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Volumn 10, Issue 11, 2015, Pages

Primary amine oxidase of Escherichia coli is a metabolic enzyme that can use a human leukocyte molecule as a substrate

Author keywords

[No Author keywords available]

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); AMINOGLYCOSIDE ANTIBIOTIC AGENT; BACTERIAL DNA; COMPLEMENTARY DNA; HYDROGEN PEROXIDE; PHENETHYLAMINE; ESCHERICHIA COLI PROTEIN; TYNA PROTEIN, E COLI;

EID: 84953335690     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0142367     Document Type: Article
Times cited : (20)

References (84)
  • 1
    • 0028244179 scopus 로고
    • Quinoenzymes in biology
    • doi: 10.1146/annurev.bi.63.070194.001503 PMID: 7979241
    • Klinman JP, Mu D (1994) Quinoenzymes in biology. Annu Rev Biochem 63: 299-344. doi: 10.1146/annurev.bi.63.070194.001503 PMID: 7979241
    • (1994) Annu Rev Biochem , vol.63 , pp. 299-344
    • Klinman, J.P.1    Mu, D.2
  • 2
    • 0028241865 scopus 로고
    • Nucleotide sequence of the gene for monamine oxidase (maoA) from Escherichia coli
    • Azakami H, Yamashita M, Roh J, Hyeob H, Suzuki H, Kumagai H, et al. (1994) Nucleotide sequence of the gene for monamine oxidase (maoA) from Escherichia coli. J Ferment Bioeng 77: 315-319.
    • (1994) J Ferment Bioeng , vol.77 , pp. 315-319
    • Azakami, H.1    Yamashita, M.2    Roh, J.3    Hyeob, H.4    Suzuki, H.5    Kumagai, H.6
  • 3
    • 0028500866 scopus 로고
    • Purification, characterization, and crystallization of monoamine oxidase from Escherichia coli K-12
    • PMID: 7765483
    • Roh JH, Suzuki H, Azakami H, Yamashita M, Murooka Y, Kumagai H (1994) Purification, characterization, and crystallization of monoamine oxidase from Escherichia coli K-12. Biosci Biotechnol Biochem 58: 1652-1656. PMID: 7765483
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 1652-1656
    • Roh, J.H.1    Suzuki, H.2    Azakami, H.3    Yamashita, M.4    Murooka, Y.5    Kumagai, H.6
  • 4
    • 0018118377 scopus 로고
    • Genetic mapping of tyramine oxidase and arylsulfatase genes and their regulation in intergeneric hybrids of enteric bacteria
    • PMID: 361719
    • Murooka Y, Higashiura T, Harada T (1978) Genetic mapping of tyramine oxidase and arylsulfatase genes and their regulation in intergeneric hybrids of enteric bacteria. J Bacteriol 136: 714-722. PMID: 361719
    • (1978) J Bacteriol , vol.136 , pp. 714-722
    • Murooka, Y.1    Higashiura, T.2    Harada, T.3
  • 5
    • 84887255561 scopus 로고    scopus 로고
    • Finely tuned regulation of the aromatic amine degradation pathway in Escherichia coli
    • doi: 10.1128/JB.00837-13 PMID: 24013633
    • Zeng J, Spiro S (2013) Finely tuned regulation of the aromatic amine degradation pathway in Escherichia coli. J Bacteriol 195: 5141-5150. doi: 10.1128/JB.00837-13 PMID: 24013633
    • (2013) J Bacteriol , vol.195 , pp. 5141-5150
    • Zeng, J.1    Spiro, S.2
  • 6
    • 6044220123 scopus 로고    scopus 로고
    • Isolation of SOS constitutive mutants of Escherichia coli
    • doi: 10.1128/JB.186.21.7149-7160.2004 PMID: 15489426
    • O'Reilly EK, Kreuzer KN (2004) Isolation of SOS constitutive mutants of Escherichia coli. J Bacteriol 186: 7149-7160. doi: 10.1128/JB.186.21.7149-7160.2004 PMID: 15489426
    • (2004) J Bacteriol , vol.186 , pp. 7149-7160
    • O'Reilly, E.K.1    Kreuzer, K.N.2
  • 7
    • 54949139647 scopus 로고    scopus 로고
    • Inducible SOS response system of DNA repair and mutagenesis in Escherichia coli
    • PMID: 18825275
    • Janion C (2008) Inducible SOS response system of DNA repair and mutagenesis in Escherichia coli. Int J Biol Sci 4: 338-344. PMID: 18825275
    • (2008) Int J Biol Sci , vol.4 , pp. 338-344
    • Janion, C.1
  • 8
    • 51549086290 scopus 로고    scopus 로고
    • Escherichia coli NsrR regulates a pathway for the oxidation of 3-nitrotyramine to 4-hydroxy-3-nitrophenylacetate
    • doi: 10.1128/JB.00508-08 PMID: 18658270
    • Rankin LD, Bodenmiller DM, Partridge JD, Nishino SF, Spain JC, Spiro S (2008) Escherichia coli NsrR regulates a pathway for the oxidation of 3-nitrotyramine to 4-hydroxy-3-nitrophenylacetate. J Bacteriol 190: 6170-6177. doi: 10.1128/JB.00508-08 PMID: 18658270
    • (2008) J Bacteriol , vol.190 , pp. 6170-6177
    • Rankin, L.D.1    Bodenmiller, D.M.2    Partridge, J.D.3    Nishino, S.F.4    Spain, J.C.5    Spiro, S.6
  • 9
    • 0029645871 scopus 로고
    • Crystal structure of a quinoenzyme: Copper amine oxidase of Escherichia coli at 2 A resolution
    • PMID: 8591028
    • Parsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, et al. (1995) Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution. Structure 3: 1171-1184. PMID: 8591028
    • (1995) Structure , vol.3 , pp. 1171-1184
    • Parsons, M.R.1    Ma, C.2    Wilmot, C.M.3    Yadav, K.D.4    Blakeley, V.5    Corner, A.S.6
  • 10
    • 0031020045 scopus 로고    scopus 로고
    • Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: Exploring the reductive half-reaction
    • doi: 10.1021/bi962205j PMID: 9048544
    • Wilmot CM, Murray JM, Alton G, Parsons MR, Convery MA, Blakeley V, et al. (1997) Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction. Biochemistry 36: 1608-1620. doi: 10.1021/bi962205j PMID: 9048544
    • (1997) Biochemistry , vol.36 , pp. 1608-1620
    • Wilmot, C.M.1    Murray, J.M.2    Alton, G.3    Parsons, M.R.4    Ma, C.5    Blakeley, V.6
  • 11
    • 0033614821 scopus 로고    scopus 로고
    • The active site base controls cofactor reactivity in Escherichia coli amine oxidase: X-ray crystallographic studies with mutational variants
    • doi: 10.1021/bi9900469 PMID: 10387067
    • Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, et al. (1999) The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants. Biochemistry 38: 8217-8227. doi: 10.1021/bi9900469 PMID: 10387067
    • (1999) Biochemistry , vol.38 , pp. 8217-8227
    • Murray, J.M.1    Saysell, C.G.2    Wilmot, C.M.3    Tambyrajah, W.S.4    Jaeger, J.5    Knowles, P.F.6
  • 12
    • 0033607735 scopus 로고    scopus 로고
    • Visualization of dioxygen bound to copper during enzyme catalysis
    • PMID: 10576737
    • Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE (1999) Visualization of dioxygen bound to copper during enzyme catalysis. Science 286: 1724-1728. PMID: 10576737
    • (1999) Science , vol.286 , pp. 1724-1728
    • Wilmot, C.M.1    Hajdu, J.2    McPherson, M.J.3    Knowles, P.F.4    Phillips, S.E.5
  • 13
    • 20844443638 scopus 로고    scopus 로고
    • Active site rearrangement of the 2-hydrazinopyridine adduct in Escherichia coli amine oxidase to an azo copper(II) chelate form: A key role for tyrosine 369 in controlling the mobility of the TPQ-2HP adduct
    • doi: 10.1021/bi0479860 PMID: 15683242
    • Mure M, Kurtis CR, Brown DE, Rogers MS, Tambyrajah WS, Saysell C, et al. (2005) Active site rearrangement of the 2-hydrazinopyridine adduct in Escherichia coli amine oxidase to an azo copper(II) chelate form: a key role for tyrosine 369 in controlling the mobility of the TPQ-2HP adduct. Biochemistry 44: 1583-1594. doi: 10.1021/bi0479860 PMID: 15683242
    • (2005) Biochemistry , vol.44 , pp. 1583-1594
    • Mure, M.1    Kurtis, C.R.2    De, B.3    Rogers, M.S.4    Tambyrajah, W.S.5    Saysell, C.6
  • 15
    • 0036685346 scopus 로고    scopus 로고
    • Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue
    • doi: 10.1042/BJ20011435 PMID: 11985492
    • Saysell CG, Tambyrajah WS, Murray JM, Wilmot CM, Phillips SE, McPherson MJ, et al. (2002) Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue. Biochem J 365: 809-816. doi: 10.1042/BJ20011435 PMID: 11985492
    • (2002) Biochem J , vol.365 , pp. 809-816
    • Saysell, C.G.1    Tambyrajah, W.S.2    Murray, J.M.3    Wilmot, C.M.4    Phillips, S.E.5    McPherson, M.J.6
  • 16
    • 0035980283 scopus 로고    scopus 로고
    • Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential
    • PMID: 11669617
    • Murray JM, Kurtis CR, Tambyrajah W, Saysell CG, Wilmot CM, Parsons MR, et al. (2001) Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential. Biochemistry 40: 12808-12818. PMID: 11669617
    • (2001) Biochemistry , vol.40 , pp. 12808-12818
    • Murray, J.M.1    Kurtis, C.R.2    Tambyrajah, W.3    Saysell, C.G.4    Wilmot, C.M.5    Parsons, M.R.6
  • 17
    • 80051671639 scopus 로고    scopus 로고
    • Tyrosine 381 in E. Coli copper amine oxidase influences substrate specificity
    • doi: 10.1007/s00702-011-0620-y PMID: 21547391
    • Kurtis CR, Knowles PF, Parsons MR, Gaule TG, Phillips SE, McPherson MJ (2011) Tyrosine 381 in E. coli copper amine oxidase influences substrate specificity. J Neural Transm 118: 1043-1053. doi: 10.1007/s00702-011-0620-y PMID: 21547391
    • (2011) J Neural Transm , vol.118 , pp. 1043-1053
    • Kurtis, C.R.1    Knowles, P.F.2    Parsons, M.R.3    Gaule, T.G.4    Phillips, S.E.5    McPherson, M.J.6
  • 18
    • 84885438576 scopus 로고    scopus 로고
    • How Escherichia coli tolerates profuse hydrogen peroxide formation by a catabolic pathway
    • doi: 10.1128/JB.00737-13 PMID: 23913322
    • Ravindra Kumar S, Imlay JA (2013) How Escherichia coli tolerates profuse hydrogen peroxide formation by a catabolic pathway. J Bacteriol 195: 4569-4579. doi: 10.1128/JB.00737-13 PMID: 23913322
    • (2013) J Bacteriol , vol.195 , pp. 4569-4579
    • Ravindra Kumar, S.1    Imlay, J.A.2
  • 19
    • 84856044295 scopus 로고    scopus 로고
    • Ectoenzymes controlling leukocyte traffic
    • doi: 10.1002/eji.201142223 PMID: 22359101
    • Salmi M, Jalkanen S (2012) Ectoenzymes controlling leukocyte traffic. Eur J Immunol 42: 284-292. doi: 10.1002/eji.201142223 PMID: 22359101
    • (2012) Eur J Immunol , vol.42 , pp. 284-292
    • Salmi, M.1    Jalkanen, S.2
  • 20
    • 0000075317 scopus 로고
    • Techniques for transformation of E. Coli
    • In: Glover D, editor., Washington DC.
    • Hanahan D (1985) Techniques for transformation of E. coli In: Glover D, editor. DNA cloning: A practical approach: IRL Press, Washington DC. pp. 109-135.
    • (1985) DNA Cloning: A Practical Approach: IRL Press , pp. 109-135
    • Hanahan, D.1
  • 21
    • 0023929118 scopus 로고
    • Evidence for two genetic loci in Yersinia enterocolitica that can promote invasion of epithelial cells
    • PMID: 2833444
    • Miller VL, Falkow S (1988) Evidence for two genetic loci in Yersinia enterocolitica that can promote invasion of epithelial cells. Infect Immun 56: 1242-1248. PMID: 2833444
    • (1988) Infect Immun , vol.56 , pp. 1242-1248
    • Miller, V.L.1    Falkow, S.2
  • 22
    • 0028358260 scopus 로고
    • Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5-and Tn10-Derived minitransposons
    • PMID: 8057911
    • de Lorenzo V, Timmis KN (1994) Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5-and Tn10-Derived minitransposons. Methods Enzymol 235: 386-405. PMID: 8057911
    • (1994) Methods Enzymol , vol.235 , pp. 386-405
    • De Lorenzo, V.1    Timmis, K.N.2
  • 23
    • 0029096439 scopus 로고
    • A novel locus of Yersinia enterocolitica serotype O:3 involved in lipopolysaccharide outer core biosynthesis
    • PMID: 8559076
    • Skurnik M, Venho R, Toivanen P, al-Hendy A (1995) A novel locus of Yersinia enterocolitica serotype O:3 involved in lipopolysaccharide outer core biosynthesis. Mol Microbiol 17: 575-594. PMID: 8559076
    • (1995) Mol Microbiol , vol.17 , pp. 575-594
    • Skurnik, M.1    Venho, R.2    Toivanen, P.3    Al-Hendy, A.4
  • 24
    • 0347325071 scopus 로고    scopus 로고
    • Lysogeny at mid-Twentieth century: P1, P2, and other experimental systems
    • PMID: 14729683
    • Bertani G (2004) Lysogeny at mid-Twentieth century: P1, P2, and other experimental systems. J Bacteriol 186: 595-600. PMID: 14729683
    • (2004) J Bacteriol , vol.186 , pp. 595-600
    • Bertani, G.1
  • 29
    • 0031568289 scopus 로고    scopus 로고
    • A continuous spectrophotometric assay for monoamine oxidase and related enzymes in tissue homogenates
    • doi: 10.1006/abio.1996.9911 PMID: 9025956
    • Holt A, Sharman DF, Baker GB, Palcic MM (1997) A continuous spectrophotometric assay for monoamine oxidase and related enzymes in tissue homogenates. Anal Biochem 244: 384-392. doi: 10.1006/abio.1996.9911 PMID: 9025956
    • (1997) Anal Biochem , vol.244 , pp. 384-392
    • Holt, A.1    Sharman, D.F.2    Baker, G.B.3    Palcic, M.M.4
  • 30
    • 33749326396 scopus 로고    scopus 로고
    • Vascular amine oxidases are needed for leukocyte extravasation into inflamed joints in vivo
    • doi: 10.1002/art.22061 PMID: 16947396
    • Marttila-Ichihara F, Smith DJ, Stolen C, Yegutkin GG, Elima K, Mercier N, et al. (2006) Vascular amine oxidases are needed for leukocyte extravasation into inflamed joints in vivo. Arthritis Rheum 54: 2852-2862. doi: 10.1002/art.22061 PMID: 16947396
    • (2006) Arthritis Rheum , vol.54 , pp. 2852-2862
    • Marttila-Ichihara, F.1    Smith, D.J.2    Stolen, C.3    Yegutkin, G.G.4    Elima, K.5    Mercier, N.6
  • 31
    • 28744458859 scopus 로고    scopus 로고
    • Bioconductor: Open software development for computational biology and bioinformatics
    • doi: 10.1186/gb-2004-5-10-r80 PMID: 15461798
    • Gentleman RC, Carey VJ, Bates DM, Bolstad B, Dettling M, Dudoit S, et al. (2004) Bioconductor: open software development for computational biology and bioinformatics. Genome Biol 5: R80. doi: 10.1186/gb-2004-5-10-r80 PMID: 15461798
    • (2004) Genome Biol , vol.5 , pp. R80
    • Gentleman, R.C.1    Carey, V.J.2    Bates, D.M.3    Bolstad, B.4    Dettling, M.5    Dudoit, S.6
  • 34
    • 0036081355 scopus 로고    scopus 로고
    • Gene Expression Omnibus: NCBI gene expression and hybridization array data repository
    • PMID: 11752295
    • Edgar R, Domrachev M, Lash AE (2002) Gene Expression Omnibus: NCBI gene expression and hybridization array data repository. Nucleic Acids Res 30: 207-210. PMID: 11752295
    • (2002) Nucleic Acids Res , vol.30 , pp. 207-210
    • Edgar, R.1    Domrachev, M.2    Lash, A.E.3
  • 35
    • 33749349218 scopus 로고    scopus 로고
    • Carbocyclic hydrazino inhibitors of copper-containing amine oxidases
    • Publ. No.: WO 03/006003 A1; Chem Abstr.
    • Smith D, Fulop F, Pihlavisto M, Lazar L, Alaranta S, Vainio P (2003) Carbocyclic hydrazino inhibitors of copper-containing amine oxidases. Int Pat Appl; Publ. No.: WO 03/006003 A1; Chem Abstr. 138, 57890.
    • (2003) Int Pat Appl , vol.138 , pp. 57890
    • Smith, D.1    Fulop, F.2    Pihlavisto, M.3    Lazar, L.4    Alaranta, S.5    Vainio, P.6
  • 36
    • 84857289455 scopus 로고    scopus 로고
    • Characterization of the in vitro binding and inhibition kinetics of primary amine oxidase/vascular adhesion protein-1 by glucosamine
    • doi: 10.1016/j.bbagen.2011.12.009 PMID: 22202180
    • Olivieri A, Tipton KF, O'Sullivan J (2012) Characterization of the in vitro binding and inhibition kinetics of primary amine oxidase/vascular adhesion protein-1 by glucosamine. Biochim Biophys Acta 1820: 482-487. doi: 10.1016/j.bbagen.2011.12.009 PMID: 22202180
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 482-487
    • Olivieri, A.1    Tipton, K.F.2    O'Sullivan, J.3
  • 37
    • 84864600170 scopus 로고    scopus 로고
    • Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria
    • doi: 10.1016/j.abb. 2012.02.007 PMID.22381957
    • Chiang SM, Schellhorn HE (2012) Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria. Arch Biochem Biophys 525: 161-169. doi: 10.1016/j.abb. 2012.02.007 PMID: 22381957
    • (2012) Arch Biochem Biophys , vol.525 , pp. 161-169
    • Chiang, S.M.1    Schellhorn, H.E.2
  • 38
    • 0036267337 scopus 로고    scopus 로고
    • Regulation of Salmonella enterica serovar Typhimurium mntH transcription by H(2)O(2), Fe(2+), and Mn(2+)
    • PMID: 12029030
    • Kehres DG, Janakiraman A, Slauch JM, Maguire ME (2002) Regulation of Salmonella enterica serovar Typhimurium mntH transcription by H(2)O(2), Fe(2+), and Mn(2+). J Bacteriol 184: 3151-3158. PMID: 12029030
    • (2002) J Bacteriol , vol.184 , pp. 3151-3158
    • Kehres, D.G.1    Janakiraman, A.2    Slauch, J.M.3    Maguire, M.E.4
  • 39
    • 0030930252 scopus 로고    scopus 로고
    • OxyR-Dependent induction of Escherichia coli grx gene expression by peroxide stress
    • PMID: 9294462
    • Tao K (1997) oxyR-Dependent induction of Escherichia coli grx gene expression by peroxide stress. J Bacteriol 179: 5967-5970. PMID: 9294462
    • (1997) J Bacteriol , vol.179 , pp. 5967-5970
    • Tao, K.1
  • 40
    • 0006198640 scopus 로고
    • Hydrogen peroxide-inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins
    • PMID: 3534881
    • Morgan RW, Christman MF, Jacobson FS, Storz G, Ames BN (1986) Hydrogen peroxide-inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins. Proc Natl Acad Sci U S A 83: 8059-8063. PMID: 3534881
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 8059-8063
    • Morgan, R.W.1    Christman, M.F.2    Jacobson, F.S.3    Storz, G.4    Ames, B.N.5
  • 41
    • 0036449408 scopus 로고    scopus 로고
    • Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase
    • PMID: 12473114
    • Brock M, Maerker C, Schutz A, Volker U, BuckelW(2002) Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Eur J Biochem 269: 6184-6194. PMID: 12473114
    • (2002) Eur J Biochem , vol.269 , pp. 6184-6194
    • Brock, M.1    Maerker, C.2    Schutz, A.3    Volker, U.4    Buckel, W.5
  • 42
    • 0034687819 scopus 로고    scopus 로고
    • Nitrogen regulatory protein C-controlled genes of Escherichia coli: Scavenging as a defense against nitrogen limitation
    • doi: 10.1073/pnas.97.26.14674 PMID: 11121068
    • Zimmer DP, Soupene E, Lee HL, Wendisch VF, Khodursky AB, Peter BJ, et al. (2000) Nitrogen regulatory protein C-controlled genes of Escherichia coli: scavenging as a defense against nitrogen limitation. Proc Natl Acad Sci U S A 97: 14674-14679. doi: 10.1073/pnas.97.26.14674 PMID: 11121068
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14674-14679
    • Zimmer, D.P.1    Soupene, E.2    Lee, H.L.3    Wendisch, V.F.4    Khodursky, A.B.5    Peter, B.J.6
  • 43
    • 0026512058 scopus 로고
    • Involvement of the narJ or narW gene product in the formation of active nitrate reductase in Escherichia coli
    • PMID: 1545706
    • Blasco F, Pommier J, Augier V, Chippaux M, Giordano G (1992) Involvement of the narJ or narW gene product in the formation of active nitrate reductase in Escherichia coli. Mol Microbiol 6: 221-230. PMID: 1545706
    • (1992) Mol Microbiol , vol.6 , pp. 221-230
    • Blasco, F.1    Pommier, J.2    Augier, V.3    Chippaux, M.4    Giordano, G.5
  • 44
    • 59049089396 scopus 로고    scopus 로고
    • Killing niche competitors by remote-control bacteriophage induction
    • doi: 10.1073/pnas.0809600106 PMID: 19141630
    • Selva L, Viana D, Regev-Yochay G, Trzcinski K, Corpa JM, Lasa I, et al. (2009) Killing niche competitors by remote-control bacteriophage induction. Proc Natl Acad Sci U S A 106: 1234-1238. doi: 10.1073/pnas.0809600106 PMID: 19141630
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 1234-1238
    • Selva, L.1    Viana, D.2    Regev-Yochay, G.3    Trzcinski, K.4    Corpa, J.M.5    Lasa, I.6
  • 45
    • 0036718479 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated killing of Caenorhabditis elegans by Streptococcus pyogenes
    • PMID: 12183571
    • Jansen WT, Bolm M, Balling R, Chhatwal GS, Schnabel R (2002) Hydrogen peroxide-mediated killing of Caenorhabditis elegans by Streptococcus pyogenes. Infect Immun 70: 5202-5207. PMID: 12183571
    • (2002) Infect Immun , vol.70 , pp. 5202-5207
    • Jansen, W.T.1    Bolm, M.2    Balling, R.3    Chhatwal, G.S.4    Schnabel, R.5
  • 46
    • 0034469174 scopus 로고    scopus 로고
    • Loss of O157 O antigenicity of verotoxin-producing Escherichia coli O157:H7 surviving under starvation conditions
    • PMID: 11097947
    • Hara-Kudo Y, Miyahara M, Kumagai S (2000) Loss of O157 O antigenicity of verotoxin-producing Escherichia coli O157:H7 surviving under starvation conditions. Appl Environ Microbiol 66: 5540-5543. PMID: 11097947
    • (2000) Appl Environ Microbiol , vol.66 , pp. 5540-5543
    • Hara-Kudo, Y.1    Miyahara, M.2    Kumagai, S.3
  • 47
    • 0031596380 scopus 로고    scopus 로고
    • Survival of enterohemorrhagic Escherichia coli O157:H7 in water
    • PMID: 9709245
    • Wang G, Doyle MP (1998) Survival of enterohemorrhagic Escherichia coli O157:H7 in water. J Food Prot 61: 662-667. PMID: 9709245
    • (1998) J Food Prot , vol.61 , pp. 662-667
    • Wang, G.1    Doyle, M.P.2
  • 48
    • 84880995036 scopus 로고    scopus 로고
    • Ss-Phenylethylamine as a novel nutrient treatment to reduce bacterial contamination due to Escherichia coli O157:H7 on beef meat
    • doi: 10.1016/j.meatsci.2013.06.030 PMID: 23896151
    • Lynnes T, Horne SM, Pruss BM (2014) ss-Phenylethylamine as a novel nutrient treatment to reduce bacterial contamination due to Escherichia coli O157:H7 on beef meat. Meat Sci 96: 165-171. doi: 10.1016/j.meatsci.2013.06.030 PMID: 23896151
    • (2014) Meat Sci , vol.96 , pp. 165-171
    • Lynnes, T.1    Horne, S.M.2    Pruss, B.M.3
  • 50
    • 77956292377 scopus 로고    scopus 로고
    • Bacterial phenylalanine and phenylacetate catabolic pathway revealed
    • doi: 10.1073/pnas.1005399107 PMID: 20660314
    • Teufel R, Mascaraque V, Ismail W, Voss M, Perera J, EisenreichW, et al. (2010) Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc Natl Acad Sci U S A 107: 14390-14395. doi: 10.1073/pnas.1005399107 PMID: 20660314
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 14390-14395
    • Teufel, R.1    Mascaraque, V.2    Ismail, W.3    Voss, M.4    EisenreichW, P.J.5
  • 51
    • 33744952844 scopus 로고    scopus 로고
    • Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI
    • doi: 10.1074/jbc.M513896200 PMID: 16464851
    • Song F, Zhuang Z, Finci L, Dunaway-Mariano D, Kniewel R, Buglino JA, et al. (2006) Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI. J Biol Chem 281: 11028-11038. doi: 10.1074/jbc.M513896200 PMID: 16464851
    • (2006) J Biol Chem , vol.281 , pp. 11028-11038
    • Song, F.1    Zhuang, Z.2    Finci, L.3    Dunaway-Mariano, D.4    Kniewel, R.5    Buglino, J.A.6
  • 52
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • PMID: 11179804
    • Pomposiello PJ, Demple B (2001) Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol 19: 109-114. PMID: 11179804
    • (2001) Trends Biotechnol , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 53
    • 84879422944 scopus 로고    scopus 로고
    • The molecular mechanisms and physiological consequences of oxidative stress: Lessons from a model bacterium
    • doi: 10.1038/nrmicro3032 PMID: 23712352
    • Imlay JA (2013) The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium. Nat Rev Microbiol 11: 443-454. doi: 10.1038/nrmicro3032 PMID: 23712352
    • (2013) Nat Rev Microbiol , vol.11 , pp. 443-454
    • Imlay, J.A.1
  • 54
    • 84874786351 scopus 로고    scopus 로고
    • Escherichia coli avoids high dissolved oxygen stress by activation of SoxRS and manganese-superoxide dismutase
    • doi: 10.1186/1475-2859-12-23 PMID: 23497217
    • Baez A, Shiloach J (2013) Escherichia coli avoids high dissolved oxygen stress by activation of SoxRS and manganese-superoxide dismutase. Microb Cell Fact 12: 23. doi: 10.1186/1475-2859-12-23 PMID: 23497217
    • (2013) Microb Cell Fact , vol.12 , pp. 23
    • Baez, A.1    Shiloach, J.2
  • 55
    • 79957788648 scopus 로고    scopus 로고
    • Novel roles of cAMP receptor protein (CRP) in regulation of transport and metabolism of carbon sources
    • doi: 10.1371/journal. pone.0020081 PMID: 21673794
    • Shimada T, Fujita N, Yamamoto K, Ishihama A (2011) Novel roles of cAMP receptor protein (CRP) in regulation of transport and metabolism of carbon sources. PLoS One 6: e20081. doi: 10.1371/journal. pone.0020081 PMID: 21673794
    • (2011) PLoS One , vol.6 , pp. e20081
    • Shimada, T.1    Fujita, N.2    Yamamoto, K.3    Ishihama, A.4
  • 56
    • 0039771974 scopus 로고    scopus 로고
    • Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in Escherichia coli
    • PMID: 10766858
    • Ferrandez A, Garcia JL, Diaz E (2000) Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in Escherichia coli. J Biol Chem 275: 12214-12222. PMID: 10766858
    • (2000) J Biol Chem , vol.275 , pp. 12214-12222
    • Ferrandez, A.1    Garcia, J.L.2    Diaz, E.3
  • 57
    • 67649400754 scopus 로고    scopus 로고
    • CAMP receptor protein from Escherichia coli as a model of signal transduction in proteins-A review
    • doi: 10.1159/000178014 PMID: 19033675
    • Fic E, Bonarek P, Gorecki A, Kedracka-Krok S, Mikolajczak J, Polit A, et al. (2009) cAMP receptor protein from escherichia coli as a model of signal transduction in proteins-A review. J Mol Microbiol Biotechnol 17: 1-11. doi: 10.1159/000178014 PMID: 19033675
    • (2009) J Mol Microbiol Biotechnol , vol.17 , pp. 1-11
    • Fic, E.1    Bonarek, P.2    Gorecki, A.3    Kedracka-Krok, S.4    Mikolajczak, J.5    Polit, A.6
  • 58
    • 84899760229 scopus 로고    scopus 로고
    • Insights on the regulation of the phenylacetate degradation pathway from Escherichia coli
    • doi: 10.1111/1758-2229.12117 PMID: 24983528
    • Fernandez C, Diaz E, Garcia JL (2014) Insights on the regulation of the phenylacetate degradation pathway from Escherichia coli. Environ Microbiol Rep 6: 239-250. doi: 10.1111/1758-2229.12117 PMID: 24983528
    • (2014) Environ Microbiol Rep , vol.6 , pp. 239-250
    • Fernandez, C.1    Diaz, E.2    Garcia, J.L.3
  • 59
    • 47549110972 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: Many ways to make the most out of nutrients
    • doi: 10.1038/nrmicro1932 PMID: 18628769
    • Gorke B, Stulke J (2008) Carbon catabolite repression in bacteria: many ways to make the most out of nutrients. Nat Rev Microbiol 6: 613-624. doi: 10.1038/nrmicro1932 PMID: 18628769
    • (2008) Nat Rev Microbiol , vol.6 , pp. 613-624
    • Gorke, B.1    Stulke, J.2
  • 60
    • 16844384950 scopus 로고    scopus 로고
    • Catabolite repression of the propionate catabolic genes in Escherichia coli and Salmonella enterica: Evidence for involvement of the cyclic AMP receptor protein
    • doi: 10.1128/JB.187.8.2793-2800.2005 PMID: 15805526
    • Lee SK, Newman JD, Keasling JD (2005) Catabolite repression of the propionate catabolic genes in Escherichia coli and Salmonella enterica: evidence for involvement of the cyclic AMP receptor protein. J Bacteriol 187: 2793-2800. doi: 10.1128/JB.187.8.2793-2800.2005 PMID: 15805526
    • (2005) J Bacteriol , vol.187 , pp. 2793-2800
    • Lee, S.K.1    Newman, J.D.2    Keasling, J.D.3
  • 61
    • 0034822014 scopus 로고    scopus 로고
    • Metabolic context and possible physiological themes of sigma(54)-Dependent genes in Escherichia coli
    • doi: 10.1128/MMBR.65.3.422-444.2001 PMID: 11528004 table of contents
    • Reitzer L, Schneider BL (2001) Metabolic context and possible physiological themes of sigma(54)-Dependent genes in Escherichia coli. Microbiol Mol Biol Rev 65: 422-444, table of contents. doi: 10.1128/MMBR.65.3.422-444.2001 PMID: 11528004
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 422-444
    • Reitzer, L.1    Schneider, B.L.2
  • 62
    • 84862338886 scopus 로고    scopus 로고
    • The mechanism of sugar-mediated catabolite repression of the propionate catabolic genes in Escherichia coli
    • doi: 10.1016/j.gene.2012.04.074 PMID: 22579471
    • Park JM, Vinuselvi P, Lee SK (2012) The mechanism of sugar-mediated catabolite repression of the propionate catabolic genes in Escherichia coli. Gene 504: 116-121. doi: 10.1016/j.gene.2012.04.074 PMID: 22579471
    • (2012) Gene , vol.504 , pp. 116-121
    • Park, J.M.1    Vinuselvi, P.2    Lee, S.K.3
  • 63
    • 0031036839 scopus 로고    scopus 로고
    • The ldhA gene encoding the fermentative lactate dehydrogenase of Escherichia coli
    • PMID: 9025293
    • Bunch PK, Mat-Jan F, Lee N, Clark DP (1997) The ldhA gene encoding the fermentative lactate dehydrogenase of Escherichia coli. Microbiology 143 (Pt 1): 187-195. PMID: 9025293
    • (1997) Microbiology 143 (Pt 1 , pp. 187-195
    • Bunch, P.K.1    Mat-Jan, F.2    Lee, N.3    Clark, D.P.4
  • 64
    • 13244255241 scopus 로고    scopus 로고
    • Isolation and characterization of an aldehyde dehydrogenase encoded by the aldB gene of Escherichia coli
    • doi: 10.1128/JB.187.3.1067-1073.2005 PMID: 15659684
    • Ho KK, Weiner H (2005) Isolation and characterization of an aldehyde dehydrogenase encoded by the aldB gene of Escherichia coli. J Bacteriol 187: 1067-1073. doi: 10.1128/JB.187.3.1067-1073.2005 PMID: 15659684
    • (2005) J Bacteriol , vol.187 , pp. 1067-1073
    • Ho, K.K.1    Weiner, H.2
  • 65
    • 33746059357 scopus 로고    scopus 로고
    • Optimal production of poly-gamma-glutamic acid by metabolically engineered Escherichia coli
    • doi: 10.1007/s10529-006-9080-0 PMID: 16816893
    • Jiang H, Shang L, Yoon SH, Lee SY, Yu Z (2006) Optimal production of poly-gamma-glutamic acid by metabolically engineered Escherichia coli. Biotechnol Lett 28: 1241-1246. doi: 10.1007/s10529-006-9080-0 PMID: 16816893
    • (2006) Biotechnol Lett , vol.28 , pp. 1241-1246
    • Jiang, H.1    Shang, L.2    Yoon, S.H.3    Lee, S.Y.4    Yu, Z.5
  • 66
    • 58249087122 scopus 로고    scopus 로고
    • A single channel for nitrate uptake, nitrite export and nitrite uptake by Escherichia coli NarU and a role for NirC in nitrite export and uptake
    • doi: 10.1042/BJ20080746 PMID: 18691156
    • Jia W, Tovell N, Clegg S, Trimmer M, Cole J (2009) A single channel for nitrate uptake, nitrite export and nitrite uptake by Escherichia coli NarU and a role for NirC in nitrite export and uptake. Biochem J 417: 297-304. doi: 10.1042/BJ20080746 PMID: 18691156
    • (2009) Biochem J , vol.417 , pp. 297-304
    • Jia, W.1    Tovell, N.2    Clegg, S.3    Trimmer, M.4    Cole, J.5
  • 67
    • 27644450582 scopus 로고    scopus 로고
    • Structural and functional comparison of HemN to other radical SAM enzymes
    • doi: 10.1515/BC.2005.113 PMID: 16218869
    • Layer G, Kervio E, Morlock G, Heinz DW, Jahn D, Retey J, et al. (2005) Structural and functional comparison of HemN to other radical SAM enzymes. Biol Chem 386: 971-980. doi: 10.1515/BC.2005.113 PMID: 16218869
    • (2005) Biol Chem , vol.386 , pp. 971-980
    • Layer, G.1    Kervio, E.2    Morlock, G.3    Heinz, D.W.4    Jahn, D.5    Retey, J.6
  • 68
    • 84878415056 scopus 로고    scopus 로고
    • GlgS, described previously as a glycogen synthesis control protein, negatively regulates motility and biofilm formation in Escherichia coli
    • doi: 10.1042/BJ20130154 PMID: 23537328
    • Rahimpour M, Montero M, Almagro G, Viale AM, Sevilla A, Canovas M, et al. (2013) GlgS, described previously as a glycogen synthesis control protein, negatively regulates motility and biofilm formation in Escherichia coli. Biochem J 452: 559-573. doi: 10.1042/BJ20130154 PMID: 23537328
    • (2013) Biochem J , vol.452 , pp. 559-573
    • Rahimpour, M.1    Montero, M.2    Almagro, G.3    Viale, A.M.4    Sevilla, A.5    Canovas, M.6
  • 69
    • 0031042325 scopus 로고    scopus 로고
    • Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca
    • doi: 10.1099/00221287-143-2-505 PMID: 9043125
    • Hacisalihoglu A, Jongejan JA, Duine JA (1997) Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca. Microbiology 143 (Pt 2): 505-512. doi: 10.1099/00221287-143-2-505 PMID: 9043125
    • (1997) Microbiology , vol.143 , Issue.PT2 , pp. 505-512
    • Hacisalihoglu, A.1    Jongejan, J.A.2    Duine, J.A.3
  • 70
    • 0026750046 scopus 로고
    • A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene
    • PMID: 1556068
    • Sugino H, Sasaki M, Azakami H, Yamashita M, Murooka Y (1992) A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene. J Bacteriol 174: 2485-2492. PMID: 1556068
    • (1992) J Bacteriol , vol.174 , pp. 2485-2492
    • Sugino, H.1    Sasaki, M.2    Azakami, H.3    Yamashita, M.4    Murooka, Y.5
  • 71
    • 0141959363 scopus 로고
    • Phenylethylamine oxidase, a novel enzyme of Arthrobacter globiformis may be a quinoprotein
    • Shimizu E, Ichise H, Yorifuji T (1990) Phenylethylamine oxidase, a novel enzyme of Arthrobacter globiformis may be a quinoprotein. Agric Biol Chem 54: 851-853.
    • (1990) Agric Biol Chem , vol.54 , pp. 851-853
    • Shimizu, E.1    Ichise, H.2    Yorifuji, T.3
  • 72
    • 0028964417 scopus 로고
    • Copper/topa quinone-containing histamine oxidase from Arthrobacter globiformis. Molecular cloning and sequencing, overproduction of precursor enzyme, and generation of topa quinone cofactor
    • PMID: 7876243
    • Choi YH, Matsuzaki R, Fukui T, Shimizu E, Yorifuji T, Sato H, et al. (1995) Copper/topa quinone-containing histamine oxidase from Arthrobacter globiformis. Molecular cloning and sequencing, overproduction of precursor enzyme, and generation of topa quinone cofactor. J Biol Chem 270: 4712-4720. PMID: 7876243
    • (1995) J Biol Chem , vol.270 , pp. 4712-4720
    • Choi, Y.H.1    Matsuzaki, R.2    Fukui, T.3    Shimizu, E.4    Yorifuji, T.5    Sato, H.6
  • 73
    • 0027254762 scopus 로고
    • Cloning, sequencing, expression, and regulation of the structural gene for the copper/topa quinone-containing methylamine oxidase from Arthrobacter strain P1, a gram-positive facultative methylotroph
    • PMID: 8366046
    • Zhang X, Fuller JH, McIntire WS (1993) Cloning, sequencing, expression, and regulation of the structural gene for the copper/topa quinone-containing methylamine oxidase from Arthrobacter strain P1, a gram-positive facultative methylotroph. J Bacteriol 175: 5617-5627. PMID: 8366046
    • (1993) J Bacteriol , vol.175 , pp. 5617-5627
    • Zhang, X.1    Fuller, J.H.2    McIntire, W.S.3
  • 74
    • 0028605705 scopus 로고
    • Evidence of a self-catalytic mechanism of 2, 4, 5-Trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase
    • PMID: 7798196
    • Cai D, Klinman JP (1994) Evidence of a self-catalytic mechanism of 2, 4, 5-Trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase. J Biol Chem 269: 32039-32042. PMID: 7798196
    • (1994) J Biol Chem , vol.269 , pp. 32039-32042
    • Cai, D.1    Klinman, J.P.2
  • 75
    • 54249116014 scopus 로고    scopus 로고
    • Copper distributed by Atx1 is available to copper amine oxidase 1 in Schizosaccharomyces pombe
    • doi: 10.1128/EC. 00230-08 PMID.18723604
    • Peter C, Laliberte J, Beaudoin J, Labbe S (2008) Copper distributed by Atx1 is available to copper amine oxidase 1 in Schizosaccharomyces pombe. Eukaryot Cell 7: 1781-1794. doi: 10.1128/EC. 00230-08 PMID: 18723604
    • (2008) Eukaryot Cell , vol.7 , pp. 1781-1794
    • Peter, C.1    Laliberte, J.2    Beaudoin, J.3    Labbe, S.4
  • 76
    • 0029621215 scopus 로고
    • Substrate-specificity of mammalian tissue-bound semicarbazide-sensitive amine oxidase
    • PMID: 8584666
    • Lyles GA (1995) Substrate-specificity of mammalian tissue-bound semicarbazide-sensitive amine oxidase. Prog Brain Res 106: 293-303. PMID: 8584666
    • (1995) Prog Brain Res , vol.106 , pp. 293-303
    • Lyles, G.A.1
  • 77
    • 19944434024 scopus 로고    scopus 로고
    • Absence of the endothelial oxidase AOC3 leads to abnormal leukocyte traffic in vivo
    • doi: 10.1016/j.immuni.2004.12.006 PMID: 15664163
    • Stolen CM, Marttila-Ichihara F, Koskinen K, Yegutkin GG, Turja R, Bono P, et al. (2005) Absence of the endothelial oxidase AOC3 leads to abnormal leukocyte traffic in vivo. Immunity 22: 105-115. doi: 10.1016/j.immuni.2004.12.006 PMID: 15664163
    • (2005) Immunity , vol.22 , pp. 105-115
    • Stolen, C.M.1    Marttila-Ichihara, F.2    Koskinen, K.3    Yegutkin, G.G.4    Turja, R.5    Bono, P.6
  • 78
    • 0028360735 scopus 로고
    • Primary structures for a mammalian cellular and serum copper amine oxidase
    • PMID: 8144587
    • Mu D, Medzihradszky KF, Adams GW, Mayer P, Hines WM, Burlingame AL, et al. (1994) Primary structures for a mammalian cellular and serum copper amine oxidase. J Biol Chem 269: 9926-9932. PMID: 8144587
    • (1994) J Biol Chem , vol.269 , pp. 9926-9932
    • Mu, D.1    Medzihradszky, K.F.2    Adams, G.W.3    Mayer, P.4    Hines, W.M.5    Burlingame, A.L.6
  • 79
    • 84899916081 scopus 로고    scopus 로고
    • Ectoenzymes in leukocyte migration and their therapeutic potential
    • doi: 10.1007/s00281-014-0417-9 PMID: 24638888
    • Salmi M, Jalkanen S (2014) Ectoenzymes in leukocyte migration and their therapeutic potential. Semin Immunopathol 36: 163-176. doi: 10.1007/s00281-014-0417-9 PMID: 24638888
    • (2014) Semin Immunopathol , vol.36 , pp. 163-176
    • Salmi, M.1    Jalkanen, S.2
  • 80
    • 25844523991 scopus 로고    scopus 로고
    • Cell-surface enzymes in control of leukocyte trafficking
    • PMID: 16200079
    • Salmi M, Jalkanen S (2005) Cell-surface enzymes in control of leukocyte trafficking. Nat Rev Immunol 5: 760-771. PMID: 16200079
    • (2005) Nat Rev Immunol , vol.5 , pp. 760-771
    • Salmi, M.1    Jalkanen, S.2
  • 82
    • 73949110156 scopus 로고    scopus 로고
    • Human Siglec-10 can bind to vascular adhesion protein-1 and serves as its substrate
    • doi: 10.1182/blood-2009-04-219253 PMID: 19861682
    • Kivi E, Elima K, Aalto K, Nymalm Y, Auvinen K, Koivunen E, et al. (2009) Human Siglec-10 can bind to vascular adhesion protein-1 and serves as its substrate. Blood 114: 5385-5392. doi: 10.1182/blood-2009-04-219253 PMID: 19861682
    • (2009) Blood , vol.114 , pp. 5385-5392
    • Kivi, E.1    Elima, K.2    Aalto, K.3    Nymalm, Y.4    Auvinen, K.5    Koivunen, E.6
  • 83
    • 80053364442 scopus 로고    scopus 로고
    • Siglec-9 is a novel leukocyte ligand for vascular adhesion protein-1 and can be used in PET imaging of inflammation and cancer
    • doi: 10.1182/blood-2010-09-311076 PMID: 21821708
    • Aalto K, Autio A, Kiss EA, Elima K, Nymalm Y, Veres TZ, et al. (2011) Siglec-9 is a novel leukocyte ligand for vascular adhesion protein-1 and can be used in PET imaging of inflammation and cancer. Blood 118: 3725-3733. doi: 10.1182/blood-2010-09-311076 PMID: 21821708
    • (2011) Blood , vol.118 , pp. 3725-3733
    • Aalto, K.1    Autio, A.2    Kiss, E.A.3    Elima, K.4    Nymalm, Y.5    Veres, T.Z.6
  • 84
    • 1942456908 scopus 로고    scopus 로고
    • Granulocyte transmigration through the endothelium is regulated by the oxidase activity of vascular adhesion protein-1 (VAP-1)
    • PMID: 14726375
    • Koskinen K, Vainio PJ, Smith DJ, Pihlavisto M, Yla-Herttuala S, Jalkanen S, et al. (2004) Granulocyte transmigration through the endothelium is regulated by the oxidase activity of vascular adhesion protein-1 (VAP-1). Blood 103: 3388-3395. doi: 10.1182/blood-2003-09-3275 PMID: 14726375
    • (2004) Blood , vol.103 , pp. 3388-3395
    • Koskinen, K.1    Vainio, P.J.2    Smith, D.J.3    Pihlavisto, M.4    Yla-Herttuala, S.5    Jalkanen, S.6


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