메뉴 건너뛰기




Volumn 183, Issue 3, 2005, Pages 176-189

Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp.

Author keywords

Carnitine; CoA transferase; Enoyl CoA hydratase; Proteus sp.; Reductase

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; BETAINE DERIVATIVE; BETAINYL COENZYME A LIGASE; CARNITINE; COENZYME A; COENZYME A TRANSFERASE; CROTONOBETAINYL COENZYME A HYDRATASE; CROTONOBETAINYL COENZYME A REDUCTASE; ENOYL COENZYME A HYDRATASE; GAMMA BUTYROBETAINYL COENZYME A; GENE PRODUCT; GENOMIC DNA; HYDROLYASE; INTEGRAL MEMBRANE PROTEIN CAIA; INTEGRAL MEMBRANE PROTEIN CAIB; INTEGRAL MEMBRANE PROTEIN CAIC; INTEGRAL MEMBRANE PROTEIN CAID; INTEGRAL MEMBRANE PROTEIN CAIT; LONG CHAIN FATTY ACID COENZYME A LIGASE; MEMBRANE PROTEIN; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 17444367677     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-005-0760-2     Document Type: Article
Times cited : (23)

References (50)
  • 1
    • 0034530550 scopus 로고    scopus 로고
    • Identification of Amycolatopsis sp. strain HR167 genes, involved in the bioconversion of ferulic acid to vanillin
    • Achterholt S, Priefert H, Steinbuchel A (2000) Identification of Amycolatopsis sp. strain HR167 genes, involved in the bioconversion of ferulic acid to vanillin. Appl Microbiol Biotechnol 54(6):799-807
    • (2000) Appl Microbiol Biotechnol , vol.54 , Issue.6 , pp. 799-807
    • Achterholt, S.1    Priefert, H.2    Steinbuchel, A.3
  • 3
    • 0025294601 scopus 로고
    • Purification and characterization of formyl-coenzyme A transferase from Oxalobacter formigenes
    • Baetz AL, Allison MJ (1990) Purification and characterization of formyl-coenzyme A transferase from Oxalobacter formigenes. J Bacteriol 172:3537-3540
    • (1990) J Bacteriol , vol.172 , pp. 3537-3540
    • Baetz, A.L.1    Allison, M.J.2
  • 4
    • 0028187864 scopus 로고
    • Preparation of proteins from gels for microsequencing
    • Baker CS, Dunn MJ (1994) Preparation of proteins from gels for microsequencing. Methods Mol Biol 32:177-184
    • (1994) Methods Mol Biol , vol.32 , pp. 177-184
    • Baker, C.S.1    Dunn, M.J.2
  • 5
    • 0030059857 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of clustered genes encoding β-hydroxybutyryl-coenzyme A dehydrogenase from Clostridium acetobutylicum ATCC 824
    • Boynton ZL, Bennett GN, Rudolph FB (1996) Cloning, sequencing, and expression of clustered genes encoding β-hydroxybutyryl-coenzyme A dehydrogenase from Clostridium acetobutylicum ATCC 824. J Bacteriol 178:3015-3024
    • (1996) J Bacteriol , vol.178 , pp. 3015-3024
    • Boynton, Z.L.1    Bennett, G.N.2    Rudolph, F.B.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0032723824 scopus 로고    scopus 로고
    • Positive co-regulation of Escherichia coli carnitine pathway cai and fix operons by CPR and the CaiF activator
    • Buchet A, Nasser W, Eichler K, Mandrand-Berthelot M-A (1999) Positive co-regulation of Escherichia coli carnitine pathway cai and fix operons by CPR and the CaiF activator. Mol Microbiol 34:562-575
    • (1999) Mol Microbiol , vol.34 , pp. 562-575
    • Buchet, A.1    Nasser, W.2    Eichler, K.3    Mandrand-Berthelot, M.-A.4
  • 8
    • 0033938369 scopus 로고    scopus 로고
    • The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes
    • Dickert S, Pierik AJ, Lindner D, Buckel W (2000) The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes. Eur J Biochem 267:3874-3884
    • (2000) Eur J Biochem , vol.267 , pp. 3874-3884
    • Dickert, S.1    Pierik, A.J.2    Lindner, D.3    Buckel, W.4
  • 9
    • 0000553533 scopus 로고
    • Sequence determination
    • Needleman SB (ed). Springer, Berlin Heidelberg New York
    • Edman P, Henschen A (1975) Sequence determination. In: Needleman SB (ed) Protein sequence determination. Springer, Berlin Heidelberg New York, pp 232-279
    • (1975) Protein Sequence Determination , pp. 232-279
    • Edman, P.1    Henschen, A.2
  • 10
    • 0027978747 scopus 로고
    • Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli
    • Eichler K, Bourgis F, Buchet A, Kleber H-P, Mandrand-Berthelot M-A (1994) Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli. Mol Microbiol 13:775-786
    • (1994) Mol Microbiol , vol.13 , pp. 775-786
    • Eichler, K.1    Bourgis, F.2    Buchet, A.3    Kleber, H.-P.4    Mandrand-Berthelot, M.-A.5
  • 11
    • 0029920825 scopus 로고    scopus 로고
    • Identification and characterization of the caiF gene encoding a potential transcriptional activator of carnitine metabolism in Escherichia coli
    • Eichler K, Lemke R, Buchet A, Kleber H-P, Mandrand-Berthelot M-A (1996) Identification and characterization of the caiF gene encoding a potential transcriptional activator of carnitine metabolism in Escherichia coli. J Bacteriol 178:1248-1257
    • (1996) J Bacteriol , vol.178 , pp. 1248-1257
    • Eichler, K.1    Lemke, R.2    Buchet, A.3    Kleber, H.-P.4    Mandrand-Berthelot, M.-A.5
  • 12
    • 0032913149 scopus 로고    scopus 로고
    • Metabolism of L(-)-carnitine by Enterobacteriaceae under aerobic conditions
    • Elssner T, Preusser A, Wagner U, Kleber H-P (1999) Metabolism of L(-)-carnitine by Enterobacteriaceae under aerobic conditions. FEMS Microbiol Lett 174:295-301
    • (1999) FEMS Microbiol Lett , vol.174 , pp. 295-301
    • Elssner, T.1    Preusser, A.2    Wagner, U.3    Kleber, H.-P.4
  • 13
    • 0034609573 scopus 로고    scopus 로고
    • Isolation, identification and synthesis of γ-butyrobetainyl-CoA and crotonobetainyl-CoA-compounds involved in carnitine metabolism of E. coli
    • Elssner T, Hennig L, Frauendorf H, Haferburg D, Kleber H-P (2000) Isolation, identification and synthesis of γ-butyrobetainyl-CoA and crotonobetainyl-CoA-compounds involved in carnitine metabolism of E. coli. Biochemistry 39:10761-10769
    • (2000) Biochemistry , vol.39 , pp. 10761-10769
    • Elssner, T.1    Hennig, L.2    Frauendorf, H.3    Haferburg, D.4    Kleber, H.-P.5
  • 14
    • 0035909051 scopus 로고    scopus 로고
    • Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli
    • Elssner T, Engemann C, Baumgart K, Kleber H-P (2001) Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli. Biochemistry 37:11140-11149
    • (2001) Biochemistry , vol.37 , pp. 11140-11149
    • Elssner, T.1    Engemann, C.2    Baumgart, K.3    Kleber, H.-P.4
  • 15
    • 0029791410 scopus 로고    scopus 로고
    • Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å resolution: A spiral fold defines the CoA-binding pocket
    • Engel CK, Mathieu M, Zeelen JP, Hiltunen JK, Wierenga RK (1996) Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å resolution: a spiral fold defines the CoA-binding pocket. EMBO J 15:5135-5145
    • (1996) EMBO J , vol.15 , pp. 5135-5145
    • Engel, C.K.1    Mathieu, M.2    Zeelen, J.P.3    Hiltunen, J.K.4    Wierenga, R.K.5
  • 16
    • 0035282410 scopus 로고    scopus 로고
    • Epigenetical regulation of carnitine metabolising enzymes in Proteus sp. under aerobic conditions
    • Engemann C, Kleber H-P (2001) Epigenetical regulation of carnitine metabolising enzymes in Proteus sp. under aerobic conditions. FEMS Microbiol Lett 196:1-6
    • (2001) FEMS Microbiol Lett , vol.196 , pp. 1-6
    • Engemann, C.1    Kleber, H.-P.2
  • 17
    • 0035011150 scopus 로고    scopus 로고
    • Biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp.
    • Engemann C, Elssner T, Kleber H-P (2001) Biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp. Arch Microbiol 175:353-359
    • (2001) Arch Microbiol , vol.175 , pp. 353-359
    • Engemann, C.1    Elssner, T.2    Kleber, H.-P.3
  • 18
    • 0035088030 scopus 로고    scopus 로고
    • Purification, characterization and cloning of isovaleryl-CoA dehydrogenase from higher plant mitochondria
    • Faivre-Nischke SE, Couee I, Vermel M, Grienenberger JM, Gualberto JM (2001) Purification, characterization and cloning of isovaleryl-CoA dehydrogenase from higher plant mitochondria. Eur J Bioche 268:1332-1339
    • (2001) Eur J Bioche , vol.268 , pp. 1332-1339
    • Faivre-Nischke, S.E.1    Couee, I.2    Vermel, M.3    Grienenberger, J.M.4    Gualberto, J.M.5
  • 20
    • 0027497020 scopus 로고
    • Identification of genes involved in utilization of acetate and acetoin in Bacillus subtilis
    • Grundy FJ, Waters DA, Takova TY, Henkin TM (1993) Identification of genes involved in utilization of acetate and acetoin in Bacillus subtilis. Mol Microbiol 10:259-271
    • (1993) Mol Microbiol , vol.10 , pp. 259-271
    • Grundy, F.J.1    Waters, D.A.2    Takova, T.Y.3    Henkin, T.M.4
  • 21
    • 0035861886 scopus 로고    scopus 로고
    • A new family of CoA-transferases
    • Heider J (2001) A new family of CoA-transferases. FEBS Lett 509:345-349
    • (2001) FEBS Lett , vol.509 , pp. 345-349
    • Heider, J.1
  • 22
    • 0024375446 scopus 로고
    • Purification and properties of carnitine dehydratase from Escherichia coli - A new enzyme of carnitine metabolisation
    • Jung H, Jung K, Kleber H-P (1989) Purification and properties of carnitine dehydratase from Escherichia coli - a new enzyme of carnitine metabolisation. Biochim Biophys Acta 1003:270-276
    • (1989) Biochim Biophys Acta , vol.1003 , pp. 270-276
    • Jung, H.1    Jung, K.2    Kleber, H.-P.3
  • 23
  • 24
    • 0037131410 scopus 로고    scopus 로고
    • CaiT of Escherichia coli, a new transporter catalysing L-carnitine/gamma-butyrobetaine exchange
    • Jung H, Buchholz M, Clausen J, Nietschke M, Revermann A, Schmidt R, Jung K (2002) CaiT of Escherichia coli, a new transporter catalysing L-carnitine/gamma-butyrobetaine exchange. J Biol Chem 42:39251-39259
    • (2002) J Biol Chem , vol.42 , pp. 39251-39259
    • Jung, H.1    Buchholz, M.2    Clausen, J.3    Nietschke, M.4    Revermann, A.5    Schmidt, R.6    Jung, K.7
  • 25
    • 0029812908 scopus 로고    scopus 로고
    • Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: Characterisation of OpuD
    • Kappes RM, Kempf B, Bremer E (1996) Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterisation of OpuD. J Bacteriol 178:5071-5079
    • (1996) J Bacteriol , vol.178 , pp. 5071-5079
    • Kappes, R.M.1    Kempf, B.2    Bremer, E.3
  • 26
    • 0027361992 scopus 로고
    • Cloning and characterization of the mouse short-chain acyl-CoA dehydrogenase cDNA
    • Kelly CL, Hinsdale ME, Wood PA (1993) Cloning and characterization of the mouse short-chain acyl-CoA dehydrogenase cDNA. Genomics 18:137-140
    • (1993) Genomics , vol.18 , pp. 137-140
    • Kelly, C.L.1    Hinsdale, M.E.2    Wood, P.A.3
  • 27
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 28
    • 0025736051 scopus 로고
    • DNA sequence and analysis of the bet genes encoding the osmoregulatory choline-glycine betaine pathway of Escherichia coli
    • Lamark T, Kaasen I, Eshoo MW, Falkenberg P, McDougall J, Strom AR (1991) DNA sequence and analysis of the bet genes encoding the osmoregulatory choline-glycine betaine pathway of Escherichia coli. Mol Microbiol 5:1049-1064
    • (1991) Mol Microbiol , vol.5 , pp. 1049-1064
    • Lamark, T.1    Kaasen, I.2    Eshoo, M.W.3    Falkenberg, P.4    McDougall, J.5    Strom, A.R.6
  • 29
    • 0027451092 scopus 로고
    • The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state
    • Lazazzera BA, Bates DM, Kiley PJ (1993) The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state. Genes Dev 7:1993-2005
    • (1993) Genes Dev , vol.7 , pp. 1993-2005
    • Lazazzera, B.A.1    Bates, D.M.2    Kiley, P.J.3
  • 30
    • 0033989161 scopus 로고    scopus 로고
    • Anaerobic toluene catabolism of Thauera aromatica: The bbs operon codes for enzymes of beta-oxidation of the intermediate benzylsuccinate
    • Leuthner B, Heider J (2000) Anaerobic toluene catabolism of Thauera aromatica: the bbs operon codes for enzymes of beta-oxidation of the intermediate benzylsuccinate. J Bacteriol 182:272-277
    • (2000) J Bacteriol , vol.182 , pp. 272-277
    • Leuthner, B.1    Heider, J.2
  • 31
    • 0034971989 scopus 로고    scopus 로고
    • Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: An enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria
    • Leutwein C, Heider J (2001) Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: an enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria. J Bacteriol 14:4288-4295
    • (2001) J Bacteriol , vol.14 , pp. 4288-4295
    • Leutwein, C.1    Heider, J.2
  • 32
    • 0024444571 scopus 로고
    • Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal β-oxidation system
    • Minami-Ishii N, Taketani S, Osumi T, Hashimoto T (1989) Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal β-oxidation system. Eur J Biochem 185:73-78
    • (1989) Eur J Biochem , vol.185 , pp. 73-78
    • Minami-Ishii, N.1    Taketani, S.2    Osumi, T.3    Hashimoto, T.4
  • 33
    • 0024599589 scopus 로고
    • Molecular cloning and nucleotide sequence of complementary DNAs encoding human short-chain acyl-coenzyme A dehydrogenase and the study of the molecular basis of human short-chain acyl-coenzyme a dehydrogenase deficiency
    • Naito E, Ozasa H, Ikeda Y, Tanaka K (1989) Molecular cloning and nucleotide sequence of complementary DNAs encoding human short-chain acyl-coenzyme A dehydrogenase and the study of the molecular basis of human short-chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest 83:1605-1613
    • (1989) J Clin Invest , vol.83 , pp. 1605-1613
    • Naito, E.1    Ozasa, H.2    Ikeda, Y.3    Tanaka, K.4
  • 34
    • 0032568611 scopus 로고    scopus 로고
    • Molecular characterization of the phenylacetic acid catabolic pathway in Pseudomonas putida U: The phenylacetyl-CoA catabolon
    • Olivera ER, Minambres B, Garcia B, Muniz C, Moreno MA, Ferrandez A, Diaz E (1998) Molecular characterization of the phenylacetic acid catabolic pathway in Pseudomonas putida U: The phenylacetyl-CoA catabolon. Proc Natl Acad Sci USA 95:6419-6424
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6419-6424
    • Olivera, E.R.1    Minambres, B.2    Garcia, B.3    Muniz, C.4    Moreno, M.A.5    Ferrandez, A.6    Diaz, E.7
  • 36
    • 0032961852 scopus 로고    scopus 로고
    • Crotonobetaine reductase from Escherichia coli consists of two proteins
    • Preusser A, Wagner U, Elssner T, Kleber H-P (1999) Crotonobetaine reductase from Escherichia coli consists of two proteins. Biochim Biophys Acta 1431:166-178
    • (1999) Biochim Biophys Acta , vol.1431 , pp. 166-178
    • Preusser, A.1    Wagner, U.2    Elssner, T.3    Kleber, H.-P.4
  • 37
    • 0032515937 scopus 로고    scopus 로고
    • Escherichia coli cAMP receptor protein-DNA complexes. 1. Energetic contributions of half-sites and flanking sequences in DNA recognition
    • Pyles EA, Chin AJ, Ching Lee J (1998) Escherichia coli cAMP receptor protein-DNA complexes. 1. Energetic contributions of half-sites and flanking sequences in DNA recognition. Biochemistry 37:5194-5200
    • (1998) Biochemistry , vol.37 , pp. 5194-5200
    • Pyles, E.A.1    Chin, A.J.2    Ching Lee, J.3
  • 38
    • 0037588575 scopus 로고    scopus 로고
    • Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer
    • Ricagno S, Jonsson S, Richards N, Lindqvist Y (2003) Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer. EMBO J 22:3210-3219
    • (2003) EMBO J , vol.22 , pp. 3210-3219
    • Ricagno, S.1    Jonsson, S.2    Richards, N.3    Lindqvist, Y.4
  • 39
    • 0028244621 scopus 로고
    • Crotonobetaine reductase from Escherichia coli - A new inducible enzyme of anaerobic metabolization of L(-)-carnitine
    • Roth S, Jung K, Jung H, Hommel RK, Kleber H-P (1994) Crotonobetaine reductase from Escherichia coli - a new inducible enzyme of anaerobic metabolization of L(-)-carnitine. Antonie van Leeuwenhoek 65:63-69
    • (1994) Antonie Van Leeuwenhoek , vol.65 , pp. 63-69
    • Roth, S.1    Jung, K.2    Jung, H.3    Hommel, R.K.4    Kleber, H.-P.5
  • 42
    • 0027324923 scopus 로고
    • Direct sequencing of single primer PCR products: A rapid method to achieve short chromosomal walks
    • Screaton GR, Bangham CR, Bell JI (1993) Direct sequencing of single primer PCR products: a rapid method to achieve short chromosomal walks. Nucleic Acids Res 21:2263-2264
    • (1993) Nucleic Acids Res , vol.21 , pp. 2263-2264
    • Screaton, G.R.1    Bangham, C.R.2    Bell, J.I.3
  • 44
    • 0000060558 scopus 로고
    • The preparation of S-succinyl coenzyme A
    • Simon EJ, Shemin D (1953) The preparation of S-succinyl coenzyme A. J Am Chem Soc 75:2520
    • (1953) J Am Chem Soc , vol.75 , pp. 2520
    • Simon, E.J.1    Shemin, D.2
  • 45
    • 0032900489 scopus 로고    scopus 로고
    • Identification and disruption of BetL, a secondary glycine betaine transport system linked to the salt tolerance of Listeria monocytogenes LO28
    • Sleator RD, Gahan CGM, Abee T, Hill C (1999) Identification and disruption of BetL, a secondary glycine betaine transport system linked to the salt tolerance of Listeria monocytogenes LO28. Appl Env Microbiol 65:2078-2083
    • (1999) Appl Env Microbiol , vol.65 , pp. 2078-2083
    • Sleator, R.D.1    Gahan, C.G.M.2    Abee, T.3    Hill, C.4
  • 47
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehlin T, Gordon J (1979) Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehlin, T.2    Gordon, J.3
  • 48
    • 0030756106 scopus 로고    scopus 로고
    • The oxygen-responsive transcriptional regulator FNR of Escherichia coli: The search for signals and reactions
    • Unden G, Schirawski J (1997) The oxygen-responsive transcriptional regulator FNR of Escherichia coli: the search for signals and reactions. Mol Microbiol 25:205-210
    • (1997) Mol Microbiol , vol.25 , pp. 205-210
    • Unden, G.1    Schirawski, J.2
  • 49
    • 0033564943 scopus 로고    scopus 로고
    • Interchange of catalytic activity within the 2-enoyl coenzyme A hydratase/isomerase superfamily based on a common active site template
    • Xiang H, Luo L, Taylor KL, Dunaway-Mariano D (1999) Interchange of catalytic activity within the 2-enoyl coenzyme A hydratase/isomerase superfamily based on a common active site template. Biochemistry 38:7638-7652
    • (1999) Biochemistry , vol.38 , pp. 7638-7652
    • Xiang, H.1    Luo, L.2    Taylor, K.L.3    Dunaway-Mariano, D.4
  • 50
    • 0032895658 scopus 로고    scopus 로고
    • The bile acid-inducible baiF gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A hydrolase
    • Ye H-Q, Mallonee DH, Wells JE, Bjoerkhem I, Hylemon PB (1999) The bile acid-inducible baiF gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A hydrolase. J Lipid Res 40:17-23
    • (1999) J Lipid Res , vol.40 , pp. 17-23
    • Ye, H.-Q.1    Mallonee, D.H.2    Wells, J.E.3    Bjoerkhem, I.4    Hylemon, P.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.