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Volumn 368, Issue 1616, 2013, Pages

Identification of Dehalobacter reductive dehalogenases that catalyse dechlorination of chloroform, 1,1,1- trichloroethane and 1,1-dichloroethane

Author keywords

Blue native PAGE; Chlorinated ethanes; Chloroform; Dehalobacter; Reductive dehalogenases; Reductive dehalogenation

Indexed keywords

AMINO ACID; BACTERIUM; BIOASSAY; CATALYSIS; CHLOROFORM; DATABASE; DECHLORINATION; ENZYME ACTIVITY; ETHANE; IDENTIFICATION METHOD; MEMBRANE; PEPTIDE; PROTEIN;

EID: 84875082630     PISSN: 09628436     EISSN: 14712970     Source Type: Journal    
DOI: 10.1098/rstb.2012.0318     Document Type: Article
Times cited : (68)

References (40)
  • 1
    • 0001939375 scopus 로고    scopus 로고
    • A history of the production and use of carbon tetrachloride, tetrachloroethylene, trichloroethylene and 1,1,1-trichloroethane in the United States. I. Historical background; carbon tetrachloride and tetrachloroethylene
    • doi:10.1006/enfo.2000.0010
    • Doherty RE. 2000 A history of the production and use of carbon tetrachloride, tetrachloroethylene, trichloroethylene and 1,1,1-trichloroethane in the United States. I. Historical background; carbon tetrachloride and tetrachloroethylene. Environ. Forensics 1, 69-81. (doi:10.1006/enfo.2000.0010)
    • (2000) Environ. Forensics , vol.1 , pp. 69-81
    • Doherty, R.E.1
  • 2
    • 0036077527 scopus 로고    scopus 로고
    • Chloroform: Exposure estimation, hazard characterization, and exposure-response analysis
    • doi:10.1080/10937400290070080
    • Meek ME, Beauchamp R, Long G, Moir D, Turner L, Walker M. 2002 Chloroform: exposure estimation, hazard characterization, and exposure-response analysis. J. Toxicol. Environ. Health B Crit. Rev. 5, 283-334. (doi:10.1080/10937400290070080)
    • (2002) J. Toxicol. Environ. Health B Crit. Rev , vol.5 , pp. 283-334
    • Meek, M.E.1    Beauchamp, R.2    Long, G.3    Moir, D.4    Turner, L.5    Walker, M.6
  • 3
    • 84866006041 scopus 로고    scopus 로고
    • Heterologous expression, purification and cofactor reconstitution of the reductive dehalogenase PceA from Dehalobacter restrictus
    • doi:10.1016/j. pep.2012.08.007
    • Sjuts H, Fisher K, Dunstan MS, Rigby SE, Leys D. 2012 Heterologous expression, purification and cofactor reconstitution of the reductive dehalogenase PceA from Dehalobacter restrictus. Protein Express. Purif. 85, 224-229. (doi:10.1016/j. pep.2012.08.007)
    • (2012) Protein Express. Purif , vol.85 , pp. 224-229
    • Sjuts, H.1    Fisher, K.2    Dunstan, M.S.3    Rigby, S.E.4    Leys, D.5
  • 4
    • 0034656432 scopus 로고    scopus 로고
    • Impact of mixtures of chlorinated aliphatic hydrocarbons on a high-rate, tetraehloroethene-dechlorinating enrichment culture
    • doi:10.1021/es990809f
    • Adamson DT, Parkin GF. 2000 Impact of mixtures of chlorinated aliphatic hydrocarbons on a high-rate, tetraehloroethene-dechlorinating enrichment culture. Environ. Sci. Technol. 34, 1959-1965. (doi:10.1021/es990809f)
    • (2000) Environ. Sci. Technol , vol.34 , pp. 1959-1965
    • Adamson, D.T.1    Parkin, G.F.2
  • 5
    • 0032985003 scopus 로고    scopus 로고
    • Complete transformation of 1,1,1- trichloroethane to chloroethane by a methanogenic mixed population
    • doi:10.1007/s002530051393
    • de Best JH, Hage A, Doddema HJ, Janssen DB, Harder W. 1999 Complete transformation of 1,1,1- trichloroethane to chloroethane by a methanogenic mixed population. Appl. Microbiol. Biotechnol. 51, 277-283. (doi:10.1007/s002530051393)
    • (1999) Appl. Microbiol. Biotechnol , vol.51 , pp. 277-283
    • de Best, J.H.1    Hage, A.2    Doddema, H.J.3    Janssen, D.B.4    Harder, W.5
  • 6
    • 0026027483 scopus 로고
    • Anaerobic treatment of a high-strength industrial waste bearing inhibitory concentrations of 1,1,1-trichloroethane
    • Suidan MT, Wuellner AM, Boyer TK. 1991 Anaerobic treatment of a high-strength industrial waste bearing inhibitory concentrations of 1,1,1-trichloroethane. Water Sci. Technol. 23, 1385-1393.
    • (1991) Water Sci. Technol , vol.23 , pp. 1385-1393
    • Suidan, M.T.1    Wuellner, A.M.2    Boyer, T.K.3
  • 8
    • 0009774298 scopus 로고
    • Metallic iron-enhanced biotransformation of carbon tetrachloride and chloroform under methanogenic conditions
    • Weathers LJ, Parkin GF. 1995 Metallic iron-enhanced biotransformation of carbon tetrachloride and chloroform under methanogenic conditions. Bioremediation Chlorinated Solvents 3, 117-122.
    • (1995) Bioremediation Chlorinated Solvents , vol.3 , pp. 117-122
    • Weathers, L.J.1    Parkin, G.F.2
  • 9
    • 0033637443 scopus 로고    scopus 로고
    • Inhibition of methanogenesis by C-1- and C-2-polychlorinated aliphatic hydrocarbons
    • Yu ZT, Smith GB. 2000 Inhibition of methanogenesis by C-1- and C-2-polychlorinated aliphatic hydrocarbons. Environ. Toxicol. Chem. 19, 2212-2217.
    • (2000) Environ. Toxicol. Chem , vol.19 , pp. 2212-2217
    • Yu, Z.T.1    Smith, G.B.2
  • 10
    • 0033622685 scopus 로고    scopus 로고
    • Acclimation of anaerobic systems to biodegrade tetrachloroethene in the presence of carbon tetrachloride and chloroform
    • doi:10.1016/S0043-1354(99)00121-9
    • Bagley DM, Lalonde M, Kaseros V, Stasiuk KE, Sleep BE. 2000 Acclimation of anaerobic systems to biodegrade tetrachloroethene in the presence of carbon tetrachloride and chloroform. Water Res. 34, 171-178. (doi:10.1016/S0043-1354(99)00121-9)
    • (2000) Water Res , vol.34 , pp. 171-178
    • Bagley, D.M.1    Lalonde, M.2    Kaseros, V.3    Stasiuk, K.E.4    Sleep, B.E.5
  • 11
    • 0036771968 scopus 로고    scopus 로고
    • Comparison of anaerobic dechlorinating enrichment cultures maintained on tetrachloroethene, trichloroethene, cis-dichloroethene and vinyl chloride
    • doi:10.1016/S0043-1354(02)00151-3
    • Duhamel M, Wehr SD, Yu L, Rizvi H, Seepersad D, Dworatzek S, Cox EE, Edwards EA. 2002 Comparison of anaerobic dechlorinating enrichment cultures maintained on tetrachloroethene, trichloroethene, cis-dichloroethene and vinyl chloride. Water Res. 36, 4193-4202. (doi:10.1016/S0043-1354(02)00151-3)
    • (2002) Water Res , vol.36 , pp. 4193-4202
    • Duhamel, M.1    Wehr, S.D.2    Yu, L.3    Rizvi, H.4    Seepersad, D.5    Dworatzek, S.6    Cox, E.E.7    Edwards, E.A.8
  • 12
    • 41349099621 scopus 로고    scopus 로고
    • Biochemical and genetic bases of dehalorespiration
    • doi:10.1002/Tcr.20134
    • Futagami T, Goto M, Furukawa K. 2008 Biochemical and genetic bases of dehalorespiration. Chem. Record 8, 1-12. (doi:10.1002/Tcr.20134)
    • (2008) Chem. Record , vol.8 , pp. 1-12
    • Futagami, T.1    Goto, M.2    Furukawa, K.3
  • 13
    • 33845528331 scopus 로고    scopus 로고
    • A 1,1,1- trichloroethane-degrading anaerobic mixed microbial culture enhances biotransformation of mixtures of chlorinated ethenes and ethanes
    • doi:10.1128/ Aem.01269-06
    • Grostern A, Edwards EA. 2006 A 1,1,1- trichloroethane-degrading anaerobic mixed microbial culture enhances biotransformation of mixtures of chlorinated ethenes and ethanes. Appl. Environ. Microbiol. 72, 7849-7856. (doi:10.1128/ Aem.01269-06)
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 7849-7856
    • Grostern, A.1    Edwards, E.A.2
  • 14
    • 77954643531 scopus 로고    scopus 로고
    • Chloroform respiration to dichloromethane by a Dehalobacter population
    • doi:10.1111/J.1462-2920.2009. 02150.X
    • Grostern A, Duhamel M, Dworatzek S, Edwards EA. 2010 Chloroform respiration to dichloromethane by a Dehalobacter population. Environ. Microbiol. 12, 1053-1060. (doi:10.1111/J.1462-2920.2009. 02150.X)
    • (2010) Environ. Microbiol , vol.12 , pp. 1053-1060
    • Grostern, A.1    Duhamel, M.2    Dworatzek, S.3    Edwards, E.A.4
  • 15
    • 0031970012 scopus 로고    scopus 로고
    • Dehalobacter restrictus gen. nov. and sp. nov., a strictly anaerobic bacterium that reductively dechlorinates tetra- and trichloroethene in an anaerobic respiration
    • doi:10.1007/s002030050577
    • Holliger C, Hahn D, Harmsen H, Ludwig W, Schumacher W, Tindall B, Vazquez F, Weiss N, Zehnder AJ. 1998 Dehalobacter restrictus gen. nov. and sp. nov., a strictly anaerobic bacterium that reductively dechlorinates tetra- and trichloroethene in an anaerobic respiration. Arch. Microbiol. 169, 313-321. (doi:10.1007/s002030050577)
    • (1998) Arch. Microbiol , vol.169 , pp. 313-321
    • Holliger, C.1    Hahn, D.2    Harmsen, H.3    Ludwig, W.4    Schumacher, W.5    Tindall, B.6    Vazquez, F.7    Weiss, N.8    Zehnder, A.J.9
  • 16
    • 65549166732 scopus 로고    scopus 로고
    • Characterization of a Dehalobacter coculture that dechlorinates 1,2- dichloroethane to ethene and identification of the putative reductive dehalogenase gene
    • doi:10.1128/ AEM.02037-08
    • Grostern A, Edwards EA. 2009 Characterization of a Dehalobacter coculture that dechlorinates 1,2- dichloroethane to ethene and identification of the putative reductive dehalogenase gene. Appl. Environ. Microbiol. 75, 2684-2693. (doi:10.1128/ AEM.02037-08)
    • (2009) Appl. Environ. Microbiol , vol.75 , pp. 2684-2693
    • Grostern, A.1    Edwards, E.A.2
  • 17
    • 0036828771 scopus 로고    scopus 로고
    • Microbial dehalorespiration with 1,1,1-trichloroethane
    • doi:10.1126/science.1074675
    • Sun B, Griffin BM, Ayala-del-Río HL, Hashsham SA, Tiedje JM. 2002 Microbial dehalorespiration with 1,1,1-trichloroethane. Science 298, 1023-1025. (doi:10.1126/science.1074675)
    • (2002) Science , vol.298 , pp. 1023-1025
    • Sun, B.1    Griffin, B.M.2    Ayala-del-Río, H.L.3    Hashsham, S.A.4    Tiedje, J.M.5
  • 18
    • 84859432408 scopus 로고    scopus 로고
    • Complete chloroform dechlorination by organochlorine respiration and fermentation
    • doi:10.1111/j.1462-2920.2011.02656.x
    • Lee M, Low A, Zemb O, Koenig J, Michaelsen A, Manefield M. 2012 Complete chloroform dechlorination by organochlorine respiration and fermentation. Environ. Microbiol. 14, 883-894. (doi:10.1111/j.1462-2920.2011.02656.x)
    • (2012) Environ. Microbiol , vol.14 , pp. 883-894
    • Lee, M.1    Low, A.2    Zemb, O.3    Koenig, J.4    Michaelsen, A.5    Manefield, M.6
  • 19
    • 80051716658 scopus 로고    scopus 로고
    • A role for Dehalobacter spp. in the reductive dehalogenation of dichlorobenzenes and monochlorobenzene
    • doi:10.1021/es200480k
    • Nelson JL, Fung JM, Cadillo-Quiroz H, Cheng X, Zinder SH. 2011 A role for Dehalobacter spp. in the reductive dehalogenation of dichlorobenzenes and monochlorobenzene. Environ. Sci. Technol. 45, 6806-6813. (doi:10.1021/es200480k)
    • (2011) Environ. Sci. Technol , vol.45 , pp. 6806-6813
    • Nelson, J.L.1    Fung, J.M.2    Cadillo-Quiroz, H.3    Cheng, X.4    Zinder, S.H.5
  • 20
    • 23744455645 scopus 로고    scopus 로고
    • Reductive dechlorination of beta-hexachlorocyclohexane (b-HCH) by a Dehalobacter species in coculture with a Sedimentibacter sp
    • doi:10.1016/j.femsec.2005.03.003
    • van Doesburg W, van Eekert MH, Middeldorp PJ, Balk M, Schraa G, Stams AJ. 2005 Reductive dechlorination of beta-hexachlorocyclohexane (b-HCH) by a Dehalobacter species in coculture with a Sedimentibacter sp. FEMS Microbiol. Ecol. 54, 87-95. (doi:10.1016/j.femsec.2005.03.003)
    • (2005) FEMS Microbiol. Ecol , vol.54 , pp. 87-95
    • van Doesburg, W.1    van Eekert, M.H.2    Middeldorp, P.J.3    Balk, M.4    Schraa, G.5    Stams, A.J.6
  • 21
    • 64749101213 scopus 로고    scopus 로고
    • A novel Dehalobacter species is involved in extensive 4,5,6,7-tetrachlorophthalide dechlorination
    • doi:10.1128/ AEM.02112-08
    • Yoshida N, Ye L, Baba D, Katayama A. 2009 A novel Dehalobacter species is involved in extensive 4,5,6,7-tetrachlorophthalide dechlorination. Appl. Environ. Microbiol. 75, 2400-2405. (doi:10.1128/ AEM.02112-08)
    • (2009) Appl. Environ. Microbiol , vol.75 , pp. 2400-2405
    • Yoshida, N.1    Ye, L.2    Baba, D.3    Katayama, A.4
  • 22
    • 84857098286 scopus 로고    scopus 로고
    • Dichloromethane fermentation by a Dehalobacter sp. in an enrichment culture derived from pristine river sediment
    • doi:10.1128/AEM. 07325-11
    • Justicia-Leon SD, Ritalahti KM, Mack EE, Löffler FE. 2012 Dichloromethane fermentation by a Dehalobacter sp. in an enrichment culture derived from pristine river sediment. Appl. Environ. Microbiol. 78, 1288-1291. (doi:10.1128/AEM. 07325-11)
    • (2012) Appl. Environ. Microbiol , vol.78 , pp. 1288-1291
    • Justicia-Leon, S.D.1    Ritalahti, K.M.2    Mack, E.E.3    Löffler, F.E.4
  • 23
    • 9244251590 scopus 로고    scopus 로고
    • Anaerobic microbial dehalogenation
    • doi:10.1146/annurev.micro.58.030603.123600
    • Smidt H, de Vos WM. 2004 Anaerobic microbial dehalogenation. Annu. Rev. Microbiol. 58, 43-73. (doi:10.1146/annurev.micro.58.030603.123600)
    • (2004) Annu. Rev. Microbiol , vol.58 , pp. 43-73
    • Smidt, H.1    de Vos, W.M.2
  • 24
    • 73649122427 scopus 로고    scopus 로고
    • Localized plasticity in the streamlined genomes of vinyl chloride respiring Dehalococcoides
    • doi:10. 1371/journal.pgen.1000714
    • McMurdie PJ et al. 2009 Localized plasticity in the streamlined genomes of vinyl chloride respiring Dehalococcoides. PLoS Genet. 5, e1000714. (doi:10. 1371/journal.pgen.1000714)
    • (2009) PLoS Genet , vol.5
    • McMurdie, P.J.1
  • 25
    • 27144500225 scopus 로고    scopus 로고
    • Genome sequence of the chlorinated compound-respiring bacterium Dehalococcoides species strain CBDB1
    • doi:10.1038/nbt1131
    • Kube M, Beck A, Zinder SH, Kuhl H, Reinhardt R, Adrian L. 2005 Genome sequence of the chlorinated compound-respiring bacterium Dehalococcoides species strain CBDB1. Nat. Biotechnol. 23, 1269-1273. (doi:10.1038/nbt1131)
    • (2005) Nat. Biotechnol , vol.23 , pp. 1269-1273
    • Kube, M.1    Beck, A.2    Zinder, S.H.3    Kuhl, H.4    Reinhardt, R.5    Adrian, L.6
  • 26
    • 84873841850 scopus 로고    scopus 로고
    • Functional characterization of Dehalococcoides reductive dehalogenases using blue native polyacrylamide gel electrophoresis
    • doi:10.1128/AEM.01873-12
    • Tang S, Chan WW, Fletcher KE, Liang X, Seifert J, Löffler FE, Edwards EA, Adrian L. 2013 Functional characterization of Dehalococcoides reductive dehalogenases using blue native polyacrylamide gel electrophoresis. Appl. Environ. Microbiol. 79, 974-981. (doi:10.1128/AEM.01873-12)
    • (2013) Appl. Environ. Microbiol , vol.79 , pp. 974-981
    • Tang, S.1    Chan, W.W.2    Fletcher, K.E.3    Liang, X.4    Seifert, J.5    Löffler, F.E.6    Edwards, E.A.7    Adrian, L.8
  • 27
    • 38449091968 scopus 로고    scopus 로고
    • Identification of a chlorobenzene reductive dehalogenase in Dehalococcoides sp. strain CBDB1
    • doi:10. 1128/AEM.01649-07
    • Adrian L, Rahnenfuhrer J, Gobom J, Hölscher T. 2007 Identification of a chlorobenzene reductive dehalogenase in Dehalococcoides sp. strain CBDB1. Appl. Environ. Microbiol. 73, 7717-7724. (doi:10. 1128/AEM.01649-07)
    • (2007) Appl. Environ. Microbiol , vol.73 , pp. 7717-7724
    • Adrian, L.1    Rahnenfuhrer, J.2    Gobom, J.3    Hölscher, T.4
  • 28
    • 79951663055 scopus 로고    scopus 로고
    • V. 5.4.2 Auckland, New Zealand: Biomatters Ltd
    • Drummond AJ et al. 2011 Geneious v. 5.4.2. Auckland, New Zealand: Biomatters Ltd.
    • (2011) Geneious
    • Drummond, A.J.1
  • 29
    • 84871353227 scopus 로고    scopus 로고
    • Semi-automatic in silico gap closure enabled de novo assembly of two Dehalobacter genomes from metagenomic data
    • doi:10.1371/journal. pone.0052038
    • Tang S, Gong Y, Edwards EA. 2012 Semi-automatic in silico gap closure enabled de novo assembly of two Dehalobacter genomes from metagenomic data. PLoS ONE 7, e52038. (doi:10.1371/journal. pone.0052038)
    • (2012) PLoS ONE , vol.7
    • Tang, S.1    Gong, Y.2    Edwards, E.A.3
  • 30
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • doi:10.1093/ nar/gkh340
    • Edgar RC. 2004 MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797. (doi:10.1093/ nar/gkh340)
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 31
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon S, Gascuel O. 2003 A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst. Biol. 52, 696-704.
    • (2003) Syst. Biol , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 32
    • 0034740227 scopus 로고    scopus 로고
    • Application of a time-delay neural network to promoter annotation in the Drosophila melanogaster genome
    • doi:10.1016/S0097-8485(01)00099-7
    • Reese MG. 2001 Application of a time-delay neural network to promoter annotation in the Drosophila melanogaster genome. Comput. Chem. 26, 51-56. (doi:10.1016/S0097-8485(01)00099-7)
    • (2001) Comput. Chem , vol.26 , pp. 51-56
    • Reese, M.G.1
  • 33
    • 0025831356 scopus 로고
    • SIGNAL SCAN: A computer program that scans DNA sequences for eukaryotic transcriptional elements
    • Prestridge DS. 1991 SIGNAL SCAN: a computer program that scans DNA sequences for eukaryotic transcriptional elements. Comput. Appl. Biosci. 7, 203-206.
    • (1991) Comput. Appl. Biosci , vol.7 , pp. 203-206
    • Prestridge, D.S.1
  • 35
    • 84875080705 scopus 로고    scopus 로고
    • Overview of organohalide-respiring bacteria and a proposal for a classification system for reductive dehalogenases
    • doi:10.1098/ rstb.2012.0322
    • Hug LA, Maphosa F, Leys D, Löffler FE, Smidt H, Edwards EA, Adrian L. 2013 Overview of organohalide-respiring bacteria and a proposal for a classification system for reductive dehalogenases. Phil. Trans. R. Soc. B 368, 20120322. (doi:10.1098/ rstb.2012.0322)
    • (2013) Phil. Trans. R. Soc. B , vol.368 , pp. 20120322
    • Hug, L.A.1    Maphosa, F.2    Leys, D.3    Löffler, F.E.4    Smidt, H.5    Edwards, E.A.6    Adrian, L.7
  • 36
    • 0042530278 scopus 로고    scopus 로고
    • Characterization of the corrinoid iron-sulfur protein tetrachloroethene reductive dehalogenase of Dehalobacter restrictus
    • doi:10. 1128/AEM.69.8.4628-4638.2003
    • Maillard J, Schumacher W, Vazquez F, Regeard C, Hagen WR, Holliger C. 2003 Characterization of the corrinoid iron-sulfur protein tetrachloroethene reductive dehalogenase of Dehalobacter restrictus. Appl. Environ. Microbiol. 69, 4628-4638. (doi:10. 1128/AEM.69.8.4628-4638.2003)
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 4628-4638
    • Maillard, J.1    Schumacher, W.2    Vazquez, F.3    Regeard, C.4    Hagen, W.R.5    Holliger, C.6
  • 37
    • 0031859044 scopus 로고    scopus 로고
    • Tetrachloroethene dehalogenase from Dehalospirillum multivorans: Cloning, sequencing of the encoding genes, and expression of the pceA gene in Escherichia coli
    • Neumann A, Wohlfarth G, Diekert G. 1998 Tetrachloroethene dehalogenase from Dehalospirillum multivorans: cloning, sequencing of the encoding genes, and expression of the pceA gene in Escherichia coli. J. Bacteriol. 180, 4140-4145.
    • (1998) J. Bacteriol , vol.180 , pp. 4140-4145
    • Neumann, A.1    Wohlfarth, G.2    Diekert, G.3
  • 38
    • 33746767681 scopus 로고    scopus 로고
    • Transcription and mass- spectroscopic proteomic studies of electron transport oxidoreductases in Dehalococcoides ethenogenes
    • doi:10.1111/j. 1462-2920.2006.01090.x
    • Morris RM, Sowell S, Barofsky D, Zinder S, Richardson R. 2006 Transcription and mass- spectroscopic proteomic studies of electron transport oxidoreductases in Dehalococcoides ethenogenes. Environ. Microbiol. 8, 1499-1509. (doi:10.1111/j. 1462-2920.2006.01090.x)
    • (2006) Environ. Microbiol , vol.8 , pp. 1499-1509
    • Morris, R.M.1    Sowell, S.2    Barofsky, D.3    Zinder, S.4    Richardson, R.5
  • 39
    • 33846123326 scopus 로고    scopus 로고
    • Comparative proteomics of Dehalococcoides spp. reveals strain- specific peptides associated with activity
    • doi:10.1128/AEM. 02129-06
    • Morris RM, Fung JM, Rahm BG, Zhang S, Freedman DL, Zinder SH, Richardson RE. 2007 Comparative proteomics of Dehalococcoides spp. reveals strain- specific peptides associated with activity. Appl. Environ. Microbiol. 73, 320-326. (doi:10.1128/AEM. 02129-06)
    • (2007) Appl. Environ. Microbiol , vol.73 , pp. 320-326
    • Morris, R.M.1    Fung, J.M.2    Rahm, B.G.3    Zhang, S.4    Freedman, D.L.5    Zinder, S.H.6    Richardson, R.E.7
  • 40
    • 79955417151 scopus 로고    scopus 로고
    • Addressing trypsin bias in large scale (phospho)proteome analysis by size exclusion chromatography and secondary digestion of large post-trypsin peptides
    • doi:10.1021/pr100951t
    • Tran BQ, Hernandez C, Waridel P, Potts A, Barblan J, Lisacek F, Quadroni M. 2011 Addressing trypsin bias in large scale (phospho)proteome analysis by size exclusion chromatography and secondary digestion of large post-trypsin peptides. J. Proteome Res. 10, 800-811. (doi:10.1021/pr100951t)
    • (2011) J. Proteome Res , vol.10 , pp. 800-811
    • Tran, B.Q.1    Hernandez, C.2    Waridel, P.3    Potts, A.4    Barblan, J.5    Lisacek, F.6    Quadroni, M.7


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