메뉴 건너뛰기




Volumn 16, Issue 12, 2012, Pages 668-680

Analysis of in vivo function of predicted isoenzymes-a metabolomic approach

Author keywords

[No Author keywords available]

Indexed keywords

ISOENZYME; OXIDOREDUCTASE; SHIKIMIC ACID;

EID: 84870882122     PISSN: 15362310     EISSN: 15578100     Source Type: Journal    
DOI: 10.1089/omi.2012.0055     Document Type: Article
Times cited : (4)

References (53)
  • 1
    • 0024286625 scopus 로고
    • Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase
    • Anton IA, and Coggins Jr. (1988). Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. Biochem J 249, 319-326.
    • (1988) Biochem J , vol.249 , pp. 319-326
    • Anton, I.A.1    Coggins, Jr.2
  • 2
    • 33847207787 scopus 로고    scopus 로고
    • Altered metabolic flux due to deletion of odhA causes L-glutamate overproduction in Corynebacterium glutamicum
    • Asakura Y, Kimura E, Usuda Y, et al. (2007). Altered metabolic flux due to deletion of odhA causes L-glutamate overproduction in Corynebacterium glutamicum. Appl Environ Microbiol 73, 1308-1319.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 1308-1319
    • Asakura, Y.1    Kimura, E.2    Usuda, Y.3
  • 3
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection
    • Baba T, Ara T, Hasegawa M, et al. (2006). Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection. Mol Systems Biol 2, 0008.
    • (2006) Mol Systems Biol , vol.2 , pp. 0008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3
  • 5
    • 33645030241 scopus 로고    scopus 로고
    • Robust Salmonella metabolism limits possibilities for new antimicrobials
    • Becker D, Selbach M, Rollenhagen C, et al. (2006). Robust Salmonella metabolism limits possibilities for new antimicrobials. Nature 440, 303-307.
    • (2006) Nature , vol.440 , pp. 303-307
    • Becker, D.1    Selbach, M.2    Rollenhagen, C.3
  • 6
    • 17844405878 scopus 로고    scopus 로고
    • Genome-scale reconstruction of the metabolic network in Staphylococcus aureus N315: An initial draft to the two-dimensional annotation
    • Becker SA, and Palsson BO. (2005). Genome-scale reconstruction of the metabolic network in Staphylococcus aureus N315: An initial draft to the two-dimensional annotation. BMC Microbiol 5, 8.
    • (2005) BMC Microbiol , vol.5 , pp. 8
    • Becker, S.A.1    Palsson, B.O.2
  • 7
    • 0038820015 scopus 로고    scopus 로고
    • The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase
    • Benach J, Lee I, Edstrom W, et al. (2003). The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase. J Biol Chem 278, 19176-19182.
    • (2003) J Biol Chem , vol.278 , pp. 19176-19182
    • Benach, J.1    Lee, I.2    Edstrom, W.3
  • 8
    • 34347239963 scopus 로고    scopus 로고
    • A highthroughput method for microbial metabolome analysis using gas chromatography/mass spectrometry
    • Borner J, Buchinger S, and Schomburg D. (2007). A highthroughput method for microbial metabolome analysis using gas chromatography/mass spectrometry. Anal Biochem 367, 143-151.
    • (2007) Anal Biochem , vol.367 , pp. 143-151
    • Borner, J.1    Buchinger, S.2    Schomburg, D.3
  • 9
    • 33644832381 scopus 로고    scopus 로고
    • In silico aided metabolic engineering of Saccharomyces cerevisiae for improved bioethanol production
    • Bro C, Regenberg B, Forster J, and Nielsen J. (2006). In silico aided metabolic engineering of Saccharomyces cerevisiae for improved bioethanol production. Metab Engin 8, 102-111.
    • (2006) Metab Engin , vol.8 , pp. 102-111
    • Bro, C.1    Regenberg, B.2    Forster, J.3    Nielsen, J.4
  • 10
    • 33644877904 scopus 로고    scopus 로고
    • MetaCyc: A multiorganism database of metabolic pathways and enzymes
    • Caspi R, Foerster H, Fulcher CA, et al. (2006). MetaCyc: A multiorganism database of metabolic pathways and enzymes. Nucleic Acids Res 34, D511-516.
    • (2006) Nucleic Acids Res , vol.34
    • Caspi, R.1    Foerster, H.2    Fulcher, C.A.3
  • 11
    • 11844292771 scopus 로고    scopus 로고
    • High level expression and single-step purification of hexahistidine-tagged L-2-hydroxyisocaproate dehydrogenase making use of a versatile expression vector set
    • Chatterjee S, Schoepe J, Lohmer S, and Schomburg D. (2005). High level expression and single-step purification of hexahistidine-tagged L-2-hydroxyisocaproate dehydrogenase making use of a versatile expression vector set. Protein Express Purif 39, 137-143.
    • (2005) Protein Express Purif , vol.39 , pp. 137-143
    • Chatterjee, S.1    Schoepe, J.2    Lohmer, S.3    Schomburg, D.4
  • 12
    • 0022425494 scopus 로고
    • The purification of shikimate dehydrogenase from Escherichia coli
    • Chaudhuri S, and Coggins Jr. (1985). The purification of shikimate dehydrogenase from Escherichia coli. Biochem J 226, 217-223.
    • (1985) Biochem J , vol.226 , pp. 217-223
    • Chaudhuri, S.1    Coggins, Jr.2
  • 13
    • 0036237128 scopus 로고    scopus 로고
    • Identification of two prpDBC gene clusters in Corynebacterium glutamicum and their involvement in propionate degradation via the 2- methylcitrate cycle
    • Claes WA, Puhler A, and Kalinowski J. (2002). Identification of two prpDBC gene clusters in Corynebacterium glutamicum and their involvement in propionate degradation via the 2- methylcitrate cycle. J Bacteriol 184, 2728-2739.
    • (2002) J Bacteriol , vol.184 , pp. 2728-2739
    • Claes, W.A.1    Puhler, A.2    Kalinowski, J.3
  • 14
    • 0038128182 scopus 로고    scopus 로고
    • Experiences with the shikimate-pathway enzymes as targets for rational drug design
    • Coggins JR, Abell C, Evans LB, et al. (2003). Experiences with the shikimate-pathway enzymes as targets for rational drug design. Biochem Soc Trans 31, 548-552.
    • (2003) Biochem Soc Trans , vol.31 , pp. 548-552
    • Coggins, J.R.1    Abell, C.2    Evans, L.B.3
  • 15
    • 42949142245 scopus 로고    scopus 로고
    • A complete collection of single-gene deletion mutants of Acinetobacter baylyi ADP1
    • De Berardinis V, Vallenet D, Castelli V, et al. (2008). A complete collection of single-gene deletion mutants of Acinetobacter baylyi ADP1. Mol Systems Biol 4, 174.
    • (2008) Mol Systems Biol , vol.4 , pp. 174
    • De Berardinis, V.1    Vallenet, D.2    Castelli, V.3
  • 16
    • 0035232521 scopus 로고    scopus 로고
    • Metabolic engineering for L-lysine production by Corynebacterium glutamicum
    • De Graaf AA, Eggeling L, and Sahm H. (2001). Metabolic engineering for L-lysine production by Corynebacterium glutamicum. Adv Biochem Engin/Biotechnol 73, 9-29.
    • (2001) Adv Biochem Engin/Biotechnol , vol.73 , pp. 9-29
    • De Graaf, A.A.1    Eggeling, L.2    Sahm, H.3
  • 17
    • 33846910173 scopus 로고    scopus 로고
    • Global reconstruction of the human metabolic network based on genomic and bibliomic data
    • Duarte NC, Becker SA, Jamshidi N, et al. (2007). Global reconstruction of the human metabolic network based on genomic and bibliomic data. Proc Natl Acad Sci USA 104, 1777-1782.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1777-1782
    • Duarte, N.C.1    Becker, S.A.2    Jamshidi, N.3
  • 18
    • 57549102595 scopus 로고    scopus 로고
    • Genomescale models of bacterial metabolism: Reconstruction and applications
    • Durot M, Bourguignon PY, and Schachter V. (2009). Genomescale models of bacterial metabolism: Reconstruction and applications. FEMS Microbiol Rev 33, 164-190.
    • (2009) FEMS Microbiol Rev , vol.33 , pp. 164-190
    • Durot, M.1    Bourguignon, P.Y.2    Schachter, V.3
  • 19
    • 0024708665 scopus 로고
    • The phosphoenolpyruvate carboxylase gene of Corynebacterium glutamicum: Molecular cloning, nucleotide sequence, and expression
    • Eikmanns BJ, Follettie MT, Griot MU, and Sinskey AJ. (1989). The phosphoenolpyruvate carboxylase gene of Corynebacterium glutamicum: Molecular cloning, nucleotide sequence, and expression. Mol Gen Genet 218, 330-339.
    • (1989) Mol Gen Genet , vol.218 , pp. 330-339
    • Eikmanns, B.J.1    Follettie, M.T.2    Griot, M.U.3    Sinskey, A.J.4
  • 20
    • 0033155976 scopus 로고    scopus 로고
    • Metabolic analysis of glutamate production by Corynebacterium glutamicum
    • Gourdon P, and Lindley ND. (1999). Metabolic analysis of glutamate production by Corynebacterium glutamicum. Metab Engin 1, 224-231.
    • (1999) Metab Engin , vol.1 , pp. 224-231
    • Gourdon, P.1    Lindley, N.D.2
  • 22
    • 0042162924 scopus 로고    scopus 로고
    • The Corynebacterium glutamicum genome: Features and impacts on biotechnological processes
    • Ikeda M, and Nakagawa S. (2003). The Corynebacterium glutamicum genome: Features and impacts on biotechnological processes. App Microbiol Biotechnol 62, 99-109.
    • (2003) App Microbiol Biotechnol , vol.62 , pp. 99-109
    • Ikeda, M.1    Nakagawa, S.2
  • 23
    • 33645241830 scopus 로고    scopus 로고
    • VANTED: A system for advanced data analysis and visualization in the context of biological networks
    • Junker BH, Klukas C, and Schreiber F. (2006). VANTED: A system for advanced data analysis and visualization in the context of biological networks. BMC Bioinform 7, 109.
    • (2006) BMC Bioinform , vol.7 , pp. 109
    • Junker, B.H.1    Klukas, C.2    Schreiber, F.3
  • 24
    • 12444259324 scopus 로고    scopus 로고
    • The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins
    • Kalinowski J, Bathe B, Bartels D, et al. (2003). The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins. J Biotechnol 104, 5-25.
    • (2003) J Biotechnol , vol.104 , pp. 5-25
    • Kalinowski, J.1    Bathe, B.2    Bartels, D.3
  • 26
    • 0037267850 scopus 로고    scopus 로고
    • Metabolic engineering of glutamate production
    • Kimura E. (2003). Metabolic engineering of glutamate production. Adv Biochem Engin/Biotechnol 79, 37-57.
    • (2003) Adv Biochem Engin/Biotechnol , vol.79 , pp. 37-57
    • Kimura, E.1
  • 27
    • 1042269472 scopus 로고    scopus 로고
    • Minimal cut sets in biochemical reaction networks
    • Klamt S, and Gilles ED. (2004). Minimal cut sets in biochemical reaction networks. Bioinformatics (Oxford, England). 20, 226-234.
    • (2004) Bioinformatics (Oxford, England) , vol.20 , pp. 226-234
    • Klamt, S.1    Gilles, E.D.2
  • 28
    • 0346494819 scopus 로고    scopus 로고
    • MetaCyc: A multiorganism database of metabolic pathways and enzymes
    • Krieger CJ, Zhang P, Mueller LA, et al., (2004). MetaCyc: A multiorganism database of metabolic pathways and enzymes. Nucleic Acids Res 32, D438-442.
    • (2004) Nucleic Acids Res , vol.32
    • Krieger, C.J.1    Zhang, P.2    Mueller, L.A.3
  • 29
    • 0036424063 scopus 로고    scopus 로고
    • Cloning and expression of functional shikimate dehydrogenase (EC 1.1.1.25) from Mycobacterium tuberculosis H37Rv
    • Magalhaes ML, Pereira CP, Basso LA, and Santos DS. (2002). Cloning and expression of functional shikimate dehydrogenase (EC 1.1.1.25) from Mycobacterium tuberculosis H37Rv. Protein Express Purif 26, 59-64.
    • (2002) Protein Express Purif , vol.26 , pp. 59-64
    • Magalhaes, M.L.1    Pereira, C.P.2    Basso, L.A.3    Santos, D.S.4
  • 30
    • 0038265866 scopus 로고    scopus 로고
    • Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities
    • Michel G, Roszak AW, Sauve V, et al. (2003). Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities. J Biol Chem 278, 19463-19472.
    • (2003) J Biol Chem , vol.278 , pp. 19463-19472
    • Michel, G.1    Roszak, A.W.2    Sauve, V.3
  • 31
    • 33646163446 scopus 로고    scopus 로고
    • Comparisons of potentials for Llysine production among different Corynebacterium glutamicum strains
    • Ohnishi J, and Ikeda M. (2006). Comparisons of potentials for Llysine production among different Corynebacterium glutamicum strains. Bio Biotechnol Biochem 70, 1017-1020.
    • (2006) Bio Biotechnol Biochem , vol.70 , pp. 1017-1020
    • Ohnishi, J.1    Ikeda, M.2
  • 32
    • 0035079744 scopus 로고    scopus 로고
    • Pyruvate carboxylase is a major bottleneck for glutamate and lysine production by Corynebacterium glutamicum
    • Peters-Wendisch PG, Schiel B, Wendisch VF, et al. (2001). Pyruvate carboxylase is a major bottleneck for glutamate and lysine production by Corynebacterium glutamicum. J Mol Microbiol Biotechnol 3, 295-300.
    • (2001) J Mol Microbiol Biotechnol , vol.3 , pp. 295-300
    • Peters-Wendisch, P.G.1    Schiel, B.2    Wendisch, V.F.3
  • 33
    • 14844349363 scopus 로고    scopus 로고
    • MetaSHARK: Software for automated metabolic network prediction from DNA sequence and its application to the genomes of Plasmodium falciparum and Eimeria tenella
    • Pinney JW, Shirley MW, McConkey GA, and Westhead DR. (2005). metaSHARK: Software for automated metabolic network prediction from DNA sequence and its application to the genomes of Plasmodium falciparum and Eimeria tenella. Nucleic Acids Res 33, 1399-1409.
    • (2005) Nucleic Acids Res , vol.33 , pp. 1399-1409
    • Pinney, J.W.1    Shirley, M.W.2    McConkey, G.A.3    Westhead, D.R.4
  • 34
    • 0037385718 scopus 로고    scopus 로고
    • Genome-scale microbial in silico models: The constraintsbased approach
    • Price ND, Papin JA, Schilling CH, and Palsson BO. (2003). Genome-scale microbial in silico models: The constraintsbased approach. Trends Biotechnol 21, 162-169.
    • (2003) Trends Biotechnol , vol.21 , pp. 162-169
    • Price, N.D.1    Papin, J.A.2    Schilling, C.H.3    Palsson, B.O.4
  • 35
    • 80053174834 scopus 로고    scopus 로고
    • EnzymeDetector: An integrated enzyme function prediction tool and database
    • Quester S, and Schomburg D. (2011). EnzymeDetector: An integrated enzyme function prediction tool and database. BMC Bioinformat 12, 376.
    • (2011) BMC Bioinformat , vol.12 , pp. 376
    • Quester, S.1    Schomburg, D.2
  • 36
    • 33747890136 scopus 로고    scopus 로고
    • Observing local and global properties of metabolic pathways: 'Load points' and 'choke points' in the metabolic networks
    • Rahman SA, and Schomburg D. (2006). Observing local and global properties of metabolic pathways: 'Load points' and 'choke points' in the metabolic networks. Bioinformatics (Oxford, England) 22, 1767-1774.
    • (2006) Bioinformatics (Oxford, England) , vol.22 , pp. 1767-1774
    • Rahman, S.A.1    Schomburg, D.2
  • 37
    • 0034218717 scopus 로고    scopus 로고
    • Technical advance: Simultaneous analysis of metabolites in potato tuber by gas chromatography-mass spectrometry
    • Roessner U, Wagner C, Kopka J, Trethewey RN, and Willmitzer L. (2000). Technical advance: Simultaneous analysis of metabolites in potato tuber by gas chromatography-mass spectrometry. Plant J 23, 131-142.
    • (2000) Plant J , vol.23 , pp. 131-142
    • Roessner, U.1    Wagner, C.2    Kopka, J.3    Trethewey, R.N.4    Willmitzer, L.5
  • 38
    • 0025239615 scopus 로고
    • High-frequency conjugal plasmid transfer from gram-negative Escherichia coli to various gram-positive coryneform bacteria
    • Schafer A, Kalinowski J, Simon R, Seep-Feldhaus AH, and Puhler A. (1990). High-frequency conjugal plasmid transfer from gram-negative Escherichia coli to various gram-positive coryneform bacteria. J Bacteriol 172, 1663-1666.
    • (1990) J Bacteriol , vol.172 , pp. 1663-1666
    • Schafer, A.1    Kalinowski, J.2    Simon, R.3    Seep-Feldhaus, A.H.4    Puhler, A.5
  • 39
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • Schafer A, Tauch A, Jager W, Kalinowski J, Thierbach G, and Puhler A. (1994). Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145, 69-73.
    • (1994) Gene , vol.145 , pp. 69-73
    • Schafer, A.1    Tauch, A.2    Jager, W.3    Kalinowski, J.4    Thierbach, G.5    Puhler, A.6
  • 40
    • 45749154191 scopus 로고    scopus 로고
    • 1.6 angstroms structure of an NAD+ -dependent quinate dehydrogenase from Corynebacterium glutamicum
    • Schoepe J, Niefind K, and Schomburg D. (2008). 1.6 angstroms structure of an NAD+ -dependent quinate dehydrogenase from Corynebacterium glutamicum. Acta Crystallograph D64, 803-809.
    • (2008) Acta Crystallograph D , vol.64 , pp. 803-809
    • Schoepe, J.1    Niefind, K.2    Schomburg, D.3
  • 41
    • 0343488601 scopus 로고    scopus 로고
    • A reconstruction of the metabolism of Methanococcus jannaschii from sequence data
    • Selkov E, Maltsev N, Olsen GJ, Overbeek R, and Whitman WB. (1997). A reconstruction of the metabolism of Methanococcus jannaschii from sequence data. Gene 197, GC11-26.
    • (1997) Gene , vol.197
    • Selkov, E.1    Maltsev, N.2    Olsen, G.J.3    Overbeek, R.4    Whitman, W.B.5
  • 42
    • 20444447086 scopus 로고    scopus 로고
    • Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae
    • Singh S, Korolev S, Koroleva O, et al. (2005). Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae. J Biol Chem 280, 17101-17108.
    • (2005) J Biol Chem , vol.280 , pp. 17101-17108
    • Singh, S.1    Korolev, S.2    Koroleva, O.3
  • 43
    • 52449083936 scopus 로고    scopus 로고
    • A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass
    • Singh S, Stavrinides J, Christendat D, and Guttman DS. (2008). A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass. Mol Biol Evol 25, 2221-2232.
    • (2008) Mol Biol Evol , vol.25 , pp. 2221-2232
    • Singh, S.1    Stavrinides, J.2    Christendat, D.3    Guttman, D.S.4
  • 44
    • 0033452842 scopus 로고    scopus 로고
    • An integrated method for spectrum extraction and compound identification from gas chromatography/mass spectrometry data
    • Stein SE. (1999). An integrated method for spectrum extraction and compound identification from gas chromatography/mass spectrometry data. J Am Soc Mass Spect 10, 770-781.
    • (1999) J Am Soc Mass Spect , vol.10 , pp. 770-781
    • Stein, S.E.1
  • 45
    • 5044224344 scopus 로고    scopus 로고
    • Comprehensive analysis of metabolites in Corynebacterium glutamicum by gas chromatography/mass spectrometry
    • Strelkov S, Von Elstermann M, and Schomburg D. (2004). Comprehensive analysis of metabolites in Corynebacterium glutamicum by gas chromatography/mass spectrometry. Biol Chem 385, 853-861.
    • (2004) Biol Chem , vol.385 , pp. 853-861
    • Strelkov, S.1    Von Elstermann, M.2    Schomburg, D.3
  • 46
    • 0036417217 scopus 로고    scopus 로고
    • The 27.8-kb R-plasmid pTET3 from Corynebacterium glutamicum encodes the aminoglycoside adenyltransferase gene cassette aadA9 and the regulated tetracycline efflux system Tet 33 flanked by active copies of the widespread insertion sequence IS6100
    • Tauch A, Gotker S, Puhler A. Kalinowski J, and Thierbach G. (2002). The 27.8-kb R-plasmid pTET3 from Corynebacterium glutamicum encodes the aminoglycoside adenyltransferase gene cassette aadA9 and the regulated tetracycline efflux system Tet 33 flanked by active copies of the widespread insertion sequence IS6100. Plasmid 48, 117-129.
    • (2002) Plasmid , vol.48 , pp. 117-129
    • Tauch, A.1    Gotker, S.2    Puhler, A.3    Kalinowski, J.4    Thierbach, G.5
  • 47
    • 66249138103 scopus 로고    scopus 로고
    • Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum
    • Teramoto H, Inui M, and Yukawa H. (2009). Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum. App Environ Microbiol 75, 3461-3468.
    • (2009) App Environ Microbiol , vol.75 , pp. 3461-3468
    • Teramoto, H.1    Inui, M.2    Yukawa, H.3
  • 48
    • 8744232018 scopus 로고    scopus 로고
    • Automated metabolic reconstruction for Methanococcus jannaschii
    • Tsoka S, Simon D, and Ouzounis CA. (2004). Automated metabolic reconstruction for Methanococcus jannaschii. Archaea (Vancouver, B.C) 1, 223-229.
    • (2004) Archaea (Vancouver, B.C) , vol.1 , pp. 223-229
    • Tsoka, S.1    Simon, D.2    Ouzounis, C.A.3
  • 49
    • 0030444169 scopus 로고    scopus 로고
    • Molecular cloning of the Corynebacterium glutamicum ('Brevibacterium lactofermentum' AJ12036) odhA gene encoding a novel type of 2-oxoglutarate dehydrogenase
    • Usuda Y, Tujimoto N, Abe C, et al. (1996). Molecular cloning of the Corynebacterium glutamicum ('Brevibacterium lactofermentum' AJ12036) odhA gene encoding a novel type of 2-oxoglutarate dehydrogenase. Microbiology (Reading, England) 142, 3347-3354.
    • (1996) Microbiology (Reading, England) , vol.142 , pp. 3347-3354
    • Usuda, Y.1    Tujimoto, N.2    Abe, C.3
  • 50
    • 34047272388 scopus 로고
    • A generalization of the retention index system including linear temperature programmed gas-liquid partition chromatography
    • Vandendool H, and Kratz PD. (1963). A generalization of the retention index system including linear temperature programmed gas-liquid partition chromatography. J Chromatog 11, 463-471.
    • (1963) J Chromatog , vol.11 , pp. 463-471
    • Vandendool, H.1    Kratz, P.D.2
  • 51
    • 0033529707 scopus 로고    scopus 로고
    • Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis
    • Winzeler EA, Shoemaker DD, Astromof FA, et al. (1999). Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science (New York, N.Y) 285, 901-906.
    • (1999) Science (New York, N.Y) , vol.285 , pp. 901-906
    • Winzeler, E.A.1    Shoemaker, D.D.2    Astromof, F.A.3
  • 52
    • 33644873213 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt): An expanding universe of protein information
    • Wu CH, Apweiler R, Bairoc, A, et al. (2006). The Universal Protein Resource (UniProt): An expanding universe of protein information. Nucleic Acids Res 34, D187-191.
    • (2006) Nucleic Acids Res , vol.34
    • Wu, C.H.1    Apweiler, R.2    Bairoc, A.3
  • 53
    • 0038154081 scopus 로고    scopus 로고
    • The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode
    • Ye S, Von Delft F, Brooun A, Knuth MW, Swanson RV, McRee DE. (2003). The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. J Bacteriol 185, 4144-4151.
    • (2003) J Bacteriol , vol.185 , pp. 4144-4151
    • Ye, S.1    Von Delft, F.2    Brooun, A.3    Knuth, M.W.4    Swanson, R.V.5    McRee, D.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.