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Volumn 4, Issue 4, 2013, Pages

Structure and evolution of chlorate reduction composite transposons

Author keywords

[No Author keywords available]

Indexed keywords

CHLORATE; DIMETHYL SULFOXIDE; PERCHLORATE; TYPE II DIMETHYL SULFOXIDE; UNCLASSIFIED DRUG;

EID: 84883390764     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00379-13     Document Type: Article
Times cited : (54)

References (74)
  • 3
    • 79551491420 scopus 로고    scopus 로고
    • Perchlorate sources, source identification and analytical methods
    • In Stroo HF, Ward CH (ed), Springer Verlag, New York, NY
    • Aziz CE, Hatzinger PB. 2009. Perchlorate sources, source identification and analytical methods, p-55-78. In Stroo HF, Ward CH (ed), In situ bioremediation of perchlorate in groundwater. Springer Verlag, New York, NY.
    • (2009) In situ bioremediation of perchlorate in groundwater , pp. 55-78
    • Aziz, C.E.1    Hatzinger, P.B.2
  • 4
    • 20044379052 scopus 로고    scopus 로고
    • Perchlorate biodegradation for water treatment
    • Hatzinger PB. 2005. Perchlorate biodegradation for water treatment. Environ. Sci. Technol. 39:239A-247A.
    • (2005) Environ. Sci. Technol. , vol.39
    • Hatzinger, P.B.1
  • 5
    • 3142726522 scopus 로고    scopus 로고
    • Microbial perchlorate reduction: Rocket-fuelled metabolism
    • Coates JD, Achenbach LA. 2004. Microbial perchlorate reduction: rocket-fuelled metabolism. Nat. Rev. Microbiol. 2:569-580.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 569-580
    • Coates, J.D.1    Achenbach, L.A.2
  • 8
    • 38349103353 scopus 로고    scopus 로고
    • (Per)chlorate reduction by the thermophilic bacterium Moorella perchloratireducens sp. nov., isolated from underground gas storage
    • Balk M, van Gelder T, Weelink SA, Stams AJ. 2008. (Per)chlorate reduction by the thermophilic bacterium Moorella perchloratireducens sp. nov., isolated from underground gas storage. Appl. Environ. Microbiol. 74:403-409.
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 403-409
    • Balk, M.1    van Gelder, T.2    Weelink, S.A.3    Stams, A.J.4
  • 9
    • 0032729246 scopus 로고    scopus 로고
    • Purification and characterization of (per)chlorate reductase from the chlorate-respiring strain GR-1
    • Kengen SW, Rikken GB, Hagen WR, van Ginkel CG, Stams AJ. 1999. Purification and characterization of (per)chlorate reductase from the chlorate-respiring strain GR-1. J. Bacteriol. 181:6706-6711.
    • (1999) J. Bacteriol. , vol.181 , pp. 6706-6711
    • Kengen, S.W.1    Rikken, G.B.2    Hagen, W.R.3    van Ginkel, C.G.4    Stams, A.J.5
  • 12
    • 20444387562 scopus 로고    scopus 로고
    • Enzymes responsible for chlorate reduction by Pseudomonas sp. are different from those used for perchlorate reduction by Azospira sp
    • Steinberg LM, Trimble JJ, Logan BE. 2005. Enzymes responsible for chlorate reduction by Pseudomonas sp. are different from those used for perchlorate reduction by Azospira sp. FEMS Microbiol. Lett. 247:153-159.
    • (2005) FEMS Microbiol. Lett. , vol.247 , pp. 153-159
    • Steinberg, L.M.1    Trimble, J.J.2    Logan, B.E.3
  • 14
    • 33748296263 scopus 로고    scopus 로고
    • Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum
    • Kloer DP, Hagel C, Heider J, Schulz GE. 2006. Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum. Structure 14:1377-1388.
    • (2006) Structure , vol.14 , pp. 1377-1388
    • Kloer, D.P.1    Hagel, C.2    Heider, J.3    Schulz, G.E.4
  • 16
    • 18144412396 scopus 로고    scopus 로고
    • The C subunit of Ideonella dechloratans chlorate reductase: Expression, purification, refolding, and heme reconstitution
    • Karlsson J, Nilsson T. 2005. The C subunit of Ideonella dechloratans chlorate reductase: expression, purification, refolding, and heme reconstitution. Protein Expr. Purif. 41:306-312.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 306-312
    • Karlsson, J.1    Nilsson, T.2
  • 18
    • 33644872480 scopus 로고    scopus 로고
    • NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly
    • Vergnes A, Pommier J, Toci R, Blasco F, Giordano G, Magalon A. 2006. NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly. J. Biol. Chem. 281:2170-2176.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2170-2176
    • Vergnes, A.1    Pommier, J.2    Toci, R.3    Blasco, F.4    Giordano, G.5    Magalon, A.6
  • 21
    • 0020014674 scopus 로고
    • Bidirectional deletions associated with IS4
    • Habermann P, Starlinger P. 1982. Bidirectional deletions associated with IS4. Mol. Gen. Genet. 185:216-222.
    • (1982) Mol. Gen. Genet. , vol.185 , pp. 216-222
    • Habermann, P.1    Starlinger, P.2
  • 22
    • 0022394254 scopus 로고
    • Dehalogenase genes of Pseudomonas putida PP3 on chromosomally located transposable elements
    • Slater JH, Weightman AJ, Hall BG. 1985. Dehalogenase genes of Pseudomonas putida PP3 on chromosomally located transposable elements. Mol. Biol. Evol. 2:557-567.
    • (1985) Mol. Biol. Evol. , vol.2 , pp. 557-567
    • Slater, J.H.1    Weightman, A.J.2    Hall, B.G.3
  • 23
    • 0025940311 scopus 로고
    • Chlorobenzoate catabolic transposon Tn5271 is a composite class I element with flanking class II insertion sequences
    • Nakatsu C, Ng J, Singh R, Straus N, Wyndham C. 1991. Chlorobenzoate catabolic transposon Tn5271 is a composite class I element with flanking class II insertion sequences. Proc. Natl. Acad. Sci. USA 88:8312-8316.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8312-8316
    • Nakatsu, C.1    Ng, J.2    Singh, R.3    Straus, N.4    Wyndham, C.5
  • 24
    • 77950658346 scopus 로고    scopus 로고
    • Improving draft assemblies by iterative mapping and assembly of short reads to eliminate gaps
    • doi: 10.1186/gb-2010-11-4-r41
    • Tsai IJ, Otto TD, Berriman M. 2010. Improving draft assemblies by iterative mapping and assembly of short reads to eliminate gaps. Genome Biol. 11:R41. doi: 10.1186/gb-2010-11-4-r41.
    • (2010) Genome Biol. , vol.11
    • Tsai, I.J.1    Otto, T.D.2    Berriman, M.3
  • 25
    • 0036889289 scopus 로고    scopus 로고
    • A third transposable element, ISPpu12, from the toluene-xylene catabolic plasmid pWW0 of Pseudomonas putida mt-2
    • Williams PA, Jones RM, Shaw LE. 2002. A third transposable element, ISPpu12, from the toluene-xylene catabolic plasmid pWW0 of Pseudomonas putida mt-2. J. Bacteriol. 184:6572-6580.
    • (2002) J. Bacteriol. , vol.184 , pp. 6572-6580
    • Williams, P.A.1    Jones, R.M.2    Shaw, L.E.3
  • 26
    • 0036889485 scopus 로고    scopus 로고
    • Transposition of DEH, a broad-host-range transposon flanked by ISPpu12, in Pseudomonas putida is associated with genomic rearrangements and dehalogenase gene silencing
    • Weightman AJ, Topping AW, Hill KE, Lee LL, Sakai K, Slater JH, Thomas AW. 2002. Transposition of DEH, a broad-host-range transposon flanked by ISPpu12, in Pseudomonas putida is associated with genomic rearrangements and dehalogenase gene silencing. J. Bacteriol. 184:6581-6591.
    • (2002) J. Bacteriol. , vol.184 , pp. 6581-6591
    • Weightman, A.J.1    Topping, A.W.2    Hill, K.E.3    Lee, L.L.4    Sakai, K.5    Slater, J.H.6    Thomas, A.W.7
  • 27
  • 28
    • 0028303763 scopus 로고
    • Ideonella dechloratans gen. nov., sp. nov., a new bacterium capable of growing anaerobically with chlorate as an electron acceptor
    • Malmqvist Å, Welander T, Moore E, Ternström A, Molin G, Stenström IM. 1994. Ideonella dechloratans gen. nov., sp. nov., a new bacterium capable of growing anaerobically with chlorate as an electron acceptor. Syst. Appl. Microbiol. 17:58-64.
    • (1994) Syst. Appl. Microbiol , vol.17 , pp. 58-64
    • Malmqvist, A.1    Welander, T.2    Moore, E.3    Ternström, A.4    Molin, G.5    Stenström, I.M.6
  • 29
    • 0037184266 scopus 로고    scopus 로고
    • Cloning, characterisation, and expression of a novel gene encoding chlorite dismutase from Ideonella dechloratans
    • Thorell HD, Karlsson J, Portelius E, Nilsson T. 2002. Cloning, characterisation, and expression of a novel gene encoding chlorite dismutase from Ideonella dechloratans. Biochim. Biophys. Acta 1577:445-451.
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 445-451
    • Thorell, H.D.1    Karlsson, J.2    Portelius, E.3    Nilsson, T.4
  • 30
    • 77956178000 scopus 로고    scopus 로고
    • Characterization of a cytochrome c gene located at the gene cluster for chlorate respiration in Ideonella dechloratans
    • Bohlin J, Bäcklund AS, Gustavsson N, Wahlberg S, Nilsson T. 2010. Characterization of a cytochrome c gene located at the gene cluster for chlorate respiration in Ideonella dechloratans. Microbiol. Res. 165: 450-457.
    • (2010) Microbiol. Res. , vol.165 , pp. 450-457
    • Bohlin, J.1    Bäcklund, A.S.2    Gustavsson, N.3    Wahlberg, S.4    Nilsson, T.5
  • 32
    • 0037096131 scopus 로고    scopus 로고
    • Evidence of perchlorate (ClO4-) reduction in plant tissues (poplar tree) using radio-labeled 36ClO4
    • Van Aken B, Schnoor JL. 2002. Evidence of perchlorate (ClO4-) reduction in plant tissues (poplar tree) using radio-labeled 36ClO4. Environ. Sci. Technol. 36:2783-2788.
    • (2002) Environ. Sci. Technol. , vol.36 , pp. 2783-2788
    • van Aken, B.1    Schnoor, J.L.2
  • 33
    • 0019774547 scopus 로고
    • Excision of the 40kb segment of the TOL plasmid from Pseudomonas putida mt-2 involves direct repeats
    • Meulien P, Downing RG, Broda P. 1981. Excision of the 40kb segment of the TOL plasmid from Pseudomonas putida mt-2 involves direct repeats. Mol. Gen. Genet. 184:97-101.
    • (1981) Mol. Gen. Genet. , vol.184 , pp. 97-101
    • Meulien, P.1    Downing, R.G.2    Broda, P.3
  • 34
  • 35
    • 0036866550 scopus 로고    scopus 로고
    • Pseudomonas chloritidismutans sp. nov., A non-denitrifying, chlorate-reducing bacterium
    • Wolterink AF, Jonker AB, Kengen SW, Stams AJ. 2002. Pseudomonas chloritidismutans sp. nov., A non-denitrifying, chlorate-reducing bacterium. Int. J. Syst. Evol. Microbiol. 52:2183-2190.
    • (2002) Int. J. Syst. Evol. Microbiol , vol.52 , pp. 2183-2190
    • Wolterink, A.F.1    Jonker, A.B.2    Kengen, S.W.3    Stams, A.J.4
  • 37
    • 0346056945 scopus 로고    scopus 로고
    • Chlorate and nitrate reduction pathways are separately induced in the perchlorate-respiring bacterium Dechlorosoma sp. KJ and the chlorate-respiring bacterium Pseudomonas sp. PDA
    • Xu J, Trimble JJ, Steinberg L, Logan BE. 2004. Chlorate and nitrate reduction pathways are separately induced in the perchlorate-respiring bacterium Dechlorosoma sp. KJ and the chlorate-respiring bacterium Pseudomonas sp. PDA. Water Res. 38:673-680.
    • (2004) Water Res. , vol.38 , pp. 673-680
    • Xu, J.1    Trimble, J.J.2    Steinberg, L.3    Logan, B.E.4
  • 38
    • 30844460335 scopus 로고    scopus 로고
    • Genotype versus phenotype in the circumscription of bacterial species: The case of Pseudomonas stutzeri and Pseudomonas chloritidismutans
    • Cladera AM, García-Valdés E, Lalucat J. 2006. Genotype versus phenotype in the circumscription of bacterial species: the case of Pseudomonas stutzeri and Pseudomonas chloritidismutans. Arch. Microbiol. 184: 353-361.
    • (2006) Arch. Microbiol. , vol.184 , pp. 353-361
    • Cladera, A.M.1    García-Valdés, E.2    Lalucat, J.3
  • 39
    • 0034830306 scopus 로고    scopus 로고
    • Properties of a thermostable nitrate reductase from the hyperthermophilic archaeon Pyrobaculum aerophilum
    • Afshar S, Johnson E, de Vries S, Schröder I. 2001. Properties of a thermostable nitrate reductase from the hyperthermophilic archaeon Pyrobaculum aerophilum. J. Bacteriol. 183:5491-5495.
    • (2001) J. Bacteriol. , vol.183 , pp. 5491-5495
    • Afshar, S.1    Johnson, E.2    de Vries, S.3    Schröder, I.4
  • 40
    • 0034708409 scopus 로고    scopus 로고
    • Purification and characterization of dissimilatory nitrate reductase from a denitrifying halophilic archaeon, Haloarcula marismortui
    • Yoshimatsu K, Sakurai T, Fujiwara T. 2000. Purification and characterization of dissimilatory nitrate reductase from a denitrifying halophilic archaeon, Haloarcula marismortui. FEBS Lett. 470:216-220.
    • (2000) FEBS Lett. , vol.470 , pp. 216-220
    • Yoshimatsu, K.1    Sakurai, T.2    Fujiwara, T.3
  • 41
    • 0025333241 scopus 로고    scopus 로고
    • Periplasmic and membranebound respiratory nitrate reductases in Thiosphaera pantotropha. The periplasmic enzyme catalyzes the first step in aerobic denitrification
    • Bell LC, Richardson DJ, Ferguson SJ. 2001. Periplasmic and membranebound respiratory nitrate reductases in Thiosphaera pantotropha. The periplasmic enzyme catalyzes the first step in aerobic denitrification. FEBS Lett. 265:85-87.
    • (2001) FEBS Lett. , vol.265 , pp. 85-87
    • Bell, L.C.1    Richardson, D.J.2    Ferguson, S.J.3
  • 42
    • 0023906754 scopus 로고
    • Nitrate respiration in relation to facultative metabolism in enterobacteria
    • Stewart V. 1988. Nitrate respiration in relation to facultative metabolism in enterobacteria. Microbiol. Rev. 52:190-232.
    • (1988) Microbiol. Rev. , vol.52 , pp. 190-232
    • Stewart, V.1
  • 43
    • 0000043258 scopus 로고    scopus 로고
    • Perchlorate chemistry: Implications for analysis and remediation
    • Urbansky ET. 1998. Perchlorate chemistry: implications for analysis and remediation. Bioremediat. J. 2:81-85.
    • (1998) Bioremediat. J. , vol.2 , pp. 81-85
    • Urbansky, E.T.1
  • 47
    • 4644239140 scopus 로고    scopus 로고
    • Metabolic primers for detection of (per)chlorate-reducing bacteria in the environment and phylogenetic analysis of cld gene sequences
    • Bender KS, Rice MR, Fugate WH, Coates JD, Achenbach LA. 2004. Metabolic primers for detection of (per)chlorate-reducing bacteria in the environment and phylogenetic analysis of cld gene sequences. Appl. Environ. Microbiol. 70:5651-5658.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 5651-5658
    • Bender, K.S.1    Rice, M.R.2    Fugate, W.H.3    Coates, J.D.4    Achenbach, L.A.5
  • 49
    • 77956480280 scopus 로고    scopus 로고
    • Structural features promoting dioxygen production by Dechloromonas aromatica chlorite dismutase
    • Goblirsch BR, Streit BR, Dubois JL, Wilmot CM. 2010. Structural features promoting dioxygen production by Dechloromonas aromatica chlorite dismutase. J. Biol. Inorg. Chem. 15:879-888.
    • (2010) J. Biol. Inorg. Chem. , vol.15 , pp. 879-888
    • Goblirsch, B.R.1    Streit, B.R.2    Dubois, J.L.3    Wilmot, C.M.4
  • 52
    • 77958161524 scopus 로고    scopus 로고
    • Structural and functional characterisation of the chlorite dismutase from the nitrite-oxidizing bacterium Candidatus Nitrospira defluvii identification of a catalytically important amino acid residue
    • Kostan J, Sjöblom B, Maixner F, Mlynek G, Furtmüller PG, Obinger C, Wagner M, Daims H, Djinović-Carugo K. 2010. Structural and functional characterisation of the chlorite dismutase from the nitrite-oxidizing bacterium Candidatus Nitrospira defluvii identification of a catalytically important amino acid residue. J. Struct. Biol. 172:331-342.
    • (2010) J. Struct. Biol. , vol.172 , pp. 331-342
    • Kostan, J.1    Sjöblom, B.2    Maixner, F.3    Mlynek, G.4    Furtmüller, P.G.5    Obinger, C.6    Wagner, M.7    Daims, H.8    Djinović-Carugo, K.9
  • 54
    • 0036016822 scopus 로고    scopus 로고
    • Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: Its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes
    • McDevitt CA, Hugenholtz P, Hanson GR, McEwan AG. 2002. Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes. Mol. Microbiol. 44: 1575-1587.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1575-1587
    • McDevitt, C.A.1    Hugenholtz, P.2    Hanson, G.R.3    McEwan, A.G.4
  • 56
    • 79960364988 scopus 로고    scopus 로고
    • Purification and characterization of a soluble cytochrome c capable of delivering electrons to chlorate reductase in Ideonella dechloratans
    • Bäcklund AS, Nilsson T. 2011. Purification and characterization of a soluble cytochrome c capable of delivering electrons to chlorate reductase in Ideonella dechloratans. FEMS Microbiol. Lett. 321:115-120.
    • (2011) FEMS Microbiol. Lett. , vol.321 , pp. 115-120
    • Bäcklund, A.S.1    Nilsson, T.2
  • 57
    • 79959931985 scopus 로고    scopus 로고
    • HMMER web server: Interactive sequence similarity searching
    • doi: 10.1093/nar/gkr367
    • Finn RD, Clements J, Eddy SR. 2011. HMMER web server: interactive sequence similarity searching. Nucleic Acids Res. 39:W29-W37. doi: 10.1093/nar/gkr367.
    • (2011) Nucleic Acids Res. , vol.39
    • Finn, R.D.1    Clements, J.2    Eddy, S.R.3
  • 58
    • 0035900575 scopus 로고    scopus 로고
    • Two c-type cytochromes, NirM and NirC, encoded in the nir gene cluster of Pseudomonas aeruginosa act as electron donors for nitrite reductase
    • Hasegawa N, Arai H, Igarashi Y. 2001. Two c-type cytochromes, NirM and NirC, encoded in the nir gene cluster of Pseudomonas aeruginosa act as electron donors for nitrite reductase. Biochem. Biophys. Res. Commun. 288:1223-1230.
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 1223-1230
    • Hasegawa, N.1    Arai, H.2    Igarashi, Y.3
  • 59
    • 84864082365 scopus 로고    scopus 로고
    • Expression of chlorite dismutase and chlorate reductase in the presence of oxygen and/or chlorate as the terminal electron acceptor in Ideonella dechloratans
    • Lindqvist MH, Johansson N, Nilsson T, Rova M. 2012. Expression of chlorite dismutase and chlorate reductase in the presence of oxygen and/or chlorate as the terminal electron acceptor in Ideonella dechloratans. Appl. Environ. Microbiol. 78:4380-4385.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 4380-4385
    • Lindqvist, M.H.1    Johansson, N.2    Nilsson, T.3    Rova, M.4
  • 60
    • 84860467728 scopus 로고    scopus 로고
    • Characterization of a novel ArsR-like regulator encoded by Rv2034 in Mycobacterium tuberculosis
    • doi: 10.1371/journal.pone.0036255
    • Gao CH, Yang M, He ZG. 2012. Characterization of a novel ArsR-like regulator encoded by Rv2034 in Mycobacterium tuberculosis. PLoS One 7:e36255. doi: 10.1371/journal.pone.0036255.
    • (2012) PLoS One , vol.7
    • Gao, C.H.1    Yang, M.2    He, Z.G.3
  • 63
    • 62349130698 scopus 로고    scopus 로고
    • Ultrafast and memory-efficient alignment of short DNA sequences to the human genome
    • doi: 10.1186/gb-2009-10-3-r25
    • Langmead B, Trapnell C, Pop M, Salzberg SL. 2009. Ultrafast and memory-efficient alignment of short DNA sequences to the human genome. Genome Biol. 10:R25. doi: 10.1186/gb-2009-10-3-r25.
    • (2009) Genome Biol. , vol.10
    • Langmead, B.1    Trapnell, C.2    Pop, M.3    Salzberg, S.L.4
  • 66
    • 33644857839 scopus 로고    scopus 로고
    • GenomeDiagram: A python package for the visualization of large-scale genomic data
    • Pritchard L, White JA, Birch PR, Toth IK. 2006. GenomeDiagram: a python package for the visualization of large-scale genomic data. Bioinformatics 22:616-617.
    • (2006) Bioinformatics , vol.22 , pp. 616-617
    • Pritchard, L.1    White, J.A.2    Birch, P.R.3    Toth, I.K.4
  • 67
    • 84870431038 scopus 로고    scopus 로고
    • CD-HIT: Accelerated for clustering the next-generation sequencing data
    • Fu L, Niu B, Zhu Z, Wu S, Li W. 2012. CD-HIT: accelerated for clustering the next-generation sequencing data. Bioinformatics 28: 3150-3152.
    • (2012) Bioinformatics , vol.28 , pp. 3150-3152
    • Fu, L.1    Niu, B.2    Zhu, Z.3    Wu, S.4    Li, W.5
  • 68
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • Castresana J. 2000. Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis. Mol. Biol. Evol. 17:540-552.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 540-552
    • Castresana, J.1
  • 69
    • 77949718257 scopus 로고    scopus 로고
    • FastTree 2-approximately maximum-likelihood trees for large alignments
    • doi: 10.1371/journal.pone.0009490
    • Price MN, Dehal PS, Arkin AP. 2010. FastTree 2-approximately maximum-likelihood trees for large alignments. PLoS One 5:e9490. doi: 10.1371/journal.pone.0009490.
    • (2010) PLoS One , vol.5
    • Price, M.N.1    Dehal, P.S.2    Arkin, A.P.3
  • 70
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: Selection of best-fit models of protein evolution
    • Abascal F, Zardoya R, Posada D. 2005. ProtTest: selection of best-fit models of protein evolution. Bioinformatics 21:2104-2105.
    • (2005) Bioinformatics , vol.21 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 71
    • 33750403801 scopus 로고    scopus 로고
    • RAxML-VI-HPC: Maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models
    • Stamatakis A. 2006. RAxML-VI-HPC: maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models. Bioinformatics 22:2688-2690.
    • (2006) Bioinformatics , vol.22 , pp. 2688-2690
    • Stamatakis, A.1
  • 73
    • 0034849408 scopus 로고    scopus 로고
    • MrBayes: Bayesian inference of phylogenetic trees
    • Huelsenbeck JP, Ronquist F. 2001. MrBayes: bayesian inference of phylogenetic trees. Bioinformatics 17:754-755.
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 74
    • 0242696464 scopus 로고    scopus 로고
    • Purification and characterization of the selenate reductase from Thauera selenatis
    • Schröder I, Rech S, Krafft T, Macy JM. 1997. Purification and characterization of the selenate reductase from Thauera selenatis. J. Biol. Chem. 272:23765-23768.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23765-23768
    • Schröder, I.1    Rech, S.2    Krafft, T.3    Macy, J.M.4


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