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Volumn 177, Issue 3, 2008, Pages 188-197

Mitochondrial protein thiol modifications in acetaminophen hepatotoxicity: Effect on HMG-CoA synthase

Author keywords

Acetaminophen; Hepatotoxicity; HMG CoA synthase; Mitochondria; Proteomics; Thiols

Indexed keywords

ALANINE AMINOTRANSFERASE; CELL PROTEIN; GLUTATHIONE; HYDROXYMETHYLGLUTARYL COENZYME A SYNTHASE; MITOCHONDRIAL PROTEIN; N ACETYL 1,4 BENZOQUINONE IMINE; PARACETAMOL; THIOL;

EID: 40849137599     PISSN: 03784274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxlet.2008.01.010     Document Type: Article
Times cited : (40)

References (56)
  • 2
    • 0141630636 scopus 로고    scopus 로고
    • Scavenging peroxynitrite with glutathione promotes regeneration and enhances survival during acetaminophen-induced liver injury in mice
    • Bajt M.L., Knight T.R., Farhood A., and Jaeschke H. Scavenging peroxynitrite with glutathione promotes regeneration and enhances survival during acetaminophen-induced liver injury in mice. J. Pharmacol. Exper. Therap. 307 (2003) 67-73
    • (2003) J. Pharmacol. Exper. Therap. , vol.307 , pp. 67-73
    • Bajt, M.L.1    Knight, T.R.2    Farhood, A.3    Jaeschke, H.4
  • 3
    • 33749617086 scopus 로고    scopus 로고
    • Nuclear translocation of endonuclease G and apoptosis-inducing factor during acetaminophen-induced liver cell injury
    • Bajt M.L., Cover C., Lemasters J.J., and Jaeschke H. Nuclear translocation of endonuclease G and apoptosis-inducing factor during acetaminophen-induced liver cell injury. Toxicol. Sci. 94 (2006) 217-225
    • (2006) Toxicol. Sci. , vol.94 , pp. 217-225
    • Bajt, M.L.1    Cover, C.2    Lemasters, J.J.3    Jaeschke, H.4
  • 4
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • Barford D. The role of cysteine residues as redox-sensitive regulatory switches. Curr. Opin. Struct. Biol. 14 (2004) 679-686
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 679-686
    • Barford, D.1
  • 5
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins
    • Beer S.M., Taylor E.R., Brown S.E., Dahm C.C., Costa N.J., Runswick M.J., and Murphy M.P. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins. J. Biol. Chem. 279 (2004) 47939-47951
    • (2004) J. Biol. Chem. , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6    Murphy, M.P.7
  • 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 M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 1-2 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 1842852852 scopus 로고    scopus 로고
    • Protection against acetaminophen hepatotoxicity by clofibrate pretreatment: role of catalase induction
    • Chen C., Hennig G.E., Whiteley H.E., and Manautou J.E. Protection against acetaminophen hepatotoxicity by clofibrate pretreatment: role of catalase induction. J. Biochem. Mol. Toxicol. 16 (2002) 227-234
    • (2002) J. Biochem. Mol. Toxicol. , vol.16 , pp. 227-234
    • Chen, C.1    Hennig, G.E.2    Whiteley, H.E.3    Manautou, J.E.4
  • 8
    • 0033594991 scopus 로고    scopus 로고
    • Protein and nonprotein cysteinyl thiol modifications by N-acetyl-p-benzoquinone imine via a novel ipso adduct
    • Chen W., Shocker J.P., Tonge R., Hunter A., Gartner C., and Nelson S.D. Protein and nonprotein cysteinyl thiol modifications by N-acetyl-p-benzoquinone imine via a novel ipso adduct. Biochemistry 38 (1999) 8159-8166
    • (1999) Biochemistry , vol.38 , pp. 8159-8166
    • Chen, W.1    Shocker, J.P.2    Tonge, R.3    Hunter, A.4    Gartner, C.5    Nelson, S.D.6
  • 9
    • 0016861431 scopus 로고
    • Intracellular localization of the 3-hydroxy-3-methylglutaryl coenzyme A cycle enzymes in liver
    • Clinkenbeard K.D., Reed W.D., Mooney R.A., and Lane M.D. Intracellular localization of the 3-hydroxy-3-methylglutaryl coenzyme A cycle enzymes in liver. J. Biol. Chem. 250 (1974) 3108-3116
    • (1974) J. Biol. Chem. , vol.250 , pp. 3108-3116
    • Clinkenbeard, K.D.1    Reed, W.D.2    Mooney, R.A.3    Lane, M.D.4
  • 11
    • 0036803249 scopus 로고    scopus 로고
    • Nanotransducers in cellular redox signaling: modifications of thiols by reactive oxygen and nitrogen species
    • Cooper C.E., Patel R.P., Brookes P.S., and Darley-Usmar V.M. Nanotransducers in cellular redox signaling: modifications of thiols by reactive oxygen and nitrogen species. Trends Biochem. Sci. 27 (2002) 489-492
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 489-492
    • Cooper, C.E.1    Patel, R.P.2    Brookes, P.S.3    Darley-Usmar, V.M.4
  • 13
    • 0342601372 scopus 로고    scopus 로고
    • Inactivation of glyceraldehydes-3-phosphate dehydrogenase by a reactive metabolite of acetaminophen and mass spectral characterization of an arylated active site peptide
    • Dietze E.C., Schafer A., Omichinski J.G., and Nelson S.D. Inactivation of glyceraldehydes-3-phosphate dehydrogenase by a reactive metabolite of acetaminophen and mass spectral characterization of an arylated active site peptide. Chem. Res. Toxicol. 10 (1997) 1097-1103
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 1097-1103
    • Dietze, E.C.1    Schafer, A.2    Omichinski, J.G.3    Nelson, S.D.4
  • 14
    • 0036802227 scopus 로고    scopus 로고
    • Recent developments in the intracellular degradation of oxidized proteins
    • Dunlop R.A., Rodgers K.J., and Dean R.T. Recent developments in the intracellular degradation of oxidized proteins. Free. Radic. Biol. Med. 33 (2002) 894-906
    • (2002) Free. Radic. Biol. Med. , vol.33 , pp. 894-906
    • Dunlop, R.A.1    Rodgers, K.J.2    Dean, R.T.3
  • 15
    • 0028868238 scopus 로고
    • Feeding S-adenosyl-l-methionine attenuates both ethanol-induced depletion of mitochondrial glutathione and mitochondrial dysfunction in periportal and perivenous rat hepatocytes
    • Garcia-Ruiz C., Morales A., Colell A., Ballesta A., Rodes J., Kaplowitz N., and Fernandez-Checa J.C. Feeding S-adenosyl-l-methionine attenuates both ethanol-induced depletion of mitochondrial glutathione and mitochondrial dysfunction in periportal and perivenous rat hepatocytes. Hepatology 21 (1995) 207-213
    • (1995) Hepatology , vol.21 , pp. 207-213
    • Garcia-Ruiz, C.1    Morales, A.2    Colell, A.3    Ballesta, A.4    Rodes, J.5    Kaplowitz, N.6    Fernandez-Checa, J.C.7
  • 16
    • 0037184525 scopus 로고    scopus 로고
    • How to flip the (redox) switch
    • Geogiou G. How to flip the (redox) switch. Cell 111 (2002) 607-610
    • (2002) Cell , vol.111 , pp. 607-610
    • Geogiou, G.1
  • 17
    • 0036304261 scopus 로고    scopus 로고
    • Mode of cell death after acetaminophen overdose in mice: apoptosis or oncotic necrosis?
    • Gujral J.S., Knight T.R., Farhood A., Bajt M.L., and Jaeschke H. Mode of cell death after acetaminophen overdose in mice: apoptosis or oncotic necrosis?. Toxicol. Sci. 67 (2002) 322-328
    • (2002) Toxicol. Sci. , vol.67 , pp. 322-328
    • Gujral, J.S.1    Knight, T.R.2    Farhood, A.3    Bajt, M.L.4    Jaeschke, H.5
  • 18
    • 0033559336 scopus 로고    scopus 로고
    • Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase: a control enzyme in ketogenesis
    • Hegardt F.G. Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase: a control enzyme in ketogenesis. Biochem. J. 338 (1999) 569-582
    • (1999) Biochem. J. , vol.338 , pp. 569-582
    • Hegardt, F.G.1
  • 20
    • 0025673837 scopus 로고
    • Glutathione disulfide formation and oxidant stress during acetaminophen-induced hepatotoxicity in mice in vivo: the protective effect of allopurinol
    • Jaeschke H. Glutathione disulfide formation and oxidant stress during acetaminophen-induced hepatotoxicity in mice in vivo: the protective effect of allopurinol. J. Pharmacol. Exp. Ther. 255 (1990) 935-941
    • (1990) J. Pharmacol. Exp. Ther. , vol.255 , pp. 935-941
    • Jaeschke, H.1
  • 21
    • 29544448331 scopus 로고    scopus 로고
    • Intracellular signaling mechanisms of acetaminophen-induced liver cell death
    • Jaeschke H., and Bajt M.L. Intracellular signaling mechanisms of acetaminophen-induced liver cell death. Toxicol. Sci. 89 (2006) 31-41
    • (2006) Toxicol. Sci. , vol.89 , pp. 31-41
    • Jaeschke, H.1    Bajt, M.L.2
  • 22
    • 0043135016 scopus 로고    scopus 로고
    • The role of oxidant stress and reactive nitrogen species in acetaminophen hepatotoxicity
    • Jaeschke H., Knight T.R., and Bajt M.L. The role of oxidant stress and reactive nitrogen species in acetaminophen hepatotoxicity. Toxicol. Lett. 144 (2003) 279-288
    • (2003) Toxicol. Lett. , vol.144 , pp. 279-288
    • Jaeschke, H.1    Knight, T.R.2    Bajt, M.L.3
  • 23
    • 0034255470 scopus 로고    scopus 로고
    • Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH
    • Kim J., Yoon H.W., Kwon K., Lee S., and Rhee S.G. Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH. Anal. Biochem. 283 (2000) 214-221
    • (2000) Anal. Biochem. , vol.283 , pp. 214-221
    • Kim, J.1    Yoon, H.W.2    Kwon, K.3    Lee, S.4    Rhee, S.G.5
  • 24
    • 0036289628 scopus 로고    scopus 로고
    • Dysfunction of rat liver mitochondria by selenite: induction of mitochondrial permeability transition through thiol-oxidation
    • Kim T.S., Jeong D.W., Yun B.Y., and Kim I.Y. Dysfunction of rat liver mitochondria by selenite: induction of mitochondrial permeability transition through thiol-oxidation. Biochem. Biophys. Res. Commun. 294 (2002) 1130-1137
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 1130-1137
    • Kim, T.S.1    Jeong, D.W.2    Yun, B.Y.3    Kim, I.Y.4
  • 25
    • 0036828064 scopus 로고    scopus 로고
    • Peroxynitrite is a critical mediator of acetaminophen hepatotoxicity in murine livers: protection by glutathione
    • Knight T.R., Ho Y.S., Farhood A., and Jaeschke H. Peroxynitrite is a critical mediator of acetaminophen hepatotoxicity in murine livers: protection by glutathione. J. Pharmacol. Exp. Ther. 303 (2002) 468-475
    • (2002) J. Pharmacol. Exp. Ther. , vol.303 , pp. 468-475
    • Knight, T.R.1    Ho, Y.S.2    Farhood, A.3    Jaeschke, H.4
  • 26
    • 0034894722 scopus 로고    scopus 로고
    • Vascular and hepatocellular peroxynitrite formation during acetaminophen-induced liver injury: role of mitochondrial oxidant stress
    • Knight T.R., Kurtz A., Bajt M.L., Hinson J.A., and Jaeschke H. Vascular and hepatocellular peroxynitrite formation during acetaminophen-induced liver injury: role of mitochondrial oxidant stress. Toxicol. Sci. 62 (2001) 212-220
    • (2001) Toxicol. Sci. , vol.62 , pp. 212-220
    • Knight, T.R.1    Kurtz, A.2    Bajt, M.L.3    Hinson, J.A.4    Jaeschke, H.5
  • 27
    • 7044226521 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in acetaminophen-induced necrotic and apoptotic cell death to cultured mouse hepatocytes
    • Kon K., Kim J.S., Jaeschke H., and Lemasters J.J. Mitochondrial permeability transition in acetaminophen-induced necrotic and apoptotic cell death to cultured mouse hepatocytes. Hepatology 40 (2004) 1170-1179
    • (2004) Hepatology , vol.40 , pp. 1170-1179
    • Kon, K.1    Kim, J.S.2    Jaeschke, H.3    Lemasters, J.J.4
  • 28
    • 31344467471 scopus 로고    scopus 로고
    • A sensitive method for the quantitative measurement of protein thiol modification in response to oxidative stress
    • Landar A., Oh J.Y., Giles N.M., Isom A., Kirk M., Barnes S., and Darley-Usmar V.M. A sensitive method for the quantitative measurement of protein thiol modification in response to oxidative stress. Free Radic. Biol. Med. 40 (2006) 459-468
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 459-468
    • Landar, A.1    Oh, J.Y.2    Giles, N.M.3    Isom, A.4    Kirk, M.5    Barnes, S.6    Darley-Usmar, V.M.7
  • 29
    • 0033135845 scopus 로고    scopus 로고
    • Inhibition of Fas receptor (CD95)-induced hepatic caspase activation and apoptosis by acetaminophen in mice
    • Lawson J.A., Fisher M.A., Simmons C.A., Farhood A., and Jaeschke H. Inhibition of Fas receptor (CD95)-induced hepatic caspase activation and apoptosis by acetaminophen in mice. Toxicol. Appl. Pharmacol. 156 (1999) 179-186
    • (1999) Toxicol. Appl. Pharmacol. , vol.156 , pp. 179-186
    • Lawson, J.A.1    Fisher, M.A.2    Simmons, C.A.3    Farhood, A.4    Jaeschke, H.5
  • 30
    • 3042738919 scopus 로고    scopus 로고
    • Acetaminophen and the U.S. Acute Liver Failure Study Group: lowering the risks of hepatic failure
    • Lee W.M. Acetaminophen and the U.S. Acute Liver Failure Study Group: lowering the risks of hepatic failure. Hepatology 40 (2004) 6-9
    • (2004) Hepatology , vol.40 , pp. 6-9
    • Lee, W.M.1
  • 35
    • 0021811013 scopus 로고
    • Active-site-directed inhibition of 3-hydroxy-3-metylglutaryl coenzyme A synthase by 3-chloropropionyl coenzyme A
    • Miziorko H.M., and Behnke C.E. Active-site-directed inhibition of 3-hydroxy-3-metylglutaryl coenzyme A synthase by 3-chloropropionyl coenzyme A. Biochemistry 24 (1985) 3174-3179
    • (1985) Biochemistry , vol.24 , pp. 3174-3179
    • Miziorko, H.M.1    Behnke, C.E.2
  • 36
    • 0025694879 scopus 로고
    • Molecular mechanisms of the hepatotoxicity caused by acetaminophen
    • Nelson S.D. Molecular mechanisms of the hepatotoxicity caused by acetaminophen. Semin. Liver Dis. 10 (1990) 267-278
    • (1990) Semin. Liver Dis. , vol.10 , pp. 267-278
    • Nelson, S.D.1
  • 38
    • 35348978636 scopus 로고    scopus 로고
    • Effects of 4-hydroxynonenal on mitochondrial 3-hydroxy-3-methylglutaryl (HMG-CoA) synthase
    • Patel V.B., Spencer C.H., Young T.A., Lively M.O., and Cunningham C.C. Effects of 4-hydroxynonenal on mitochondrial 3-hydroxy-3-methylglutaryl (HMG-CoA) synthase. Free Radic. Biol. Med. 43 (2007) 1499-1507
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 1499-1507
    • Patel, V.B.1    Spencer, C.H.2    Young, T.A.3    Lively, M.O.4    Cunningham, C.C.5
  • 39
    • 0025295133 scopus 로고
    • Immunochemical quantitation of 3-(cystein-S-yl)acetaminophen protein adducts in subcellular liver fractions following a hepatotoxic dose of acetaminophen
    • Pumford N.R., Roberts D.W., Benson R.W., and Hinson J.A. Immunochemical quantitation of 3-(cystein-S-yl)acetaminophen protein adducts in subcellular liver fractions following a hepatotoxic dose of acetaminophen. Biochem. Pharmacol. 40 (1990) 573-579
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 573-579
    • Pumford, N.R.1    Roberts, D.W.2    Benson, R.W.3    Hinson, J.A.4
  • 40
    • 0032504193 scopus 로고    scopus 로고
    • Identification of the hepatic protein targets of reactive metabolites of acetaminophen in vivo in mice using two-dimensional gel electrophoresis and mass spectrometry
    • Qiu Y., Benet L.Z., and Burlingame A.L. Identification of the hepatic protein targets of reactive metabolites of acetaminophen in vivo in mice using two-dimensional gel electrophoresis and mass spectrometry. J. Biol. Chem. 273 (1998) 17940-17953
    • (1998) J. Biol. Chem. , vol.273 , pp. 17940-17953
    • Qiu, Y.1    Benet, L.Z.2    Burlingame, A.L.3
  • 41
    • 0035697715 scopus 로고    scopus 로고
    • Identification of hepatic protein targets of the reactive metabolites of the non-hepatotoxic regioisomer of acetaminophen, 3′-hydroxyacetanilide, in the mouse in vivo using two-dimensional gel electrophoresis and mass spectrometry
    • Qiu Y., Benet L.Z., and Burlingame A.L. Identification of hepatic protein targets of the reactive metabolites of the non-hepatotoxic regioisomer of acetaminophen, 3′-hydroxyacetanilide, in the mouse in vivo using two-dimensional gel electrophoresis and mass spectrometry. Adv. Exp. Med. Biol. 500 (2001) 663-673
    • (2001) Adv. Exp. Med. Biol. , vol.500 , pp. 663-673
    • Qiu, Y.1    Benet, L.Z.2    Burlingame, A.L.3
  • 42
    • 0024454385 scopus 로고
    • In vitro effects of acetaminophen metabolites and analogs on the respiration of mouse liver mitochondria
    • Ramsay R.R., Rashed M.S., and Nelson S.D. In vitro effects of acetaminophen metabolites and analogs on the respiration of mouse liver mitochondria. Arch. Biochem. Biophys. 273 (1989) 449-457
    • (1989) Arch. Biochem. Biophys. , vol.273 , pp. 449-457
    • Ramsay, R.R.1    Rashed, M.S.2    Nelson, S.D.3
  • 44
    • 0027932251 scopus 로고
    • Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase; expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes
    • Rokosz L.L., Boulton D.A., Butkiewicz E.A., Sanyal G., Cueto M.A., Lachance P.A., and Hermes J.D. Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase; expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes. Arch. Biochem. Biophys. 312 (1994) 1-13
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 1-13
    • Rokosz, L.L.1    Boulton, D.A.2    Butkiewicz, E.A.3    Sanyal, G.4    Cueto, M.A.5    Lachance, P.A.6    Hermes, J.D.7
  • 47
    • 0029069966 scopus 로고
    • The cysteines of catalase HPII of Escherichia coli, including Cys438 which is blocked, do not have a catalytic role
    • Sevinc M.S., Ens W., and Loewen P.C. The cysteines of catalase HPII of Escherichia coli, including Cys438 which is blocked, do not have a catalytic role. Eur. J. Biochem. 230 (1995) 127-132
    • (1995) Eur. J. Biochem. , vol.230 , pp. 127-132
    • Sevinc, M.S.1    Ens, W.2    Loewen, P.C.3
  • 49
    • 0022371112 scopus 로고
    • Acetaminophen hepatotoxicity in vivo is not accompanied by oxidant stress
    • Smith C.V., and Mitchell J.R. Acetaminophen hepatotoxicity in vivo is not accompanied by oxidant stress. Biochem. Biophys. Res. Commun. 133 (1985) 329-336
    • (1985) Biochem. Biophys. Res. Commun. , vol.133 , pp. 329-336
    • Smith, C.V.1    Mitchell, J.R.2
  • 50
    • 0024345539 scopus 로고
    • Subcellular binding and effects on calcium homeostasis produced by acetaminophen and a nonhepatotoxic regioisomer, 3′-hydroxyacetanilide, in mouse liver
    • Tirmenstein M.A., and Nelson S.D. Subcellular binding and effects on calcium homeostasis produced by acetaminophen and a nonhepatotoxic regioisomer, 3′-hydroxyacetanilide, in mouse liver. J. Biol. Chem. 264 (1989) 9814-9819
    • (1989) J. Biol. Chem. , vol.264 , pp. 9814-9819
    • Tirmenstein, M.A.1    Nelson, S.D.2
  • 51
    • 0025250140 scopus 로고
    • Acetaminophen-induced oxidation of protein thiols. Contribution of impaired thiol-metabolizing enzymes and the breakdown of adenine nucleotides
    • Tirmenstein M.A., and Nelson S.D. Acetaminophen-induced oxidation of protein thiols. Contribution of impaired thiol-metabolizing enzymes and the breakdown of adenine nucleotides. J. Biol. Chem. 265 (1990) 3059-3065
    • (1990) J. Biol. Chem. , vol.265 , pp. 3059-3065
    • Tirmenstein, M.A.1    Nelson, S.D.2
  • 52
    • 0028270687 scopus 로고
    • Overexpression of mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase in transgenic mice causes hepatic hyperketogenesis
    • Valera A., Pelegrin M., Asins G., Fillat C., Sabater J., Pujol A., Hegardt F.G., and Bosch F. Overexpression of mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase in transgenic mice causes hepatic hyperketogenesis. J. Biol. Chem. 269 (1994) 3117-3123
    • (1994) J. Biol. Chem. , vol.269 , pp. 3117-3123
    • Valera, A.1    Pelegrin, M.2    Asins, G.3    Fillat, C.4    Sabater, J.5    Pujol, A.6    Hegardt, F.G.7    Bosch, F.8
  • 55
    • 1942455710 scopus 로고    scopus 로고
    • Oxidative stress triggers thiol oxidation in the glyceraldehyde-3-phosphate dehydrogenase of Staphylococcus aureus
    • Weber H., Engelmann S., Becher D., and Hecker M. Oxidative stress triggers thiol oxidation in the glyceraldehyde-3-phosphate dehydrogenase of Staphylococcus aureus. Mol. Microbiol. 52 (2004) 133-140
    • (2004) Mol. Microbiol. , vol.52 , pp. 133-140
    • Weber, H.1    Engelmann, S.2    Becher, D.3    Hecker, M.4


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