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Volumn 54, Issue 1, 2004, Pages 56-59

Entamoeba histolytica alcohol dehydrogenase 2 (EhADH2) as a target for anti-amoebic agents

Author keywords

Alcohol dehydrogenase E; Bifunctional proteins; Cycloalkanols; Eukaryotic parasites; Glycolytic pathways

Indexed keywords

ALCOHOL DEHYDROGENASE; ALDEHYDE DEHYDROGENASE; ANTIAMEBIC AGENT; METHANOL DERIVATIVE;

EID: 3543150722     PISSN: 03057453     EISSN: None     Source Type: Journal    
DOI: 10.1093/jac/dkh280     Document Type: Article
Times cited : (21)

References (25)
  • 1
    • 0002635272 scopus 로고
    • Prevalence of Entamoeba histolytica infection
    • (Ravdin, J. I., Ed.) Wiley Medical, New York, NY, USA
    • Walsh, J. A. (1988). Prevalence of Entamoeba histolytica infection. In Amoebiasis: Human Infection by Entamoeba histolytica (Ravdin, J. I., Ed.), pp. 93-105. Wiley Medical, New York, NY, USA.
    • (1988) Amoebiasis: Human Infection By Entamoeba Histolytica , pp. 93-105
    • Walsh, J.A.1
  • 2
    • 0022684067 scopus 로고
    • Problems in recognition and diagnosis of amoebiasis: Estimation of the global magnitude of morbidity and mortality
    • Walsh, J. A. (1986). Problems in recognition and diagnosis of amoebiasis: estimation of the global magnitude of morbidity and mortality. Reviews in Infectious Diseases 8, 228-38.
    • (1986) Reviews in Infectious Diseases , vol.8 , pp. 228-238
    • Walsh, J.A.1
  • 3
    • 0022589220 scopus 로고
    • Comparing the reduction of nitroimidazoles in bacteria and mammalian tissues and relating it to biological activity
    • Goldman, P., Koch, R. L., Yeung, T. C. et al. (1986). Comparing the reduction of nitroimidazoles in bacteria and mammalian tissues and relating it to biological activity. Biochemical Pharmacology 35, 43-51.
    • (1986) Biochemical Pharmacology , vol.35 , pp. 43-51
    • Goldman, P.1    Koch, R.L.2    Yeung, T.C.3
  • 6
    • 0019498508 scopus 로고
    • A metronidazole metabolite in human urine and its risk
    • Kock, R. L., Beaulieu, B. B., Jr, Chrystal, E. J. T. et al. (1981). A metronidazole metabolite in human urine and its risk. Science 211, 398-400.
    • (1981) Science , vol.211 , pp. 398-400
    • Kock, R.L.1    Beaulieu Jr., B.B.2    Chrystal, E.J.T.3
  • 7
    • 0021729633 scopus 로고
    • Metabolism of Entamoeba histolytica Schaudinn, 1903
    • Reeves, R. E. (1984). Metabolism of Entamoeba histolytica Schaudinn, 1903. Advances in Parasitology 23, 105-42.
    • (1984) Advances in Parasitology , vol.23 , pp. 105-142
    • Reeves, R.E.1
  • 8
    • 0018142363 scopus 로고
    • Pyruvate-to-ethanol pathway in Entamoeba histolytica
    • Lo, H. & Reeves, R. E. (1978). Pyruvate-to-ethanol pathway in Entamoeba histolytica. Biochemical Journal 171, 225-30.
    • (1978) Biochemical Journal , vol.171 , pp. 225-230
    • Lo, H.1    Reeves, R.E.2
  • 9
    • 0028356258 scopus 로고
    • Entamoeba histolytica has an alcohol dehydrogenase homologous to the adhE gene product of Escherichia coli
    • Yang, W., Li, E., Kairong, T. et al. (1994). Entamoeba histolytica has an alcohol dehydrogenase homologous to the adhE gene product of Escherichia coli. Molecular and Biochemical Parasitology 64, 253-60.
    • (1994) Molecular and Biochemical Parasitology , vol.64 , pp. 253-260
    • Yang, W.1    Li, E.2    Kairong, T.3
  • 10
    • 0031032112 scopus 로고    scopus 로고
    • Expression of the alcohol dehydrogenase (ADH) domain of Entamoeba histolytica EhADH2 enzyme
    • Espinosa, A., Wang, L., Li, E. et al. (1997). Expression of the alcohol dehydrogenase (ADH) domain of Entamoeba histolytica EhADH2 enzyme. Archives of Medical Research 28, S78-81.
    • (1997) Archives of Medical Research , vol.28
    • Espinosa, A.1    Wang, L.2    Li, E.3
  • 11
    • 0035827566 scopus 로고    scopus 로고
    • The bifunctional Entamoeba histolytica 2 (EhADH2) protein is necessary for amoebic growth and survival and requires an intact C-terminal domain for both alcohol dehydrogenase and aldehyde dehydrogenase activity
    • Espinosa, A., Yang, L., Zhang, Z. et al. (2001). The bifunctional Entamoeba histolytica 2 (EhADH2) protein is necessary for amoebic growth and survival and requires an intact C-terminal domain for both alcohol dehydrogenase and aldehyde dehydrogenase activity. Journal of Biological Chemistry 276, 20136-43.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 20136-20143
    • Espinosa, A.1    Yang, L.2    Zhang, Z.3
  • 12
    • 0024849185 scopus 로고
    • Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli
    • Goodlove, P. E., Cunningham, P. R., Parker, J. et al. (1989). Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli. Gene 85, 209-14.
    • (1989) Gene , vol.85 , pp. 209-214
    • Goodlove, P.E.1    Cunningham, P.R.2    Parker, J.3
  • 13
    • 0029987452 scopus 로고    scopus 로고
    • Complementation of an Escherichia coli adhE mutant by the Entamoeba histolytica EhADH2 gene provides a method for the identification of new anti-amoebic drugs
    • Yong, T., Li, E., Clark, D. et al. (1996). Complementation of an Escherichia coli adhE mutant by the Entamoeba histolytica EhADH2 gene provides a method for the identification of new anti-amoebic drugs. Proceedings of the National Academy of Sciences, USA 93, 6464-9.
    • (1996) Proceedings of the National Academy of Sciences, USA , vol.93 , pp. 6464-6469
    • Yong, T.1    Li, E.2    Clark, D.3
  • 14
    • 0026662009 scopus 로고
    • Ultrastructure and pyruvate formate-lyase radical quenching property of the multienzymic AdhE protein of Escherichia coli
    • Kessler, D., Herth, W. & Knappe, J. (1992). Ultrastructure and pyruvate formate-lyase radical quenching property of the multienzymic AdhE protein of Escherichia coli. Journal of Biological Chemistry 267, 18073-9.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 18073-18079
    • Kessler, D.1    Herth, W.2    Knappe, J.3
  • 15
    • 0025972739 scopus 로고
    • Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE
    • Kessler, D., Leibrecht, I. & Knappe, J. (1991). Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE FEBS Letters 281, 59-63.
    • (1991) FEBS Letters , vol.281 , pp. 59-63
    • Kessler, D.1    Leibrecht, I.2    Knappe, J.3
  • 16
    • 0028212644 scopus 로고
    • Molecular characterization of microbial alcohol dehydrogenases
    • Reid, M. F. & Fewson, C. A. (1994). Molecular characterization of microbial alcohol dehydrogenases. Critical Reviews in Microbiology 20, 13-56.
    • (1994) Critical Reviews in Microbiology , vol.20 , pp. 13-56
    • Reid, M.F.1    Fewson, C.A.2
  • 17
    • 0032780258 scopus 로고    scopus 로고
    • Why metronidazole is active against both bacteria and parasites
    • Samuelson, J. (1999). Why metronidazole is active against both bacteria and parasites. Antimicrobial Agents and Chemotherapy 43, 1533-41.
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , pp. 1533-1541
    • Samuelson, J.1
  • 18
    • 0030896337 scopus 로고    scopus 로고
    • The site of general anesthesia and cytochrome P450 oxygenases: Similarities defined by straight chain and cyclic alcohols
    • LaBella, F. S., Chen, Q. M., Stein, D. et al. (1997). The site of general anesthesia and cytochrome P450 oxygenases: similarities defined by straight chain and cyclic alcohols. British Journal of Pharmacology 120, 1158-64.
    • (1997) British Journal of Pharmacology , vol.120 , pp. 1158-1164
    • LaBella, F.S.1    Chen, Q.M.2    Stein, D.3
  • 19
    • 0026680589 scopus 로고
    • Alcohol, nitric oxide, and neurotoxicity: Is there a connection? A review
    • Lancaster, F. E. (1992). Alcohol, nitric oxide, and neurotoxicity: is there a connection? A review. Alcohol Clinical & Experimental Research 6, 539-41.
    • (1992) Alcohol Clinical & Experimental Research , vol.6 , pp. 539-541
    • Lancaster, F.E.1
  • 20
    • 0022429988 scopus 로고
    • Mechanism of action of methanol oxidase, reconstitution of methanol oxidase with 5-deazaflavin, and inactivation of methanol oxidase by cyclopropanol
    • Sherry, B. & Abeles, R. H. (1985). Mechanism of action of methanol oxidase, reconstitution of methanol oxidase with 5-deazaflavin, and inactivation of methanol oxidase by cyclopropanol. Biochemistry 24, 2594-605.
    • (1985) Biochemistry , vol.24 , pp. 2594-2605
    • Sherry, B.1    Abeles, R.H.2
  • 21
    • 0023224688 scopus 로고
    • Effects of biogenic aldehydes and aldehyde dehydrogenase inhibitors on rat brain tryptophan hydrolase activity in vitro
    • Nilsson, G. E. & Tottmar, O. (1987). Effects of biogenic aldehydes and aldehyde dehydrogenase inhibitors on rat brain tryptophan hydrolase activity in vitro. Brain Research 409, 374-9.
    • (1987) Brain Research , vol.409 , pp. 374-379
    • Nilsson, G.E.1    Tottmar, O.2
  • 22
    • 0027768957 scopus 로고
    • Cycloalkane-methanols discriminate between volume- and length-dependent loss of activity of alkanols at the torpedo nicotinic acetylcholine receptor
    • Wood, S. C., Hill, W. A. & Miller, K. W. (1993). Cycloalkane-methanols discriminate between volume- and length-dependent loss of activity of alkanols at the torpedo nicotinic acetylcholine receptor. Molecular Pharmacology 44, 1219-26.
    • (1993) Molecular Pharmacology , vol.44 , pp. 1219-1226
    • Wood, S.C.1    Hill, W.A.2    Miller, K.W.3
  • 23
    • 0034900561 scopus 로고    scopus 로고
    • Nonhalogenated alkane anesthetics fail to potentiate agonistic actions on two ligand-gated ion channels
    • Raines, D. E., Claycomb, R. J., Scheller, M. et al. (2001). Nonhalogenated alkane anesthetics fail to potentiate agonistic actions on two ligand-gated ion channels. Anesthesiology 95, 470-7.
    • (2001) Anesthesiology , vol.95 , pp. 470-477
    • Raines, D.E.1    Claycomb, R.J.2    Scheller, M.3
  • 24
    • 0037433938 scopus 로고    scopus 로고
    • Comparative metabolism of methyl isobutyl carbinol and methyl isobutyl ketone in male rats
    • Gingell, R., Regnier, J. F., Wilson, D. M. et al. (2003). Comparative metabolism of methyl isobutyl carbinol and methyl isobutyl ketone in male rats. Toxicology Letters 136, 199-204.
    • (2003) Toxicology Letters , vol.136 , pp. 199-204
    • Gingell, R.1    Regnier, J.F.2    Wilson, D.M.3
  • 25
    • 0033878311 scopus 로고    scopus 로고
    • Role of alcohol dehydrogenase E (ADHE) in the energy metabolism of Giardia lamblia
    • Wang, D. M. (2000). Role of alcohol dehydrogenase E (ADHE) in the energy metabolism of Giardia lamblia. Molecular and Biochemical Parasitology 109, 25-36.
    • (2000) Molecular and Biochemical Parasitology , vol.109 , pp. 25-36
    • Wang, D.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.