메뉴 건너뛰기




Volumn 163, Issue 1, 2009, Pages 19-27

Glyoxalase II does not support methylglyoxal detoxification but serves as a general trypanothione thioesterase in African trypanosomes

Author keywords

Advanced glycation end products; Glutathionylspermidine; Ketoaldehyde; Thioester; Transesterification; Trypanosoma brucei

Indexed keywords

GLYOXAL; HYDROXYACYLGLUTATHIONE HYDROLASE; LACTOYLGLUTATHIONE LYASE; METHYLGLYOXAL; THIOESTER; THIOL ESTER HYDROLASE; TRYPANOTHIONE;

EID: 56549120525     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2008.09.005     Document Type: Article
Times cited : (36)

References (50)
  • 1
    • 4244040278 scopus 로고    scopus 로고
    • Glutathione-dependent detoxification of alpha-oxoaldehydes by the glyoxalase system: involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors
    • Thornalley P.J. Glutathione-dependent detoxification of alpha-oxoaldehydes by the glyoxalase system: involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors. Chem Biol Interact 111-112 (1998) 137-151
    • (1998) Chem Biol Interact , vol.111-112 , pp. 137-151
    • Thornalley, P.J.1
  • 2
    • 0037327816 scopus 로고    scopus 로고
    • Methylglyoxal metabolism and diabetic complications: roles of aldose reductase, glyoxalase-I, betaine aldehyde dehydrogenase and 2-oxoaldehyde dehydrogenase
    • Vander Jagt D.L., and Hunsaker L.A. Methylglyoxal metabolism and diabetic complications: roles of aldose reductase, glyoxalase-I, betaine aldehyde dehydrogenase and 2-oxoaldehyde dehydrogenase. Chem Biol Interact 143-144 (2003) 341-351
    • (2003) Chem Biol Interact , vol.143-144 , pp. 341-351
    • Vander Jagt, D.L.1    Hunsaker, L.A.2
  • 3
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the Kinetoplastida
    • Fairlamb A.H., and Cerami A. Metabolism and functions of trypanothione in the Kinetoplastida. Annu Rev Microbiol 46 (1992) 695-729
    • (1992) Annu Rev Microbiol , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 4
    • 33645856407 scopus 로고    scopus 로고
    • Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia
    • Krauth-Siegel R.L., Bauer H., and Schirmer R.H. Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia. Angew Chem 117 (2005) 698-724
    • (2005) Angew Chem , vol.117 , pp. 698-724
    • Krauth-Siegel, R.L.1    Bauer, H.2    Schirmer, R.H.3
  • 5
    • 2542450775 scopus 로고    scopus 로고
    • Glyoxalase II of African trypanosomes is trypanothione-dependent
    • Irsch T., and Krauth-Siegel R.L. Glyoxalase II of African trypanosomes is trypanothione-dependent. J Biol Chem 279 (2004) 22209-22217
    • (2004) J Biol Chem , vol.279 , pp. 22209-22217
    • Irsch, T.1    Krauth-Siegel, R.L.2
  • 6
    • 33845190312 scopus 로고    scopus 로고
    • Trypanothione-dependent glyoxalase I in Trypanosoma cruzi
    • Greig N., Wyllie S., Vickers T.J., and Fairlamb A.H. Trypanothione-dependent glyoxalase I in Trypanosoma cruzi. Biochem J 400 (2006) 217-223
    • (2006) Biochem J , vol.400 , pp. 217-223
    • Greig, N.1    Wyllie, S.2    Vickers, T.J.3    Fairlamb, A.H.4
  • 7
    • 27144440496 scopus 로고    scopus 로고
    • Glyoxalase I from Leishmania donovani: a potential target for anti-parasite drug
    • Padmanabhan P.K., Mukherjee A., Singh S., et al. Glyoxalase I from Leishmania donovani: a potential target for anti-parasite drug. Biochem Biophys Res Commun 337 (2005) 1237-1248
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 1237-1248
    • Padmanabhan, P.K.1    Mukherjee, A.2    Singh, S.3
  • 8
    • 30044446214 scopus 로고    scopus 로고
    • Characterization of the gene encoding glyoxalase II from Leishmania donovani: a potential target for anti-parasite drugs
    • Padmanabhan P.K., Mukherjee A., and Madhubala R. Characterization of the gene encoding glyoxalase II from Leishmania donovani: a potential target for anti-parasite drugs. Biochem J 393 (2006) 227-234
    • (2006) Biochem J , vol.393 , pp. 227-234
    • Padmanabhan, P.K.1    Mukherjee, A.2    Madhubala, R.3
  • 9
    • 4444278762 scopus 로고    scopus 로고
    • A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major
    • Vickers T.J., Greig N., and Fairlamb A.H. A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major. Proc Natl Acad Sci USA 101 (2004) 13186-13191
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13186-13191
    • Vickers, T.J.1    Greig, N.2    Fairlamb, A.H.3
  • 10
    • 18944383472 scopus 로고    scopus 로고
    • Quantitative assessment of the glyoxalase pathway in Leishmania infantum as a therapeutic target by modelling and computer simulation
    • Sousa Silva M., Ferreira A.E.N., Tomas A.M., Cordeiro C., and Ponces Freire A. Quantitative assessment of the glyoxalase pathway in Leishmania infantum as a therapeutic target by modelling and computer simulation. FEBS J 272 (2005) 2388-2398
    • (2005) FEBS J , vol.272 , pp. 2388-2398
    • Sousa Silva, M.1    Ferreira, A.E.N.2    Tomas, A.M.3    Cordeiro, C.4    Ponces Freire, A.5
  • 11
    • 37849007277 scopus 로고    scopus 로고
    • Catalysis and structural properties of Leishmania infantum glyoxalase II: trypanothione specificity and phylogeny
    • Silva M.S., Barata L., Ferreira A.E., et al. Catalysis and structural properties of Leishmania infantum glyoxalase II: trypanothione specificity and phylogeny. Biochemistry 47 (2008) 195-204
    • (2008) Biochemistry , vol.47 , pp. 195-204
    • Silva, M.S.1    Barata, L.2    Ferreira, A.E.3
  • 12
    • 0033977079 scopus 로고    scopus 로고
    • Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress
    • Krieger S., Schwarz W., Ariyanayagam M.R., Fairlamb A.H., Krauth-Siegel R.L., and Clayton C. Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress. Mol Microbiol 35 (2000) 542-552
    • (2000) Mol Microbiol , vol.35 , pp. 542-552
    • Krieger, S.1    Schwarz, W.2    Ariyanayagam, M.R.3    Fairlamb, A.H.4    Krauth-Siegel, R.L.5    Clayton, C.6
  • 13
    • 0041355353 scopus 로고    scopus 로고
    • RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the bloodstream form of the African trypanosome
    • Wilkinson S.R., Horn D., Prathalingam S.R., and Kelly J.M. RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the bloodstream form of the African trypanosome. J Biol Chem 278 (2003) 31640-31646
    • (2003) J Biol Chem , vol.278 , pp. 31640-31646
    • Wilkinson, S.R.1    Horn, D.2    Prathalingam, S.R.3    Kelly, J.M.4
  • 14
    • 17644393919 scopus 로고    scopus 로고
    • Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei
    • Schlecker T., Schmidt A., Dirdjaja N., Voncken F., Clayton C., and Krauth-Siegel R.L. Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei. J Biol Chem 280 (2005) 14385-14394
    • (2005) J Biol Chem , vol.280 , pp. 14385-14394
    • Schlecker, T.1    Schmidt, A.2    Dirdjaja, N.3    Voncken, F.4    Clayton, C.5    Krauth-Siegel, R.L.6
  • 15
    • 33846963220 scopus 로고    scopus 로고
    • Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defence in African trypanosomes
    • Comini M.A., Krauth-Siegel R.L., and Flohe L. Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defence in African trypanosomes. Biochem J 402 (2007) 43-49
    • (2007) Biochem J , vol.402 , pp. 43-49
    • Comini, M.A.1    Krauth-Siegel, R.L.2    Flohe, L.3
  • 16
    • 0001227791 scopus 로고
    • Carbohydrate metabolism in African trypanosomes, with special reference to the glycosome
    • Morgan M.J. (Ed), Plenum Publishing Corp., New York
    • Fairlamb A.H., and Opperdoes F.R. Carbohydrate metabolism in African trypanosomes, with special reference to the glycosome. In: Morgan M.J. (Ed). Carbohydrate Metabolism in Cultured Cells (1986), Plenum Publishing Corp., New York 183-224
    • (1986) Carbohydrate Metabolism in Cultured Cells , pp. 183-224
    • Fairlamb, A.H.1    Opperdoes, F.R.2
  • 17
    • 0027196331 scopus 로고
    • Formation of methylglyoxal and d-lactate in human red blood cells in vitro
    • Philipps S.A., and Thornalley P.J. Formation of methylglyoxal and d-lactate in human red blood cells in vitro. Biochem Soc Trans 21 (1993) 163S
    • (1993) Biochem Soc Trans , vol.21
    • Philipps, S.A.1    Thornalley, P.J.2
  • 18
    • 24644494767 scopus 로고    scopus 로고
    • Protein glycation in Saccharomyces cerevisiae. Argpyrimidine formation and methylglyoxal catabolism
    • Gomes R.A., Silva M.S., Miranda H.V., Ferreira A.E.N., Cordeiro C.A.A., and Freire A.P. Protein glycation in Saccharomyces cerevisiae. Argpyrimidine formation and methylglyoxal catabolism. FEBS J 272 (2005) 4521-4531
    • (2005) FEBS J , vol.272 , pp. 4521-4531
    • Gomes, R.A.1    Silva, M.S.2    Miranda, H.V.3    Ferreira, A.E.N.4    Cordeiro, C.A.A.5    Freire, A.P.6
  • 19
    • 22244441812 scopus 로고    scopus 로고
    • The genome of the African trypanosome Trypanosoma brucei
    • Berriman M., Ghedin E., Hertz-Fowler C., et al. The genome of the African trypanosome Trypanosoma brucei. Science 309 (2005) 416-422
    • (2005) Science , vol.309 , pp. 416-422
    • Berriman, M.1    Ghedin, E.2    Hertz-Fowler, C.3
  • 20
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman G.L. Tissue sulfhydryl groups. Arch Biochem Biophys 82 (1959) 70-77
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 21
    • 1642457324 scopus 로고    scopus 로고
    • In vitro reactivity of carboxylic acid-CoA thioesters with glutathione
    • Sidenius U., Skonberg C., Olsen J., and Hansen S.H. In vitro reactivity of carboxylic acid-CoA thioesters with glutathione. Chem Res Toxicol 17 (2004) 75-81
    • (2004) Chem Res Toxicol , vol.17 , pp. 75-81
    • Sidenius, U.1    Skonberg, C.2    Olsen, J.3    Hansen, S.H.4
  • 22
    • 0015858087 scopus 로고
    • Preparation and assay of glutathione thiol esters, survey of human liver glutathione thiol esterases
    • Uotila L. Preparation and assay of glutathione thiol esters, survey of human liver glutathione thiol esterases. Biochemistry 12 (1973) 3938-3943
    • (1973) Biochemistry , vol.12 , pp. 3938-3943
    • Uotila, L.1
  • 23
    • 70449154891 scopus 로고
    • The effects of some analogues of glutathione on the glyoxalase system
    • Kermack W.O., and Matheson N.A. The effects of some analogues of glutathione on the glyoxalase system. Biochem J 65 (1957) 48-58
    • (1957) Biochem J , vol.65 , pp. 48-58
    • Kermack, W.O.1    Matheson, N.A.2
  • 24
    • 0343907190 scopus 로고    scopus 로고
    • Vectors for inducible expression of toxic gene products in bloodstream and procyclic Trypanosoma brucei
    • Biebinger S., Wirtz L., Lorenz P., and Clayton C. Vectors for inducible expression of toxic gene products in bloodstream and procyclic Trypanosoma brucei. Mol Biochem Parasitol 85 (1997) 99-112
    • (1997) Mol Biochem Parasitol , vol.85 , pp. 99-112
    • Biebinger, S.1    Wirtz, L.2    Lorenz, P.3    Clayton, C.4
  • 25
    • 11144327213 scopus 로고    scopus 로고
    • A doubly inducible system for RNA interference and rapid RNAi plasmid construction in Trypanosoma brucei
    • Alibu V.P., Storm L., Haile S., Clayton C., and Horn D. A doubly inducible system for RNA interference and rapid RNAi plasmid construction in Trypanosoma brucei. Mol Biochem Parasitol 139 (2004) 75-82
    • (2004) Mol Biochem Parasitol , vol.139 , pp. 75-82
    • Alibu, V.P.1    Storm, L.2    Haile, S.3    Clayton, C.4    Horn, D.5
  • 26
    • 0027997868 scopus 로고
    • Guide RNAs of the recently isolated LEM125 strain of Leishmania tarentolae: an unexpected complexity
    • Thiemann O.H., Maslov D.A., and Simpson L. Guide RNAs of the recently isolated LEM125 strain of Leishmania tarentolae: an unexpected complexity. EMBO J 13 (1994) 5689-5700
    • (1994) EMBO J , vol.13 , pp. 5689-5700
    • Thiemann, O.H.1    Maslov, D.A.2    Simpson, L.3
  • 27
    • 0033928734 scopus 로고    scopus 로고
    • Genetic interference in Trypanosoma brucei by heritable and inducible double-stranded RNA
    • Shi H., Djikeng A., Tomer M., Wirtz E., Tschudi C., and Ullu E. Genetic interference in Trypanosoma brucei by heritable and inducible double-stranded RNA. RNA 6 (2000) 1069-1076
    • (2000) RNA , vol.6 , pp. 1069-1076
    • Shi, H.1    Djikeng, A.2    Tomer, M.3    Wirtz, E.4    Tschudi, C.5    Ullu, E.6
  • 29
    • 33747080843 scopus 로고    scopus 로고
    • Increased dicarbonyl metabolism in endothelial cells in hyperglycemia induces anoikis and impairs angiogenesis by RGD and GFOGER motif modification
    • Dobler D., Ahmed N., Song L., Eboigbodin K.E., and Thornalley P.J. Increased dicarbonyl metabolism in endothelial cells in hyperglycemia induces anoikis and impairs angiogenesis by RGD and GFOGER motif modification. Diabetes 55 (2006) 1961-1969
    • (2006) Diabetes , vol.55 , pp. 1961-1969
    • Dobler, D.1    Ahmed, N.2    Song, L.3    Eboigbodin, K.E.4    Thornalley, P.J.5
  • 30
    • 0242468729 scopus 로고    scopus 로고
    • Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry
    • Thornalley P.J., Battah S., Ahmed N., et al. Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry. Biochem J 375 (2003) 581-592
    • (2003) Biochem J , vol.375 , pp. 581-592
    • Thornalley, P.J.1    Battah, S.2    Ahmed, N.3
  • 31
    • 0025165956 scopus 로고
    • Kinetic analysis of the human erythrocyte glyoxalase system using 1H NMR and a computer model
    • Rae C., Berners-Price S.J., Bulliman B.T., and Kuchel P.W. Kinetic analysis of the human erythrocyte glyoxalase system using 1H NMR and a computer model. Eur J Biochem 193 (1990) 83-90
    • (1990) Eur J Biochem , vol.193 , pp. 83-90
    • Rae, C.1    Berners-Price, S.J.2    Bulliman, B.T.3    Kuchel, P.W.4
  • 32
    • 0024419592 scopus 로고
    • Isolation of glyoxalase II from two different compartments of rat liver mitochondria. Kinetic and immunochemical characterization of the enzymes
    • Talesa V., Uotila L., Koivusalo M., Principato G., Giovannini E., and Rosi G. Isolation of glyoxalase II from two different compartments of rat liver mitochondria. Kinetic and immunochemical characterization of the enzymes. Biochem Biophys Acta 993 (1989) 7-11
    • (1989) Biochem Biophys Acta , vol.993 , pp. 7-11
    • Talesa, V.1    Uotila, L.2    Koivusalo, M.3    Principato, G.4    Giovannini, E.5    Rosi, G.6
  • 33
    • 0015791813 scopus 로고
    • Purification and characterization of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from human liver
    • Uotila L. Purification and characterization of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from human liver. Biochemistry 12 (1973) 3944-3951
    • (1973) Biochemistry , vol.12 , pp. 3944-3951
    • Uotila, L.1
  • 34
    • 15044345677 scopus 로고    scopus 로고
    • Proline metabolism in procyclic Trypanosoma brucei is down-regulated in the presence of glucose
    • Lamour N., Rivière L., Coustou V., Coombs G.H., Barrett M.P., and Bringaud F. Proline metabolism in procyclic Trypanosoma brucei is down-regulated in the presence of glucose. J Biol Chem 280 (2005) 11902-11910
    • (2005) J Biol Chem , vol.280 , pp. 11902-11910
    • Lamour, N.1    Rivière, L.2    Coustou, V.3    Coombs, G.H.4    Barrett, M.P.5    Bringaud, F.6
  • 35
    • 16844370149 scopus 로고    scopus 로고
    • New functions for parts of the Krebs cycle in procyclic Trypanosoma brucei, a cycle not operating as a cycle
    • van Weelden S.W., van Hellemond J.J., Opperdoes F.R., and Tielens A.G. New functions for parts of the Krebs cycle in procyclic Trypanosoma brucei, a cycle not operating as a cycle. J Biol Chem 280 (2005) 12451-12460
    • (2005) J Biol Chem , vol.280 , pp. 12451-12460
    • van Weelden, S.W.1    van Hellemond, J.J.2    Opperdoes, F.R.3    Tielens, A.G.4
  • 36
    • 0024263395 scopus 로고
    • Inhibition of proliferation of human promyelocytic leukaemia HL60 cells by S-d-lactoylglutathione in vitro
    • Thornalley P.J., and Tisdale M.J. Inhibition of proliferation of human promyelocytic leukaemia HL60 cells by S-d-lactoylglutathione in vitro. Leuk Res 12 (1988) 897-904
    • (1988) Leuk Res , vol.12 , pp. 897-904
    • Thornalley, P.J.1    Tisdale, M.J.2
  • 37
    • 0024399730 scopus 로고
    • Methylglyoxal-catabolizing enzymes of Leishmania donovani promastigotes
    • Goshal K., Banerjee A.B., and Ray S. Methylglyoxal-catabolizing enzymes of Leishmania donovani promastigotes. Mol Biochem Parasitol 35 (1989) 21-29
    • (1989) Mol Biochem Parasitol , vol.35 , pp. 21-29
    • Goshal, K.1    Banerjee, A.B.2    Ray, S.3
  • 38
    • 0348049818 scopus 로고    scopus 로고
    • The enzymatic defence against glycation in health, disease and therapeutics: a symposium to examine the concept
    • Thornalley P.J. The enzymatic defence against glycation in health, disease and therapeutics: a symposium to examine the concept. Biochem Soc Trans 31 (2003) 1341-1342
    • (2003) Biochem Soc Trans , vol.31 , pp. 1341-1342
    • Thornalley, P.J.1
  • 39
    • 0023688052 scopus 로고
    • A comparative study of d-lactate, l-lactate and glycerol formation by four species of Leishmania and by Trypanosoma lewisi and Trypanosoma brucei gambiense
    • Darling T.N., Balber A.E., and Blum J.J. A comparative study of d-lactate, l-lactate and glycerol formation by four species of Leishmania and by Trypanosoma lewisi and Trypanosoma brucei gambiense. Mol Biochem Parasitol 30 (1988) 253-257
    • (1988) Mol Biochem Parasitol , vol.30 , pp. 253-257
    • Darling, T.N.1    Balber, A.E.2    Blum, J.J.3
  • 40
    • 0034333236 scopus 로고    scopus 로고
    • Metabolic aspects of glycosomes in trypanosomatidae-new data and views
    • Michels P.A., Hannaert V., and Bringaud F. Metabolic aspects of glycosomes in trypanosomatidae-new data and views. Parasitol Today 16 (2000) 482-489
    • (2000) Parasitol Today , vol.16 , pp. 482-489
    • Michels, P.A.1    Hannaert, V.2    Bringaud, F.3
  • 41
    • 0030761248 scopus 로고    scopus 로고
    • Identification and phenotypic analysis of two glyoxalase II encoding genes from Saccharomyces cerevisiae, GLO2 and GLO4, and intracellular localization of the corresponding proteins
    • Bito A., Haider M., Halder I., and Breitenbach M. Identification and phenotypic analysis of two glyoxalase II encoding genes from Saccharomyces cerevisiae, GLO2 and GLO4, and intracellular localization of the corresponding proteins. J Biol Chem 272 (1997) 21509-21519
    • (1997) J Biol Chem , vol.272 , pp. 21509-21519
    • Bito, A.1    Haider, M.2    Halder, I.3    Breitenbach, M.4
  • 42
    • 0025351070 scopus 로고
    • Relative distribution of glutathione transferase, glyoxalase I and glyoxalase II in helminths
    • Brophy P.M., Crowley P., and Barrett J. Relative distribution of glutathione transferase, glyoxalase I and glyoxalase II in helminths. Int J Parasitol 20 (1989) 259-261
    • (1989) Int J Parasitol , vol.20 , pp. 259-261
    • Brophy, P.M.1    Crowley, P.2    Barrett, J.3
  • 43
    • 0025298551 scopus 로고
    • The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life
    • Thornalley P.J. The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem J 269 (1990) 1-11
    • (1990) Biochem J , vol.269 , pp. 1-11
    • Thornalley, P.J.1
  • 44
    • 0030200936 scopus 로고    scopus 로고
    • Method for determination of free intracellular and extracellular methylglyoxal in animal cells grown in culture
    • Chaplen F.W.R., Fahl W.E., and Cameron D.C. Method for determination of free intracellular and extracellular methylglyoxal in animal cells grown in culture. Anal Biochem 238 (1996) 171-178
    • (1996) Anal Biochem , vol.238 , pp. 171-178
    • Chaplen, F.W.R.1    Fahl, W.E.2    Cameron, D.C.3
  • 45
    • 0036704798 scopus 로고    scopus 로고
    • Accumulation of a GPI-anchored protein at the cell surface requires sorting at multiple intracellular levels
    • Grünfelder C.G., Engstler M., Weise F., et al. Accumulation of a GPI-anchored protein at the cell surface requires sorting at multiple intracellular levels. Traffic 3 (2002) 547-559
    • (2002) Traffic , vol.3 , pp. 547-559
    • Grünfelder, C.G.1    Engstler, M.2    Weise, F.3
  • 46
    • 4544289321 scopus 로고    scopus 로고
    • Dual action of antimonial drugs on thiol redox metabolism in the human pathogen Leishmania donovani
    • Wyllie S., Cunningham M.L., and Fairlamb A.H. Dual action of antimonial drugs on thiol redox metabolism in the human pathogen Leishmania donovani. J Biol Chem 279 (2004) 39925-39932
    • (2004) J Biol Chem , vol.279 , pp. 39925-39932
    • Wyllie, S.1    Cunningham, M.L.2    Fairlamb, A.H.3
  • 47
    • 17744390197 scopus 로고    scopus 로고
    • Aldosterone makes human endothelium stiff and vulnerable
    • Oberleithner H. Aldosterone makes human endothelium stiff and vulnerable. Kidney Int 67 (2005) 1680-1682
    • (2005) Kidney Int , vol.67 , pp. 1680-1682
    • Oberleithner, H.1
  • 48
    • 0036899862 scopus 로고    scopus 로고
    • Genomic scale mutant hunt identifies cell size homeostasis genes in S. cerevisiae
    • Zhang J., Schneider C., Ottmers L., et al. Genomic scale mutant hunt identifies cell size homeostasis genes in S. cerevisiae. Curr Biol 12 (2005) 1992-2001
    • (2005) Curr Biol , vol.12 , pp. 1992-2001
    • Zhang, J.1    Schneider, C.2    Ottmers, L.3
  • 49
    • 0033486132 scopus 로고    scopus 로고
    • Heterologous expression, purification, and kinetic comparison of the cytoplasmic and mitochondrial glyoxalase II enzymes, Glo2p and Glo4p, from Saccharomyces cerevisiae
    • Bito A., Haider M., Briza P., Strasser P., and Breitenbach M. Heterologous expression, purification, and kinetic comparison of the cytoplasmic and mitochondrial glyoxalase II enzymes, Glo2p and Glo4p, from Saccharomyces cerevisiae. Protein Exp Purif 17 (1999) 456-464
    • (1999) Protein Exp Purif , vol.17 , pp. 456-464
    • Bito, A.1    Haider, M.2    Briza, P.3    Strasser, P.4    Breitenbach, M.5
  • 50
    • 28844503390 scopus 로고    scopus 로고
    • Structural studies on a mitochondrial glyoxalase II
    • Marasinghe G.P.K., Sander I.M., Bennett B., et al. Structural studies on a mitochondrial glyoxalase II. J Biol Chem 280 (2005) 40668-40675
    • (2005) J Biol Chem , vol.280 , pp. 40668-40675
    • Marasinghe, G.P.K.1    Sander, I.M.2    Bennett, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.