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Volumn 390, Issue 2, 2005, Pages 583-590

Bacillus subtilis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase revisited: Resolution of two long-standing enigmas

Author keywords

3 deoxy D arabino heptulosonate 7 phosphate synthase (DAHPS); Bacillus subtilis; Bifunctional enzyme; Chorismate mutase; Marburg strain; Metalloenzyme

Indexed keywords

BACTERIA; BIOCHEMISTRY; CARBOXYLIC ACIDS; DERIVATIVES; PHOSPHATES; REACTION KINETICS;

EID: 25144431811     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050294     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 0029556907 scopus 로고
    • The biosynthesis of shikimate metabolites
    • Dewick, P. M. (1995) The biosynthesis of shikimate metabolites. Nat. Prod. Rep. 12, 579-607
    • (1995) Nat. Prod. Rep. , vol.12 , pp. 579-607
    • Dewick, P.M.1
  • 2
    • 0034956417 scopus 로고    scopus 로고
    • The biosynthesis of shikimate metabolites
    • Knaggs, A. R. (2001) The biosynthesis of shikimate metabolites. Nat. Prod. Rep. 18, 334-355
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 334-355
    • Knaggs, A.R.1
  • 3
    • 0037321888 scopus 로고    scopus 로고
    • The biosynthesis of shikimate metabolites
    • Knaggs, A. R. (2003) The biosynthesis of shikimate metabolites. Nat. Prod. Rep. 20, 119-136
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 119-136
    • Knaggs, A.R.1
  • 4
    • 0025189923 scopus 로고
    • Monofunctional chorismate mutase from Bacillus subtilis: Purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli
    • Gray, J. V., Golinelli-Pimpaneau, B. and Knowles, J. R. (1990) Monofunctional chorismate mutase from Bacillus subtilis: purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli. Biochemistry 29, 376-383
    • (1990) Biochemistry , vol.29 , pp. 376-383
    • Gray, J.V.1    Golinelli-Pimpaneau, B.2    Knowles, J.R.3
  • 6
    • 1442264878 scopus 로고    scopus 로고
    • Expression, purification, and characterization of 3-deoxy-d-arabino- heptulosonate 7-phosphate synthase from Pyrococcus furiosus
    • Schofield, L. R., Patchett, M. L. and Parker, E. J. (2004) Expression, purification, and characterization of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Pyrococcus furiosus. Protein Expr. Purif. 34, 17-27
    • (2004) Protein Expr. Purif. , vol.34 , pp. 17-27
    • Schofield, L.R.1    Patchett, M.L.2    Parker, E.J.3
  • 7
    • 0035843276 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase does not catalyze the formation of the ribo analogue
    • Sundaram, A. K. and Woodard, R. W. (2001) Neisseria gonorrhoeae 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase does not catalyze the formation of the ribo analogue. Org. Lett. 3, 21-24
    • (2001) Org. Lett. , vol.3 , pp. 21-24
    • Sundaram, A.K.1    Woodard, R.W.2
  • 8
    • 0027992458 scopus 로고
    • The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction
    • Chook, Y. M., Gray, J. V., Ke, H. and Lipscomb, W. N. (1994) The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction. J. Mol. Biol. 240, 476-500
    • (1994) J. Mol. Biol. , vol.240 , pp. 476-500
    • Chook, Y.M.1    Gray, J.V.2    Ke, H.3    Lipscomb, W.N.4
  • 9
    • 0016194177 scopus 로고
    • Regulation of aromatic amino acid biosynthesis in Bacillus subtilis 168. Purification, characterization, and subunit structure of the bifunctional enzyme 3-deoxy-D-arabinoheptulosonate 7-phosphate synthetase-chorismate mutase
    • Huang, L., Nakatsukasa, M. and Nester, E. (1974) Regulation of aromatic amino acid biosynthesis in Bacillus subtilis 168. Purification, characterization, and subunit structure of the bifunctional enzyme 3-deoxy-D-arabinoheptulosonate 7-phosphate synthetase-chorismate mutase. J. Biol. Chem. 249, 4467-4472
    • (1974) J. Biol. Chem. , vol.249 , pp. 4467-4472
    • Huang, L.1    Nakatsukasa, M.2    Nester, E.3
  • 10
    • 0001380494 scopus 로고
    • Induced biochemical mutations in Bacillus subtilis
    • Burkholder, P. R. and Giles, Jr, N. H. (1947) Induced biochemical mutations in Bacillus subtilis. Am. J. Bot. 34, 345-348
    • (1947) Am. J. Bot. , vol.34 , pp. 345-348
    • Burkholder, P.R.1    Giles Jr., N.H.2
  • 11
    • 0016230962 scopus 로고
    • Characterization of the functional activities of the subunits of 3-deoxy-D-arabinoheptulosonate 7-phosphate synthetase-chorismate mutase from Bacillus subtilis 168
    • Huang, L., Montoya, A. L. and Nester, E. W. (1974) Characterization of the functional activities of the subunits of 3-deoxy-D-arabinoheptulosonate 7-phosphate synthetase-chorismate mutase from Bacillus subtilis 168. J. Biol. Chem. 249, 4473-4479
    • (1974) J. Biol. Chem. , vol.249 , pp. 4473-4479
    • Huang, L.1    Montoya, A.L.2    Nester, E.W.3
  • 12
    • 0018900465 scopus 로고
    • Evidence for an artificially evolved bifunctional 3-deoxy-D-arabino- heptulosonate-7-phosphatesynthase-chorismate mutase in Bacillus subtilis
    • Llewellyn, D. J., Daday, A. and Smith, G. D. (1980) Evidence for an artificially evolved bifunctional 3-deoxy-D-arabino-heptulosonate-7- phosphatesynthase-chorismate mutase in Bacillus subtilis. J. Biol. Chem. 255, 2077-2084
    • (1980) J. Biol. Chem. , vol.255 , pp. 2077-2084
    • Llewellyn, D.J.1    Daday, A.2    Smith, G.D.3
  • 13
    • 0028825812 scopus 로고
    • Identical amino acid sequence of the aroA(G) gene products of Bacillus subtilis 168 and B. subtilis Marburg strain
    • Bolotin, A., Khazak, V., Stoynova, N., Ratmanova, K., Yomantas, Y. and Kozlov, Y. (1995) Identical amino acid sequence of the aroA(G) gene products of Bacillus subtilis 168 and B. subtilis Marburg strain. Microbiology 141, 2219-2222
    • (1995) Microbiology , vol.141 , pp. 2219-2222
    • Bolotin, A.1    Khazak, V.2    Stoynova, N.3    Ratmanova, K.4    Yomantas, Y.5    Kozlov, Y.6
  • 14
    • 0035097138 scopus 로고    scopus 로고
    • Aquifex aeolicus 3-deoxy-d-manno-2-octulosonic acid 8-phosphate synthase: A new class of KDO 8-P synthase?
    • Birck, M. R. and Woodard, R. W. (2001) Aquifex aeolicus 3-deoxy-d-manno-2-octulosonic acid 8-phosphate synthase: a new class of KDO 8-P synthase? J. Mol. Evol. 52, 205-214
    • (2001) J. Mol. Evol. , vol.52 , pp. 205-214
    • Birck, M.R.1    Woodard, R.W.2
  • 15
    • 0036175457 scopus 로고    scopus 로고
    • The correct phylogenetic relationship of KdsA (3-deoxy-d-manno- octulosonate 8-phosphate synthase) with one of two independently evolved classes of AroA (3-deoxy-d-arabino-heptulosonate 7-phosphate synthase)
    • Jensen, R. A., Xie, G., Calhoun, D. H. and Bonner, C. A. (2002) The correct phylogenetic relationship of KdsA (3-deoxy-d-manno-octulosonate 8-phosphate synthase) with one of two independently evolved classes of AroA (3-deoxy-d-arabino-heptulosonate 7-phosphate synthase). J. Mol. Evol. 54, 416-423
    • (2002) J. Mol. Evol. , vol.54 , pp. 416-423
    • Jensen, R.A.1    Xie, G.2    Calhoun, D.H.3    Bonner, C.A.4
  • 16
    • 0031963257 scopus 로고    scopus 로고
    • Substrate ambiguit of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Neisseria gonorrhoeae in the context of its membership in a protein family containing a subset of 3-deoxy-D-arabino-heptulosonate 8-phosphate synthases
    • Subramaniam, P. S., Xie, G., Xia, T. and Jensen, R. A. (1998) Substrate ambiguit of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Neisseria gonorrhoeae in the context of its membership in a protein family containing a subset of 3-deoxy-D-arabino-heptulosonate 8-phosphate synthases. J. Bacteriol. 180, 119-127
    • (1998) J. Bacteriol. , vol.180 , pp. 119-127
    • Subramaniam, P.S.1    Xie, G.2    Xia, T.3    Jensen, R.A.4
  • 17
    • 0034972509 scopus 로고    scopus 로고
    • Microbial origin of plant-type 2-keto-3-deoxy-D-arabino-heptulosonate 7-phosphate synthases, exemplified by the chorismate- and tryptophan-regulated enzyme from Xanthomonas campestris
    • Gosset, G., Bonner, C. A. and Jensen, R. A. (2001) Microbial origin of plant-type 2-keto-3-deoxy-D-arabino-heptulosonate 7-phosphate synthases, exemplified by the chorismate- and tryptophan-regulated enzyme from Xanthomonas campestris. J. Bacteriol. 183, 4061-4070
    • (2001) J. Bacteriol. , vol.183 , pp. 4061-4070
    • Gosset, G.1    Bonner, C.A.2    Jensen, R.A.3
  • 18
    • 0014027806 scopus 로고
    • Regulatory enzymes of aromatic amino acid biosynthesis in Bacillus subtilis. I. Purification and properties of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase
    • Jensen, R. A. and Nester, E. W. (1966) Regulatory enzymes of aromatic amino acid biosynthesis in Bacillus subtilis. I. Purification and properties of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase. J. Biol. Chem. 241, 3365-3372
    • (1966) J. Biol. Chem. , vol.241 , pp. 3365-3372
    • Jensen, R.A.1    Nester, E.W.2
  • 19
    • 0025720117 scopus 로고
    • Analysis of the metal requirement of 3-deoxy-D-arabino-heptulosonate-7- phosphate synthase from Escherichia coli
    • Stephens, C. M. and Bauerle, R. (1991) Analysis of the metal requirement of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. J. Biol. Chem. 266, 20810-20817
    • (1991) J. Biol. Chem. , vol.266 , pp. 20810-20817
    • Stephens, C.M.1    Bauerle, R.2
  • 20
    • 0041845392 scopus 로고    scopus 로고
    • Thermotoga maritima 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase: The ancestral eubacterial DAHP synthase?
    • Wu, J., Howe, D. L. and Woodard, R. W. (2003) Thermotoga maritima 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase: the ancestral eubacterial DAHP synthase? J. Biol. Chem. 278, 27525-27531
    • (2003) J. Biol. Chem. , vol.278 , pp. 27525-27531
    • Wu, J.1    Howe, D.L.2    Woodard, R.W.3
  • 21
    • 0034636974 scopus 로고    scopus 로고
    • Structure of 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: Comparison of the Mn(2+)*2-phosphoglycolate and the Pb(2+)*2-phosphoenolpyruvate complexes and implications for catalysis
    • Wagner, T., Shumilin, I. A., Bauerle, R. and Kretsinger, R. H. (2000) Structure of 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: comparison of the Mn(2+)*2-phosphoglycolate and the Pb(2+)*2-phosphoenolpyruvate complexes and implications for catalysis. J. Mol. Biol. 301, 389-399
    • (2000) J. Mol. Biol. , vol.301 , pp. 389-399
    • Wagner, T.1    Shumilin, I.A.2    Bauerle, R.3    Kretsinger, R.H.4
  • 23
    • 0032483696 scopus 로고    scopus 로고
    • Enzymatic synthesis of 3-deoxy-D-manno-octulosonate 8-phosphate, 3-deoxy-D-altro-octulosonate 8-phosphate, 3,5-dideoxy-D-gluco(manno)- octulosonate 8-phosphate by 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
    • Sheflyan, G. Y., Howe, D. L., Wilson, T. L. and Woodard, R. W. (1998) Enzymatic synthesis of 3-deoxy-D-manno-octulosonate 8-phosphate, 3-deoxy-D-altro-octulosonate 8-phosphate, 3,5-dideoxy-D-gluco(manno)- octulosonate 8-phosphate by 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. J. Am. Chem. Soc. 120, 11027-11032
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11027-11032
    • Sheflyan, G.Y.1    Howe, D.L.2    Wilson, T.L.3    Woodard, R.W.4
  • 24
    • 0014951925 scopus 로고
    • Tyrosine biosynthesis in Aerobacter-Aerogenes - Purification and properties of chorismate mutase-prephenate dehydrogenase
    • Koch, G. L. E., Shaw, D. C. and Gibson, F. (1970) Tyrosine biosynthesis in Aerobacter-Aerogenes - purification and properties of chorismate mutase-prephenate dehydrogenase. Biochim. Biophys. Acta 212, 375-386
    • (1970) Biochim. Biophys. Acta , vol.212 , pp. 375-386
    • Koch, G.L.E.1    Shaw, D.C.2    Gibson, F.3
  • 25
    • 0035235980 scopus 로고    scopus 로고
    • The emerging periplasm-localized subclass of AroQ chorismate mutases, exemplified by those from Salmonella typhimurium and Pseudomonas aeruginosa
    • research0030.1-research0030.16
    • Calhoun, D. H., Bonner, C. A., Gu, W., Xie, G. and Jensen, R. A. (2001) The emerging periplasm-localized subclass of AroQ chorismate mutases, exemplified by those from Salmonella typhimurium and Pseudomonas aeruginosa. Genome Biol. 2, research0030.1-research0030.16
    • (2001) Genome Biol. , vol.2
    • Calhoun, D.H.1    Bonner, C.A.2    Gu, W.3    Xie, G.4    Jensen, R.A.5
  • 26
    • 0029109922 scopus 로고
    • Atomic-structure of the buried catalytic pocket of Escherichia-coli chorismate mutase
    • Lee, A. Y., Karplus, P. A., Ganem, B. and Clardy, J. (1995) Atomic-structure of the buried catalytic pocket of Escherichia-coli chorismate mutase. J. Am. Chem. Soc. 117, 3627-3628
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3627-3628
    • Lee, A.Y.1    Karplus, P.A.2    Ganem, B.3    Clardy, J.4
  • 27
    • 0034700263 scopus 로고    scopus 로고
    • Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random protein-termination strategy
    • Gamper, M., Hilvert, D. and Kast, P. (2000) Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random protein-termination strategy. Biochemistry 39, 14087-14094
    • (2000) Biochemistry , vol.39 , pp. 14087-14094
    • Gamper, M.1    Hilvert, D.2    Kast, P.3
  • 28
    • 0034725580 scopus 로고    scopus 로고
    • A metal bridge between two enzyme families: 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Aquifex aeolicus requires a divalent metal for activity
    • Duewel, H. S. and Woodard, R. W. (2000) A metal bridge between two enzyme families: 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Aquifex aeolicus requires a divalent metal for activity. J. Biol. Chem. 275, 22824-22831
    • (2000) J. Biol. Chem. , vol.275 , pp. 22824-22831
    • Duewel, H.S.1    Woodard, R.W.2
  • 29
    • 0033565448 scopus 로고    scopus 로고
    • Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino- heptulosonate-7-phosphate synthase from Escherichia coli
    • Shumilin, I. A., Kretsinger, R. H. and Bauerle, R. (1999) Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. Structure Fold. Des. 7, 865-875
    • (1999) Structure Fold. Des. , vol.7 , pp. 865-875
    • Shumilin, I.A.1    Kretsinger, R.H.2    Bauerle, R.3
  • 30
    • 0035951088 scopus 로고    scopus 로고
    • Structures of Aquifex aeolicus KD08P synthase in complex with R5P and PEP, and with a bisubstrate inhibitor: Role of active site water in catalysis
    • Wang, J., Duewel, H. S., Woodard, R. W. and Gatti, D. L. (2001) Structures of Aquifex aeolicus KD08P synthase in complex with R5P and PEP, and with a bisubstrate inhibitor: role of active site water in catalysis. Biochemistry 40, 15676-15683
    • (2001) Biochemistry , vol.40 , pp. 15676-15683
    • Wang, J.1    Duewel, H.S.2    Woodard, R.W.3    Gatti, D.L.4
  • 31
    • 0035896523 scopus 로고    scopus 로고
    • Substrate and metal complexes of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Aquifex aeolicus at 1.9 Å resolution: Implications for the condensation mechanism
    • Duewel, H. S., Radaev, S., Wang, J., Woodard, R. W. and Gatti, D. L. (2001) Substrate and metal complexes of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Aquifex aeolicus at 1.9 Å resolution: implications for the condensation mechanism. J. Biol. Chem. 276, 8393-8402
    • (2001) J. Biol. Chem. , vol.276 , pp. 8393-8402
    • Duewel, H.S.1    Radaev, S.2    Wang, J.3    Woodard, R.W.4    Gatti, D.L.5
  • 32
    • 0037060468 scopus 로고    scopus 로고
    • Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme
    • Krosky, D. J., Alm, R., Berg, M., Carmel, G., Tummino, P. J., Xu, B. and Yang, W. (2002) Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme. Biochim. Biophys. Acta 1594, 297-306
    • (2002) Biochim. Biophys. Acta , vol.1594 , pp. 297-306
    • Krosky, D.J.1    Alm, R.2    Berg, M.3    Carmel, G.4    Tummino, P.J.5    Xu, B.6    Yang, W.7
  • 33
    • 0017114285 scopus 로고
    • 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase - Purification, properties, and kinetics of tyrosine-sensitive isozyme from Escherichia coli
    • Schoner, R. and Herrmann, K. M. (1976) 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase - purification, properties, and kinetics of tyrosine-sensitive isozyme from Escherichia coli. J. Biol. Chem. 251, 5440-5447
    • (1976) J. Biol. Chem. , vol.251 , pp. 5440-5447
    • Schoner, R.1    Herrmann, K.M.2
  • 34
    • 0026065718 scopus 로고
    • Purification and properties of tryptophan-sensitive 3-deoxy-D-arabino- heptulosonate-7-phosphate synthase from Escherichia coli
    • Ray, J. M. and Bauerle, R. (1991) Purification and properties of tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. J. Bacteriol. 173, 1894-1901
    • (1991) J. Bacteriol. , vol.173 , pp. 1894-1901
    • Ray, J.M.1    Bauerle, R.2
  • 35
    • 0019743835 scopus 로고
    • Some kinetic properties of the tryptophan-sensitive 3-deoxy-D-arabino- heptulosonate 7-phosphate synthase from Neurospora crassa
    • Nimmo, G. A. and Coggins, J. R. (1981) Some kinetic properties of the tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Neurospora crassa. Biochem. J. 199, 657-665
    • (1981) Biochem. J. , vol.199 , pp. 657-665
    • Nimmo, G.A.1    Coggins, J.R.2
  • 36
    • 0014013007 scopus 로고
    • Control of three isoenzymic 7-phospho-2-oxo-3-deoxy-D-arabino-heptonate- D-erythrose-4-phosphate lyases of Escherichia coli W and derived mutants by repressive and 'inductive' effects of the aromatic amino acids
    • Brown, K. D. and Doy, C. H. (1966) Control of three isoenzymic 7-phospho-2-oxo-3-deoxy-D-arabino-heptonate-D-erythrose-4-phosphate lyases of Escherichia coli W and derived mutants by repressive and 'inductive' effects of the aromatic amino acids. Biochim. Biophys. Acta 118, 157-172
    • (1966) Biochim. Biophys. Acta , vol.118 , pp. 157-172
    • Brown, K.D.1    Doy, C.H.2
  • 37
    • 0027464649 scopus 로고
    • The cloning and nucleotide sequence of a Corynebacterium glutamicum 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase gene
    • Chen, C. C., Liao, C. C. and Hsu, W. H. (1993) The cloning and nucleotide sequence of a Corynebacterium glutamicum 3-deoxy-D-arabinoheptulosonate-7- phosphate synthase gene. FEMS Microbiol. Lett. 107, 223-229
    • (1993) FEMS Microbiol. Lett. , vol.107 , pp. 223-229
    • Chen, C.C.1    Liao, C.C.2    Hsu, W.H.3
  • 38
    • 0014027850 scopus 로고
    • Regulatory enzymes of aromatic amino acid biosynthesis in Bacillus subtilis. II. The enzymology of feedback inhibition of 3-deoxy-D-arabino- heptulosonate 7-phosphate synthetase
    • Jensen, R. A. and Nester, E. W. (1966) Regulatory enzymes of aromatic amino acid biosynthesis in Bacillus subtilis. II. The enzymology of feedback inhibition of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase. J. Biol. Chem. 241, 3373-3380
    • (1966) J. Biol. Chem. , vol.241 , pp. 3373-3380
    • Jensen, R.A.1    Nester, E.W.2
  • 39
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


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