.3
  • 232
    • 0034435877 scopus 로고    scopus 로고
    • Crystal structure of protein isoaspartyl methyltransferase: A catalyst for protein repair
    • Skinner MM, Puvathingal JM, Walter RL & Friedman AM (2000) Crystal structure of protein isoaspartyl methyltransferase: a catalyst for protein repair. Structure Fold Des 8: 1189-1201.
    • (2000) Structure Fold des , vol.8 , pp. 1189-1201
    • Skinner, M.M.1    Puvathingal, J.M.2    Walter, R.L.3    Friedman, A.M.4
  • 233
    • 0034666108 scopus 로고    scopus 로고
    • STRING: A web-server to retrieve and display the repeatedly occurring neighbourhood of a gene
    • Snel B, Lehmann G, Bork P & Huynen MA (2000) STRING: a web-server to retrieve and display the repeatedly occurring neighbourhood of a gene. Nucleic Acids Res 28: 3442-3444.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3442-3444
    • Snel, B.1    Lehmann, G.2    Bork, P.3    Huynen, M.A.4
  • 234
    • 0037438628 scopus 로고    scopus 로고
    • Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV
    • Song HK, Bochtler M, Azim MK, Hartmann C, Huber R & Ramachandran R (2003) Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV. Biophys Chem 100: 437-452.
    • (2003) Biophys Chem , vol.100 , pp. 437-452
    • Song, H.K.1    Bochtler, M.2    Azim, M.K.3    Hartmann, C.4    Huber, R.5    Ramachandran, R.6
  • 235
    • 9344256689 scopus 로고    scopus 로고
    • On the use of DXMS to produce more crystallizable proteins: Structures of the T. maritima proteins TM0160 and TM1171
    • Spraggon G, Pantazatos D, Klock HE, Wilson IA, Woods VL Jr & Lesley SA (2004a) On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171. Protein Sci 13: 3187-3199.
    • (2004) Protein Sci , vol.13 , pp. 3187-3199
    • Spraggon, G.1    Pantazatos, D.2    Klock, H.E.3    Wilson, I.A.4    Woods Jr., V.L.5    Lesley, S.A.6
  • 236
    • 2542587769 scopus 로고    scopus 로고
    • Crystal structure of an Udp-N-acetylmuramate-alanine ligase MurC (TM0231) from Thermotoga maritima at 2.3 Å resolution
    • Spraggon G, Schwarzenbacher R, Kreusch A et al. (2004b) Crystal structure of an Udp-N-acetylmuramate-alanine ligase MurC (TM0231) from Thermotoga maritima at 2.3 Å resolution. Proteins 55: 1078-1081.
    • (2004) Proteins , vol.55 , pp. 1078-1081
    • Spraggon, G.1    Schwarzenbacher, R.2    Kreusch, A.3
  • 237
    • 3042724734 scopus 로고    scopus 로고
    • Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 Å resolution
    • Spraggon G, Schwarzenbacher R, Kreusch A et al. (2004c) Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 Å resolution. Proteins 56: 396-400.
    • (2004) Proteins , vol.56 , pp. 396-400
    • Spraggon, G.1    Schwarzenbacher, R.2    Kreusch, A.3
  • 238
    • 0034073503 scopus 로고    scopus 로고
    • Molecular determinants of xylose isomerase thermal stability and activity: Analysis of thermozymes by site-directed mutagenesis
    • Sriprapundh D, Vieille C & Zeikus JG (2000) Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis. Protein Eng 13: 259-265.
    • (2000) Protein Eng , vol.13 , pp. 259-265
    • Sriprapundh, D.1    Vieille, C.2    Zeikus, J.G.3
  • 239
    • 0142215371 scopus 로고    scopus 로고
    • Directed evolution of Thermotoga neapolitana xylose isomerase: High activity on glucose at low temperature and low pH
    • Sriprapundh D, Vieille C & Zeikus JG (2003) Directed evolution of Thermotoga neapolitana xylose isomerase: high activity on glucose at low temperature and low pH. Protein Eng 16: 683-690.
    • (2003) Protein Eng , vol.16 , pp. 683-690
    • Sriprapundh, D.1    Vieille, C.2    Zeikus, J.G.3
  • 241
    • 0026485198 scopus 로고
    • Partial purification and characterization of mannitol: Mannose 1-oxidoreductase from celeriac (Apium graveolens var. rapaceum) roots
    • Stoop JM & Pharr DM (1992) Partial purification and characterization of mannitol: mannose 1-oxidoreductase from celeriac (Apium graveolens var. rapaceum) roots. Arch Biochem Biophys 298: 612-619.
    • (1992) Arch Biochem Biophys , vol.298 , pp. 612-619
    • Stoop, J.M.1    Pharr, D.M.2
  • 242
    • 1842477147 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis
    • Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B & Bourne Y (2004) Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis. J Biol Chem 279: 13119-13128.
    • (2004) J Biol Chem , vol.279 , pp. 13119-13128
    • Sulzenbacher, G.1    Bignon, C.2    Nishimura, T.3    Tarling, C.A.4    Withers, S.G.5    Henrissat, B.6    Bourne, Y.7
  • 243
    • 0037165613 scopus 로고    scopus 로고
    • Evidence that the putative alpha-glucosidase of Thermotoga maritima MSB8 is a pNP alpha-D-glucuronopyranoside hydrolyzing alpha-glucuronidase
    • Suresh C, Rus'd AA, Kitaoka M & Hayashi K (2002) Evidence that the putative alpha-glucosidase of Thermotoga maritima MSB8 is a pNP alpha-D-glucuronopyranoside hydrolyzing alpha-glucuronidase. FEBS Lett 517: 159-162.
    • (2002) FEBS Lett , vol.517 , pp. 159-162
    • Suresh, C.1    Rus'D, A.A.2    Kitaoka, M.3    Hayashi, K.4
  • 244
    • 3042846865 scopus 로고    scopus 로고
    • A thermostable non-xylanolytic alpha-glucuronidase of Thermotoga maritima MSB8
    • Suresh C, Kitaoka M & Hayashi K (2003) A thermostable non-xylanolytic alpha-glucuronidase of Thermotoga maritima MSB8. Biosci Biotechnol Biochem 67: 2359-2364.
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 2359-2364
    • Suresh, C.1    Kitaoka, M.2    Hayashi, K.3
  • 245
    • 4944247158 scopus 로고    scopus 로고
    • Functional and structural analysis of HrcA repressor protein from Caulobacter crescentus
    • Susin MF, Perez HR, Baldini RL & Gomes SL (2004) Functional and structural analysis of HrcA repressor protein from Caulobacter crescentus. J Bacteriol 186: 6759-6767.
    • (2004) J Bacteriol , vol.186 , pp. 6759-6767
    • Susin, M.F.1    Perez, H.R.2    Baldini, R.L.3    Gomes, S.L.4
  • 247
    • 0034815472 scopus 로고    scopus 로고
    • Thermotoga petrophila sp. nov. and Thermotoga naphthophila sp. nov., two hyperthermophilic bacteria from the Kubiki oil reservoir in Niigata, Japan
    • Takahata Y, Nishijima M, Hoaki T & Maruyama T (2001) Thermotoga petrophila sp. nov. and Thermotoga naphthophila sp. nov., two hyperthermophilic bacteria from the Kubiki oil reservoir in Niigata, Japan. Int J Syst Evol Microbiol 51: 1901-1909.
    • (2001) Int J Syst Evol Microbiol , vol.51 , pp. 1901-1909
    • Takahata, Y.1    Nishijima, M.2    Hoaki, T.3    Maruyama, T.4
  • 248
    • 3142721163 scopus 로고    scopus 로고
    • Concerted action of diacetylchitobiose deacetylase and Exo-ss-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Tanaka T, Fukui T, Fujiwara S, Atomi H & Imanaka T (2004) Concerted action of diacetylchitobiose deacetylase and Exo-ss-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J Biol Chem 279: 30021-30027.
    • (2004) J Biol Chem , vol.279 , pp. 30021-30027
    • Tanaka, T.1    Fukui, T.2    Fujiwara, S.3    Atomi, H.4    Imanaka, T.5
  • 249
    • 0346220296 scopus 로고    scopus 로고
    • Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Thermotoga maritima through trapping of a covalent glycosylenzyme intermediate and mutagenesis
    • Tarling CA, He S, Sulzenbacher G, Bignon C, Bourne Y, Henrissat B & Withers SG (2003) Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Thermotoga maritima through trapping of a covalent glycosylenzyme intermediate and mutagenesis. J Biol Chem 278: 47394-47399.
    • (2003) J Biol Chem , vol.278 , pp. 47394-47399
    • Tarling, C.A.1    He, S.2    Sulzenbacher, G.3    Bignon, C.4    Bourne, Y.5    Henrissat, B.6    Withers, S.G.7
  • 250
    • 3843069972 scopus 로고    scopus 로고
    • Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation
    • Tischler AD & Camilli A (2004) Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation. Mol Microbiol 53: 857-869.
    • (2004) Mol Microbiol , vol.53 , pp. 857-869
    • Tischler, A.D.1    Camilli, A.2
  • 252
    • 0034651835 scopus 로고    scopus 로고
    • The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway
    • Toth EA & Yeates TO (2000) The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway. Structure Fold Des 8: 163-174.
    • (2000) Structure Fold des , vol.8 , pp. 163-174
    • Toth, E.A.1    Yeates, T.O.2
  • 253
    • 0034675921 scopus 로고    scopus 로고
    • Crystal structure of the cell division protein FtsA from Thermotoga maritima
    • van den Ent F & Lowe J (2000) Crystal structure of the cell division protein FtsA from Thermotoga maritima. EMBO J 19: 5300-5307.
    • (2000) EMBO J , vol.19 , pp. 5300-5307
    • Van Den Ent, F.1    Lowe, J.2
  • 254
    • 0036237024 scopus 로고    scopus 로고
    • Hydrogen production by the thermophilic bacterium Thermotoga neapolitana
    • Van Ooteghem SA, Beer SK & Yue PC (2002) Hydrogen production by the thermophilic bacterium Thermotoga neapolitana. Appl Biochem Biotechnol 98-100: 177-189.
    • (2002) Appl Biochem Biotechnol , vol.98-100 , pp. 177-189
    • Van Ooteghem, S.A.1    Beer, S.K.2    Yue, P.C.3
  • 255
    • 13544259604 scopus 로고    scopus 로고
    • H(2) production and carbon utilization by Thermotoga neapolitana under anaerobic and microaerobic growth conditions
    • Van Ooteghem SA, Jones A, Van Der Lelie D, Dong B & Mahajan D (2004) H(2) production and carbon utilization by Thermotoga neapolitana under anaerobic and microaerobic growth conditions. Biotechnol Lett 26: 1223-1232.
    • (2004) Biotechnol Lett , vol.26 , pp. 1223-1232
    • Van Ooteghem, S.A.1    Jones, A.2    Van Der Lelie, D.3    Dong, B.4    Mahajan, D.5
  • 256
    • 0030053953 scopus 로고    scopus 로고
    • Catabolite repression in the hyperthermophilic bacterium Thermotoga neapolitana is independent of cAMP
    • Vargas M & Noll KM (1996) Catabolite repression in the hyperthermophilic bacterium Thermotoga neapolitana is independent of cAMP. Microbiology 142: 139-144.
    • (1996) Microbiology , vol.142 , pp. 139-144
    • Vargas, M.1    Noll, K.M.2
  • 257
    • 12544256751 scopus 로고    scopus 로고
    • NAD+and metal-ion dependent hydrolysis by family 4 glycosidases: Structural insight into specificity for phospho-beta-D-glucosides
    • Varrot A, Yip VL, Li Y, Rajan SS, Yang X, Anderson WF, Thompson J, Withers SG & Davies GJ (2005) NAD+and metal-ion dependent hydrolysis by family 4 glycosidases: structural insight into specificity for phospho-beta-D-glucosides. J Mol Biol 346: 423-435.
    • (2005) J Mol Biol , vol.346 , pp. 423-435
    • Varrot, A.1    Yip, V.L.2    Li, Y.3    Rajan, S.S.4    Yang, X.5    Anderson, W.F.6    Thompson, J.7    Withers, S.G.8    Davies, G.J.9
  • 258
  • 259
    • 0029018981 scopus 로고
    • xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana
    • Vieille C, Hess JM, Kelly RM & Zeikus JG (1995) xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana. Appl Environ Microbiol 61: 1867-1875.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1867-1875
    • Vieille, C.1    Hess, J.M.2    Kelly, R.M.3    Zeikus, J.G.4
  • 261
    • 0034677211 scopus 로고    scopus 로고
    • Flexibility, conformational diversity and two dimerization modes in complexes of ribosomal protein L12
    • Wahl MC, Bourenkov GP, Bartunik HD & Huber R (2000a) Flexibility, conformational diversity and two dimerization modes in complexes of ribosomal protein L12. EMBO J 19: 174-186.
    • (2000) EMBO J , vol.19 , pp. 174-186
    • Wahl, M.C.1    Bourenkov, G.P.2    Bartunik, H.D.3    Huber, R.4
  • 262
    • 0034075016 scopus 로고    scopus 로고
    • Structural investigations of the highly flexible recombinant ribosomal protein L12 from Thermotoga maritima
    • Wahl MC, Huber R, Marinkovic S, Weyher-Stingl E & Ehlert S (2000b) Structural investigations of the highly flexible recombinant ribosomal protein L12 from Thermotoga maritima. Biol Chem 381: 221-229.
    • (2000) Biol Chem , vol.381 , pp. 221-229
    • Wahl, M.C.1    Huber, R.2    Marinkovic, S.3    Weyher-Stingl, E.4    Ehlert, S.5
  • 263
    • 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 & Jaenicke R (1997) Xylanase XynA from the hyperthermophilic bacterium Thermotoga maritima: structure and stability of the recombinant enzyme and its isolated cellulose-binding domain. Protein Sci 6: 1718-1726.
    • (1997) Protein Sci , vol.6 , pp. 1718-1726
    • Wassenberg, D.1    Schurig, H.2    Liebl, W.3    Jaenicke, R.4
  • 264
    • 0034645778 scopus 로고    scopus 로고
    • Maltose-binding protein from the hyperthermophilic bacterium Thermotoga maritima: Stability and binding properties
    • Wassenberg D, Liebl W & 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
  • 265
    • 0043062670 scopus 로고    scopus 로고
    • Mannitol-1-phosphate dehydrogenase (MtlD) is required for mannitol and glucitol assimilation in Bacillus subtilis: Possible cooperation of mtl and gut operons
    • Watanabe S, Hamano M, Kakeshita H, Bunai K, Tojo S, Yamaguchi H, Fujita Y, Wong SL & Yamane K (2003) Mannitol-1-phosphate dehydrogenase (MtlD) is required for mannitol and glucitol assimilation in Bacillus subtilis: possible cooperation of mtl and gut operons. J Bacteriol 185: 4816-4824.
    • (2003) J Bacteriol , vol.185 , pp. 4816-4824
    • Watanabe, S.1    Hamano, M.2    Kakeshita, H.3    Bunai, K.4    Tojo, S.5    Yamaguchi, H.6    Fujita, Y.7    Wong, S.L.8    Yamane, K.9
  • 267
    • 1942438136 scopus 로고    scopus 로고
    • Analysis of orthologous hrcA genes in Escherichia coli and Bacillus subtilis
    • Wiegert T, Hagmaier K & Schumann W (2004) Analysis of orthologous hrcA genes in Escherichia coli and Bacillus subtilis. FEMS Microbiol Lett 234: 9-17.
    • (2004) FEMS Microbiol Lett , vol.234 , pp. 9-17
    • Wiegert, T.1    Hagmaier, K.2    Schumann, W.3
  • 269
    • 0028901697 scopus 로고
    • Identification of a novel cellulose-binding domain within the multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima
    • Winterhalter C, Heinrich P, Candussio A, Wich G & Liebl W (1995) Identification of a novel cellulose-binding domain within the multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima. Mol Microbiol 15: 431-444.
    • (1995) Mol Microbiol , vol.15 , pp. 431-444
    • Winterhalter, C.1    Heinrich, P.2    Candussio, A.3    Wich, G.4    Liebl, W.5
  • 271
    • 0034161434 scopus 로고    scopus 로고
    • Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon
    • Worbs M, Huber R & Wahl MC (2000) Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon. EMBO J 19: 807-818.
    • (2000) EMBO J , vol.19 , pp. 807-818
    • Worbs, M.1    Huber, R.2    Wahl, M.C.3
  • 272
    • 0034141421 scopus 로고    scopus 로고
    • Structural analysis of DNA sequence: Evidence for lateral gene transfer in Thermotoga maritima
    • Worning P, Jensen LJ, Nelson KE, Brunak S & Ussery DW (2000) Structural analysis of DNA sequence: evidence for lateral gene transfer in Thermotoga maritima. Nucleic Acids Res 28: 706-709.
    • (2000) Nucleic Acids Res , vol.28 , pp. 706-709
    • Worning, P.1    Jensen, L.J.2    Nelson, K.E.3    Brunak, S.4    Ussery, D.W.5
  • 273
    • 15544365805 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Molecular chaperone DnaK promotes IscU-bound [2Fe-2S] cluster stability and inhibits cluster transfer activity
    • Wu SP, Mansy SS & Cowan JA (2005) Iron-sulfur cluster biosynthesis. Molecular chaperone DnaK promotes IscU-bound [2Fe-2S] cluster stability and inhibits cluster transfer activity. Biochemistry (Moscow) 44: 4284-4293.
    • (2005) Biochemistry (Moscow) , vol.44 , pp. 4284-4293
    • Wu, S.P.1    Mansy, S.S.2    Cowan, J.A.3
  • 274
    • 2642584066 scopus 로고    scopus 로고
    • Crystal structure of a ribose-5-phosphate isomerase RpiB (TM1080) from Thermotoga maritima at 1.90 Å resolution
    • Xu Q, Schwarzenbacher R, McMullan D et al. (2004) Crystal structure of a ribose-5-phosphate isomerase RpiB (TM1080) from Thermotoga maritima at 1.90 Å resolution. Proteins 56: 171-175.
    • (2004) Proteins , vol.56 , pp. 171-175
    • Xu, Q.1    Schwarzenbacher, R.2    McMullan, D.3
  • 275
    • 13944282222 scopus 로고    scopus 로고
    • Crystal structure of a formiminotetrahydrofolate cyclodeaminase (TM1560) from Thermotoga maritima at 2.80 Å resolution reveals a new fold
    • Xu Q, Schwarzenbacher R, McMullan D et al. (2005) Crystal structure of a formiminotetrahydrofolate cyclodeaminase (TM1560) from Thermotoga maritima at 2.80 Å resolution reveals a new fold. Proteins 58: 976-981.
    • (2005) Proteins , vol.58 , pp. 976-981
    • Xu, Q.1    Schwarzenbacher, R.2    McMullan, D.3
  • 276
    • 21644485757 scopus 로고    scopus 로고
    • Expression and characterization of a thermostable beta-xylosidase from the hyperthermophile, Thermotoga maritima
    • Xue Y & Shao W (2004) Expression and characterization of a thermostable beta-xylosidase from the hyperthermophile, Thermotoga maritima. Biotechnol Lett 26: 1511-1515.
    • (2004) Biotechnol Lett , vol.26 , pp. 1511-1515
    • Xue, Y.1    Shao, W.2
  • 277
    • 0037424378 scopus 로고    scopus 로고
    • Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643
    • Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith C & Tong L (2003) Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643. J Biol Chem 278: 8804-8808.
    • (2003) J Biol Chem , vol.278 , pp. 8804-8808
    • Yang, Z.1    Savchenko, A.2    Yakunin, A.3    Zhang, R.4    Edwards, A.5    Arrowsmith, C.6    Tong, L.7
  • 278
    • 33344458735 scopus 로고    scopus 로고
    • Characterization of a thermostable endobeta-1,4-D-galactanase from the hyperthermophile Thermotoga maritima
    • Yang H, Ichinose H, Yoshida M, Nakajima M, Kobayashi H & Kaneko S (2006) Characterization of a thermostable endobeta-1,4-D-galactanase from the hyperthermophile Thermotoga maritima. Biosci Biotechnol Biochem 70: 538-541.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 538-541
    • Yang, H.1    Ichinose, H.2    Yoshida, M.3    Nakajima, M.4    Kobayashi, H.5    Kaneko, S.6
  • 279
    • 0033810985 scopus 로고    scopus 로고
    • Cloning and characterization of the glucooligosaccharide catabolic pathway beta-glucan glucohydrolase and cellobiose phosphorylase in the marine hyperthermophile Thermotoga neapolitana
    • Yernool DA, McCarthy JK, Eveleigh DE & Bok JD (2000) Cloning and characterization of the glucooligosaccharide catabolic pathway beta-glucan glucohydrolase and cellobiose phosphorylase in the marine hyperthermophile Thermotoga neapolitana. J Bacteriol 182: 5172-5179.
    • (2000) J Bacteriol , vol.182 , pp. 5172-5179
    • Yernool, D.A.1    McCarthy, J.K.2    Eveleigh, D.E.3    Bok, J.D.4
  • 280
    • 3142761743 scopus 로고    scopus 로고
    • An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 beta-glycosidase from Thermotoga maritima
    • Yip VL, Varrot A, Davies GJ, Rajan SS, Yang X, Thompson J, Anderson WF & Withers SG (2004) An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 beta-glycosidase from Thermotoga maritima. J Am Chem Soc 126: 8354-8355.
    • (2004) J Am Chem Soc , vol.126 , pp. 8354-8355
    • Yip, V.L.1    Varrot, A.2    Davies, G.J.3    Rajan, S.S.4    Yang, X.5    Thompson, J.6    Anderson, W.F.7    Withers, S.G.8
  • 281
    • 0035259957 scopus 로고    scopus 로고
    • Liposome-mediated DNA uptake and transient expression in Thermotoga
    • Yu JS, Vargas M, Mityas C & Noll KM (2001) Liposome-mediated DNA uptake and transient expression in Thermotoga. Extremophiles 5: 53-60.
    • (2001) Extremophiles , vol.5 , pp. 53-60
    • Yu, J.S.1    Vargas, M.2    Mityas, C.3    Noll, K.M.4
  • 283
    • 0037485102 scopus 로고    scopus 로고
    • Thermotoga maritima MazG protein has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities
    • Zhang J, Zhang Y & Inouye M (2003) Thermotoga maritima MazG protein has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities. J Biol Chem 278: 21408-21414.
    • (2003) J Biol Chem , vol.278 , pp. 21408-21414
    • Zhang, J.1    Zhang, Y.2    Inouye, M.3
  • 284
    • 0028292919 scopus 로고
    • CIRCE, a novel heat shock element involved in regulation of heat shock operon dnaK of Bacillus subtilis
    • Zuber U & Schumann W (1994) CIRCE, a novel heat shock element involved in regulation of heat shock operon dnaK of Bacillus subtilis. J Bacteriol 176: 1359-1363.
    • (1994) J Bacteriol , vol.176 , pp. 1359-1363
    • Zuber, U.1    Schumann, W.2
  • 285
    • 0029916417 scopus 로고    scopus 로고
    • The multidomain xylanase a of the hyperthermophilic bacterium Thermotoga neapolitana is extremely thermoresistant
    • Zverlov V, Piotukh K, Dakhova O, Velikodvorskaya G & Borriss R (1996) The multidomain xylanase A of the hyperthermophilic bacterium Thermotoga neapolitana is extremely thermoresistant. Appl Microbiol Biotechnol 45: 245-247.
    • (1996) Appl Microbiol Biotechnol , vol.45 , pp. 245-247
    • Zverlov, V.1    Piotukh, K.2    Dakhova, O.3    Velikodvorskaya, G.4    Borriss, R.5
  • 286
    • 0030680965 scopus 로고    scopus 로고
    • Thermotoga neapolitana bglB gene, upstream of lamA, encodes a highly thermostable beta-glucosidase that is a laminaribiase
    • Zverlov VV, Volkov IY, Velikodvorskaya TV & Schwarz WH (1997a) Thermotoga neapolitana bglB gene, upstream of lamA, encodes a highly thermostable beta-glucosidase that is a laminaribiase. Microbiology 143: 3537-3542.
    • (1997) Microbiology , vol.143 , pp. 3537-3542
    • Zverlov, V.V.1    Volkov, I.Y.2    Velikodvorskaya, T.V.3    Schwarz, W.H.4
  • 287
    • 0030943791 scopus 로고    scopus 로고
    • Highly thermostable endo-1,3-beta-glucanase (laminarinase) LamA from Thermotoga neapolitana: Nucleotide sequence of the gene and characterization of the recombinant gene product
    • Zverlov VV, Volkov IY, Velikodvorskaya TV & Schwarz WH (1997b) Highly thermostable endo-1,3-beta-glucanase (laminarinase) LamA from Thermotoga neapolitana: nucleotide sequence of the gene and characterization of the recombinant gene product. Microbiology 143: 1701-1708.
    • (1997) Microbiology , vol.143 , pp. 1701-1708
    • Zverlov, V.V.1    Volkov, I.Y.2    Velikodvorskaya, T.V.3    Schwarz, W.H.4
  • 288
    • 0035078068 scopus 로고    scopus 로고
    • The binding pattern of two carbohydrate-binding modules of laminarinase Lam16A from Thermotoga neapolitana: Differences in beta-glucan binding within family CBM4
    • Zverlov VV, Volkov IY, Velikodvorskaya GA & Schwarz WH (2001) The binding pattern of two carbohydrate-binding modules of laminarinase Lam16A from Thermotoga neapolitana: differences in beta-glucan binding within family CBM4. Microbiology 147: 621-629.
    • (2001) Microbiology , vol.147 , pp. 621-629
    • Zverlov, V.V.1    Volkov, I.Y.2    Velikodvorskaya, G.A.3    Schwarz, W.H.4


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