메뉴 건너뛰기




Volumn 60, Issue , 2005, Pages 1-99

Sulfur-containing amino acid metabolism in parasitic protozoa

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYSTEINE; GLUTATHIONE; METHIONINE; METHIONINE DERIVATIVE; METHIONINE GAMMA LYASE; POLYAMINE; PROPARGYLGLYCINE; SERINE; SULFUR; TRIFLUOROMETHIONINE; UNCLASSIFIED DRUG;

EID: 26844478710     PISSN: 0065308X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-308X(05)60001-2     Document Type: Review
Times cited : (102)

References (362)
  • 2
    • 0030890811 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase
    • Y. Achouri, M.H. Rider, E.V. Schaftingen, and M. Robbi Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase Biochemical Journal 323 1997 365 370
    • (1997) Biochemical Journal , vol.323 , pp. 365-370
    • Achouri, Y.1    Rider, M.H.2    Schaftingen, E.V.3    Robbi, M.4
  • 3
    • 0033571715 scopus 로고    scopus 로고
    • Role of cysteine in the dietary control of the expression of 3-phosphoglycerate dehydrogenase in rat liver
    • Y. Achouri, M. Robbi, and E. Van Schaftingen Role of cysteine in the dietary control of the expression of 3-phosphoglycerate dehydrogenase in rat liver Biochemical Journal 344 1999 15 21
    • (1999) Biochemical Journal , vol.344 , pp. 15-21
    • Achouri, Y.1    Robbi, M.2    Van Schaftingen, E.3
  • 4
    • 0025831040 scopus 로고
    • The biology of Giardia spp
    • R.D. Adam The biology of Giardia spp Microbiology Reviews 55 1991 706 732
    • (1991) Microbiology Reviews , vol.55 , pp. 706-732
    • Adam, R.D.1
  • 5
    • 0033737481 scopus 로고    scopus 로고
    • Gene organization of a Plasmodium falciparum serine hydroxymethyltransferase and its functional expression in Escherichia coli
    • S. Alfadhli, and P.K. Rathod Gene organization of a Plasmodium falciparum serine hydroxymethyltransferase and its functional expression in Escherichia coli Molecular and Biochemical Parasitology 110 2000 283 291
    • (2000) Molecular and Biochemical Parasitology , vol.110 , pp. 283-291
    • Alfadhli, S.1    Rathod, P.K.2
  • 6
    • 0242721300 scopus 로고    scopus 로고
    • Molecular and structural characterization of NADPH-dependent d-glycerate dehydrogenase from the enteric parasitic protist Entamoeba histolytica
    • V. Ali, Y. Shigeta, and T. Nozaki Molecular and structural characterization of NADPH-dependent d-glycerate dehydrogenase from the enteric parasitic protist Entamoeba histolytica Biochemical Journal 375 2003 729 736
    • (2003) Biochemical Journal , vol.375 , pp. 729-736
    • Ali, V.1    Shigeta, Y.2    Nozaki, T.3
  • 7
    • 1942490139 scopus 로고    scopus 로고
    • An intestinal parasitic protist, Entamoeba histolytica, possesses a non-redundant nitrogen fixation-like system for iron-sulfur cluster assembly under anaerobic conditions
    • V. Ali, Y. Shigeta, U. Tokumoto, Y. Takahashi, and T. Nozaki An intestinal parasitic protist, Entamoeba histolytica, possesses a non-redundant nitrogen fixation-like system for iron-sulfur cluster assembly under anaerobic conditions Journal of Biological Chemistry 279 2004 16863 16874
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 16863-16874
    • Ali, V.1    Shigeta, Y.2    Tokumoto, U.3    Takahashi, Y.4    Nozaki, T.5
  • 8
    • 3042844282 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of d-phosphoglycerate dehydrogenase from Entamoeba histolytica. a unique enteric protozoan parasite that possesses both phosphorylated and nonphosphorylated serine metabolic pathways
    • V. Ali, T. Hashimoto, Y. Shigeta, and T. Nozaki Molecular and biochemical characterization of d-phosphoglycerate dehydrogenase from Entamoeba histolytica. A unique enteric protozoan parasite that possesses both phosphorylated and nonphosphorylated serine metabolic pathways European Journal of Biochemistry 271 2004 2670 2681
    • (2004) European Journal of Biochemistry , vol.271 , pp. 2670-2681
    • Ali, V.1    Hashimoto, T.2    Shigeta, Y.3    Nozaki, T.4
  • 9
    • 0027302694 scopus 로고
    • Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: Tissue-specific gene expression and mRNA levels in hepatopathies
    • L. Alvarez, F. Corrales, A. Martin-Duce, and J.M. Mato Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies Biochemical Journal 293 1993 481 486
    • (1993) Biochemical Journal , vol.293 , pp. 481-486
    • Alvarez, L.1    Corrales, F.2    Martin-Duce, A.3    Mato, J.M.4
  • 10
  • 11
    • 0025954883 scopus 로고
    • Compartmentation of folate-mediated one-carbon metabolism in eukaryotes
    • D.R. Appling Compartmentation of folate-mediated one-carbon metabolism in eukaryotes FASEB Journal 5 1991 2645 2651
    • (1991) FASEB Journal , vol.5 , pp. 2645-2651
    • Appling, D.R.1
  • 14
    • 0041461862 scopus 로고    scopus 로고
    • Bis(glutathionyl)spermine and other novel trypanothione analogues in Trypanosoma cruzi
    • M.R. Ariyanayagam, S.L. Oza, A. Mehlert, and A.H. Fairlamb Bis(glutathionyl)spermine and other novel trypanothione analogues in Trypanosoma cruzi Journal of Biological Chemistry 278 2003 27612 27619
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 27612-27619
    • Ariyanayagam, M.R.1    Oza, S.L.2    Mehlert, A.3    Fairlamb, A.H.4
  • 15
    • 0027263498 scopus 로고
    • The methionine synthesis cycle and salvage of methyltetrahydrofolate from host red cells in the malaria parasite (Plasmodium falciparum)
    • W. Asawamahasakda, and Y. Yuthavong The methionine synthesis cycle and salvage of methyltetrahydrofolate from host red cells in the malaria parasite (Plasmodium falciparum) Parasitology 107 1993 1 10
    • (1993) Parasitology , vol.107 , pp. 1-10
    • Asawamahasakda, W.1    Yuthavong, Y.2
  • 16
    • 0021127290 scopus 로고
    • Polyamine levels and the activity of their biosynthetic enzymes in human erythrocytes infected with the malarial parasite, Plasmodium falciparum
    • Y.G. Assaraf, J. Golenser, D.T. Spira, and U. Bachrach Polyamine levels and the activity of their biosynthetic enzymes in human erythrocytes infected with the malarial parasite, Plasmodium falciparum Biochemical Journal 222 1984 815 819
    • (1984) Biochemical Journal , vol.222 , pp. 815-819
    • Assaraf, Y.G.1    Golenser, J.2    Spira, D.T.3    Bachrach, U.4
  • 17
    • 0027510274 scopus 로고
    • Uptake and metabolism of S-adenosyl-l-methionine by Leishmania mexicana and Leishmania braziliensis promastigotes
    • J.L. Avila, and M.A. Polegre Uptake and metabolism of S-adenosyl-l-methionine by Leishmania mexicana and Leishmania braziliensis promastigotes Molecular and Biochemical Parasitology 58 1993 123 134
    • (1993) Molecular and Biochemical Parasitology , vol.58 , pp. 123-134
    • Avila, J.L.1    Polegre, M.A.2
  • 18
    • 0027182786 scopus 로고
    • Resistance to dl-α-difluoromethylornithine by clinical isolates of Trypanosoma brucei rhodesiense. Role of S-adenosylmethionine
    • C.J. Bacchi, J. Garofalo, M. Ciminelli, D. Rattendi, B. Goldberg, P.P. McCann, and N. Yarlett Resistance to dl-α-difluoromethylornithine by clinical isolates of Trypanosoma brucei rhodesiense. Role of S-adenosylmethionine Biochemical Pharmacology 46 1993 471 481
    • (1993) Biochemical Pharmacology , vol.46 , pp. 471-481
    • Bacchi, C.J.1    Garofalo, J.2    Ciminelli, M.3    Rattendi, D.4    Goldberg, B.5    McCann, P.P.6    Yarlett, N.7
  • 19
    • 0027437962 scopus 로고
    • Effects of antagonists of polyamine metabolism on African trypanosomes
    • C.J. Bacchi, and N. Yarlett Effects of antagonists of polyamine metabolism on African trypanosomes Acta Tropica 54 1993 225 236
    • (1993) Acta Tropica , vol.54 , pp. 225-236
    • Bacchi, C.J.1    Yarlett, N.2
  • 20
    • 0141829789 scopus 로고    scopus 로고
    • Polyamine metabolism as chemotherapeutic target in protozoan parasites
    • C.J. Bacchi, and N. Yarlett Polyamine metabolism as chemotherapeutic target in protozoan parasites Mini Review Medicinal Chemistry 2 2002 553 563
    • (2002) Mini Review Medicinal Chemistry , vol.2 , pp. 553-563
    • Bacchi, C.J.1    Yarlett, N.2
  • 22
    • 0023134509 scopus 로고
    • Effects of the ornithine decarboxylase inhibitors dl-α- difluoromethylornithine and α-monofluoromethyldehydroornithine methyl ester alone and in combination with suramin against Trypanosoma brucei brucei central nervous system models
    • C.J. Bacchi, H.C. Nathan, A.B. Clarkson jr, E.J. Bienen, A.J. Bitonti, P.P. McCann, and A. Sjoerdsma Effects of the ornithine decarboxylase inhibitors dl-α-difluoromethylornithine and α-monofluoromethyldehydroornithine methyl ester alone and in combination with suramin against Trypanosoma brucei brucei central nervous system models American Journal of Tropical Medicine and Hygiene 36 1987 46 52
    • (1987) American Journal of Tropical Medicine and Hygiene , vol.36 , pp. 46-52
    • Bacchi, C.J.1    Nathan, H.C.2    Clarkson Jr., A.B.3    Bienen, E.J.4    Bitonti, A.J.5    McCann, P.P.6    Sjoerdsma, A.7
  • 27
    • 0038109848 scopus 로고    scopus 로고
    • Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of l-serine biosynthesis
    • J.Y. Baek, Y. Jun do, D. Taub, and Y.H. Kim Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of l-serine biosynthesis Biochemical Journal 373 2003 191 200
    • (2003) Biochemical Journal , vol.373 , pp. 191-200
    • Baek, J.Y.1    Jun Do, Y.2    Taub, D.3    Kim, Y.H.4
  • 30
    • 0033372849 scopus 로고    scopus 로고
    • Phosphoserine aminotransferase, the second step-catalyzing enzyme for serine biosynthesis
    • M.J. Basurko, M. Marche, M. Darriet, and A. Cassaigne Phosphoserine aminotransferase, the second step-catalyzing enzyme for serine biosynthesis IUBMB Life 48 1999 525 529
    • (1999) IUBMB Life , vol.48 , pp. 525-529
    • Basurko, M.J.1    Marche, M.2    Darriet, M.3    Cassaigne, A.4
  • 31
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: Ancient structures, still full of surprises
    • H. Beinert Iron-sulfur proteins: ancient structures, still full of surprises Journal of Biological Inorganic Chemistry 5 2000 2 15
    • (2000) Journal of Biological Inorganic Chemistry , vol.5 , pp. 2-15
    • Beinert, H.1
  • 32
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • H. Beinert, R.H. Holm, and E. Munck Iron-sulfur clusters: nature's modular, multipurpose structures Science 277 1997 653 659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 34
    • 0032468851 scopus 로고    scopus 로고
    • Methionine formation from α-ketomethiobutyrate in the trypanosomatid Crithidia fasciculata
    • B.J. Berger, W.W. Dai, and J. Wilson Methionine formation from α-ketomethiobutyrate in the trypanosomatid Crithidia fasciculata FEMS Microbiology Letters 165 1998 305 312
    • (1998) FEMS Microbiology Letters , vol.165 , pp. 305-312
    • Berger, B.J.1    Dai, W.W.2    Wilson, J.3
  • 35
    • 0034932250 scopus 로고    scopus 로고
    • Methionine regeneration and aspartate aminotransferase in parasitic protozoa
    • L.C. Berger, J. Wilson, P. Wood, and B.J. Berger Methionine regeneration and aspartate aminotransferase in parasitic protozoa Journal of Bacteriology 183 2001 4421 4434
    • (2001) Journal of Bacteriology , vol.183 , pp. 4421-4434
    • Berger, L.C.1    Wilson, J.2    Wood, P.3    Berger, B.J.4
  • 36
    • 0037441470 scopus 로고    scopus 로고
    • Comparative properties of a three-dimensional model of Plasmodium falciparum ornithine decarboxylase
    • L. Birkholtz, F. Joubert, A.W. Neitz, and A.I. Louw Comparative properties of a three-dimensional model of Plasmodium falciparum ornithine decarboxylase Proteins 50 2003 464 473
    • (2003) Proteins , vol.50 , pp. 464-473
    • Birkholtz, L.1    Joubert, F.2    Neitz, A.W.3    Louw, A.I.4
  • 37
    • 0942301186 scopus 로고    scopus 로고
    • Parasite-specific inserts in the bifunctional S-adenosylmethionine decarboxylase/ornithine decarboxylase of Plasmodium falciparum modulate catalytic activities and domain interactions
    • L.M. Birkholtz, C. Wrenger, F. Joubert, G.A. Wells, R.D. Walter, and A.I. Louw Parasite-specific inserts in the bifunctional S-adenosylmethionine decarboxylase/ornithine decarboxylase of Plasmodium falciparum modulate catalytic activities and domain interactions Biochemical Journal 377 2004 439 448
    • (2004) Biochemical Journal , vol.377 , pp. 439-448
    • Birkholtz, L.M.1    Wrenger, C.2    Joubert, F.3    Wells, G.A.4    Walter, R.D.5    Louw, A.I.6
  • 38
    • 0022454288 scopus 로고
    • Characterization of Trypanosoma brucei brucei S-adenosyl-l-methionine decarboxylase and its inhibition by Berenil, pentamidine and methylglyoxal-bis(guanylhydrazone)
    • A.J. Bitonti, J.A. Dumont, and P.P. McCann Characterization of Trypanosoma brucei brucei S-adenosyl-l-methionine decarboxylase and its inhibition by Berenil, pentamidine and methylglyoxal-bis(guanylhydrazone) Biochemical Journal 237 1986 685 689
    • (1986) Biochemical Journal , vol.237 , pp. 685-689
    • Bitonti, A.J.1    Dumont, J.A.2    McCann, P.P.3
  • 39
    • 0024286846 scopus 로고
    • Effects of α-difluoromethylornithine on protein synthesis and synthesis of the variant-specific glycoprotein (VSG) in Trypanosoma brucei brucei
    • A.J. Bitonti, D.E. Cross-Doersen, and P.P. McCann Effects of α-difluoromethylornithine on protein synthesis and synthesis of the variant-specific glycoprotein (VSG) in Trypanosoma brucei brucei Biochemical Journal 250 1988 295 298
    • (1988) Biochemical Journal , vol.250 , pp. 295-298
    • Bitonti, A.J.1    Cross-Doersen, D.E.2    McCann, P.P.3
  • 40
    • 0025298557 scopus 로고
    • Antimalarial activity of a 4′,5′-unsaturated 5′-fluoroadenosine mechanism-based inhibitor of S-adenosyl-l-homocysteine hydrolase
    • A.J. Bitonti, R.J. Baumann, E.T. Jarvi, J.R. McCarthy, and P.P. McCann Antimalarial activity of a 4′,5′-unsaturated 5′- fluoroadenosine mechanism-based inhibitor of S-adenosyl-l-homocysteine hydrolase Biochemical Pharmacology 40 1990 601 606
    • (1990) Biochemical Pharmacology , vol.40 , pp. 601-606
    • Bitonti, A.J.1    Baumann, R.J.2    Jarvi, E.T.3    McCarthy, J.R.4    McCann, P.P.5
  • 43
    • 0029036040 scopus 로고
    • Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase
    • J.M. Bollinger jr, D.S. Kwon, G.W. Huisman, R. Kolter, and C.T. Walsh Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase Journal of Biological Chemistry 270 1995 14031 14041
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 14031-14041
    • Bollinger Jr., J.M.1    Kwon, D.S.2    Huisman, G.W.3    Kolter, R.4    Walsh, C.T.5
  • 45
    • 0036668633 scopus 로고    scopus 로고
    • The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations
    • D. Bordo, and P. Bork The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations EMBO Reports 3 2002 741 746
    • (2002) EMBO Reports , vol.3 , pp. 741-746
    • Bordo, D.1    Bork, P.2
  • 46
    • 0015235272 scopus 로고
    • Specificity and some other properties of liver serine sulphydrase: Evidence for its identity with cystathionine β-synthase
    • A.E. Braunstein, E.V. Goryachenkova, E.A. Tolosa, I.H. Willhardt, and L.L. Yefremova Specificity and some other properties of liver serine sulphydrase: evidence for its identity with cystathionine β-synthase Biochimica et Biophysica Acta 242 1971 247 260
    • (1971) Biochimica et Biophysica Acta , vol.242 , pp. 247-260
    • Braunstein, A.E.1    Goryachenkova, E.V.2    Tolosa, E.A.3    Willhardt, I.H.4    Yefremova, L.L.5
  • 49
    • 0028054245 scopus 로고
    • Induction of the iron-containing superoxide dismutase in Entamoeba histolytica by a superoxide anion-generating system or by iron chelation
    • I. Bruchhaus, and E. Tannich Induction of the iron-containing superoxide dismutase in Entamoeba histolytica by a superoxide anion-generating system or by iron chelation Molecular and Biochemical Parasitology 67 1994 281 288
    • (1994) Molecular and Biochemical Parasitology , vol.67 , pp. 281-288
    • Bruchhaus, I.1    Tannich, E.2
  • 50
    • 0027196296 scopus 로고
    • Analysis of the genomic sequence encoding the 29-kDa cysteine-rich protein of Entamoeba histolytica
    • I. Bruchhaus, and E. Tannich Analysis of the genomic sequence encoding the 29-kDa cysteine-rich protein of Entamoeba histolytica Tropical Medicine and Parasitology 44 1993 116 118
    • (1993) Tropical Medicine and Parasitology , vol.44 , pp. 116-118
    • Bruchhaus, I.1    Tannich, E.2
  • 51
    • 0032521604 scopus 로고    scopus 로고
    • Recombinant expression and biochemical characterization of an NADPH:flavin oxidoreductase from Entamoeba histolytica
    • I. Bruchhaus, S. Richter, and E. Tannich Recombinant expression and biochemical characterization of an NADPH:flavin oxidoreductase from Entamoeba histolytica Biochemical Journal 330 1998 1217 1221
    • (1998) Biochemical Journal , vol.330 , pp. 1217-1221
    • Bruchhaus, I.1    Richter, S.2    Tannich, E.3
  • 52
    • 0018601361 scopus 로고
    • Cultivation and in vitro cloning of procyclic culture forms of Trypanosoma brucei in a semi-defined medium
    • R. Brun, and M. Schonenberger Cultivation and in vitro cloning of procyclic culture forms of Trypanosoma brucei in a semi-defined medium Acta Tropica 36 1979 289 292
    • (1979) Acta Tropica , vol.36 , pp. 289-292
    • Brun, R.1    Schonenberger, M.2
  • 56
    • 0026033857 scopus 로고
    • Antitrypanosomal effects of polyamine biosynthesis inhibitors correlate with increases in Trypanosoma brucei brucei S-adenosyl-l-methionine
    • T.L. Byers, T.L. Bush, P.P. McCann, and A.J. Bitonti Antitrypanosomal effects of polyamine biosynthesis inhibitors correlate with increases in Trypanosoma brucei brucei S-adenosyl-l-methionine Biochemical Journal 274 1991 527 533
    • (1991) Biochemical Journal , vol.274 , pp. 527-533
    • Byers, T.L.1    Bush, T.L.2    McCann, P.P.3    Bitonti, A.J.4
  • 57
    • 0024040340 scopus 로고
    • DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH
    • C.R. Byrne, R.S. Monroe, K.A. Ward, and N.M. Kredich DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH Journal of Bacteriology 170 1988 3150 3157
    • (1988) Journal of Bacteriology , vol.170 , pp. 3150-3157
    • Byrne, C.R.1    Monroe, R.S.2    Ward, K.A.3    Kredich, N.M.4
  • 58
    • 0016421339 scopus 로고
    • Biological methylation: Selected aspects
    • G.L. Cantoni Biological methylation: selected aspects Annual Review of Biochemistry 44 1975 435 451
    • (1975) Annual Review of Biochemistry , vol.44 , pp. 435-451
    • Cantoni, G.L.1
  • 59
    • 0035804314 scopus 로고    scopus 로고
    • Terminally alkylated polyamine analogues as chemotherapeutic agents
    • R.A. Casero jr, and P.M. Woster Terminally alkylated polyamine analogues as chemotherapeutic agents Journal of Medicinal Chemistry 44 2001 1 26
    • (2001) Journal of Medicinal Chemistry , vol.44 , pp. 1-26
    • Casero Jr., R.A.1    Woster, P.M.2
  • 60
    • 0034678528 scopus 로고    scopus 로고
    • Intracellular glutathione levels determine cerebellar granule neuron sensitivity to excitotoxic injury by kainic acid
    • M. Ceccon, P. Giusti, L. Facci, G. Borin, M. Imbesi, M. Floreani, and S.D. Skaper Intracellular glutathione levels determine cerebellar granule neuron sensitivity to excitotoxic injury by kainic acid Brain Research 862 2000 83 89
    • (2000) Brain Research , vol.862 , pp. 83-89
    • Ceccon, M.1    Giusti, P.2    Facci, L.3    Borin, G.4    Imbesi, M.5    Floreani, M.6    Skaper, S.D.7
  • 62
    • 0030252899 scopus 로고    scopus 로고
    • Detoxicating enzymes of Entamoeba histolytica and their detoxifying roles
    • J. Chen, X. Huang, Y. Liu, G. Dai, and W. Chen Detoxicating enzymes of Entamoeba histolytica and their detoxifying roles Chinese Medical Journal 109 1996 792 794
    • (1996) Chinese Medical Journal , vol.109 , pp. 792-794
    • Chen, J.1    Huang, X.2    Liu, Y.3    Dai, G.4    Chen, W.5
  • 63
    • 0023814271 scopus 로고
    • Pathway of gluconeogenesis from d- and l-glycerate in rat hepatocytes
    • K.S. Chen, and H.A. Lardy Pathway of gluconeogenesis from d- and l-glycerate in rat hepatocytes Archives of Biochemistry and Biophysics 265 1988 433 440
    • (1988) Archives of Biochemistry and Biophysics , vol.265 , pp. 433-440
    • Chen, K.S.1    Lardy, H.A.2
  • 64
    • 0014470830 scopus 로고
    • The effects of dietary protein on the hepatic enzymes of serine metabolism in the rabbit
    • G.P. Cheung, J.P. Cotropia, and H.J. Sallach The effects of dietary protein on the hepatic enzymes of serine metabolism in the rabbit Archives of Biochemistry and Biophysics 129 1969 672 682
    • (1969) Archives of Biochemistry and Biophysics , vol.129 , pp. 672-682
    • Cheung, G.P.1    Cotropia, J.P.2    Sallach, H.J.3
  • 65
    • 0017401520 scopus 로고
    • Activation of methionine for transmethylation. Purification of the S-adenosylmethionine synthetase of bakers' yeast and its separation into two forms
    • P.K. Chiang, and G.L. Cantoni Activation of methionine for transmethylation. Purification of the S-adenosylmethionine synthetase of bakers' yeast and its separation into two forms Journal of Biological Chemistry 252 1977 4506 4513
    • (1977) Journal of Biological Chemistry , vol.252 , pp. 4506-4513
    • Chiang, P.K.1    Cantoni, G.L.2
  • 68
    • 0038695655 scopus 로고    scopus 로고
    • Primary hyperoxalurias
    • J. Fernandes J.M. Saudubray G. Van der Berghe Springer-Verlag Berlin
    • P. Cochat, and M.O. Rolland Primary hyperoxalurias J. Fernandes J.M. Saudubray G. Van der Berghe Inborn Metabolic Diseases 2002 Springer-Verlag Berlin 446 452
    • (2002) Inborn Metabolic Diseases , pp. 446-452
    • Cochat, P.1    Rolland, M.O.2
  • 70
    • 0034999373 scopus 로고    scopus 로고
    • Trifluoromethionine, a prodrug designed against methionine γ-lyase-containing pathogens, has efficacy in vitro and in vivo against Trichomonas vaginalis
    • G.H. Coombs, and J.C. Mottram Trifluoromethionine, a prodrug designed against methionine γ-lyase-containing pathogens, has efficacy in vitro and in vivo against Trichomonas vaginalis Antimicrobial Agents and Chemotherapy 45 2001 1743 1745
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , pp. 1743-1745
    • Coombs, G.H.1    Mottram, J.C.2
  • 71
    • 0020686355 scopus 로고
    • Biochemistry of sulfur-containing amino acids
    • A.J. Cooper Biochemistry of sulfur-containing amino acids Annual Review of Biochemistry 52 1983 187 222
    • (1983) Annual Review of Biochemistry , vol.52 , pp. 187-222
    • Cooper, A.J.1
  • 72
    • 0015528204 scopus 로고
    • Isolation and properties of highly purified glutamine transaminase
    • J.L. Cooper, and A. Meister Isolation and properties of highly purified glutamine transaminase Biochemistry 11 1972 661 671
    • (1972) Biochemistry , vol.11 , pp. 661-671
    • Cooper, J.L.1    Meister, A.2
  • 73
    • 0027158311 scopus 로고
    • Deletion of an immunodominant Trypanosoma cruzi surface glycoprotein disrupts flagellum-cell adhesion
    • R. Cooper, A.R. de Jesus, and G.A. Cross Deletion of an immunodominant Trypanosoma cruzi surface glycoprotein disrupts flagellum-cell adhesion Journal of Cell Biology 122 1993 149 156
    • (1993) Journal of Cell Biology , vol.122 , pp. 149-156
    • Cooper, R.1    De Jesus, A.R.2    Cross, G.A.3
  • 74
    • 0002774017 scopus 로고    scopus 로고
    • The molecular basis of resistance to the sulfones, sulfonamides, and dihydrofolate reductase inhibitors
    • I.W. Sherman ASM Press Washington, DC
    • A.F. Cowman The molecular basis of resistance to the sulfones, sulfonamides, and dihydrofolate reductase inhibitors I.W. Sherman Malaria Parasite Biology, Pathogenesis, and Protection 1998 ASM Press Washington, DC 317 330
    • (1998) Malaria Parasite Biology, Pathogenesis, and Protection , pp. 317-330
    • Cowman, A.F.1
  • 75
    • 0028292569 scopus 로고
    • Plasmodium falciparum S-adenosylhomocysteine hydrolase. cDNA identification, predicted protein sequence, and expression in Escherichia coli
    • K.A. Creedon, P.K. Rathod, and T.E. Wellems Plasmodium falciparum S-adenosylhomocysteine hydrolase. cDNA identification, predicted protein sequence, and expression in Escherichia coli Journal of Biological Chemistry 269 1994 16364 16370
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 16364-16370
    • Creedon, K.A.1    Rathod, P.K.2    Wellems, T.E.3
  • 76
    • 0031049525 scopus 로고    scopus 로고
    • Combined action of inhibitors of S-adenosylmethionine decarboxylase with an antimalarial drug, chloroquine, on Plasmodium falciparum
    • B. Das, R. Gupta, and R. Madhubala Combined action of inhibitors of S-adenosylmethionine decarboxylase with an antimalarial drug, chloroquine, on Plasmodium falciparum Journal of Eukaryotic Microbiology 44 1997 12 17
    • (1997) Journal of Eukaryotic Microbiology , vol.44 , pp. 12-17
    • Das, B.1    Gupta, R.2    Madhubala, R.3
  • 80
    • 0027527252 scopus 로고
    • A familial/genetic study of plasma serine and glycine concentrations
    • E.J. Devor, and R. Waziri A familial/genetic study of plasma serine and glycine concentrations Biology of Psychiatry 34 1993 221 225
    • (1993) Biology of Psychiatry , vol.34 , pp. 221-225
    • Devor, E.J.1    Waziri, R.2
  • 81
    • 0031662724 scopus 로고    scopus 로고
    • Purification and characterization of l-methionine γ-lyase from Brevibacterium linens BL2
    • B. Dias, and B. Weimer Purification and characterization of l-methionine γ-lyase from Brevibacterium linens BL2 Applied Environmental Microbiology 64 1998 3327 3331
    • (1998) Applied Environmental Microbiology , vol.64 , pp. 3327-3331
    • Dias, B.1    Weimer, B.2
  • 83
    • 0032974143 scopus 로고    scopus 로고
    • The glutathione system of peroxide detoxification is less efficient in neurons than in astroglial cells
    • R. Dringen, L. Kussmaul, J.M. Gutterer, J. Hirrlinger, and B. Hamprecht The glutathione system of peroxide detoxification is less efficient in neurons than in astroglial cells Journal of Neurochemistry 72 1999 2523 2530
    • (1999) Journal of Neurochemistry , vol.72 , pp. 2523-2530
    • Dringen, R.1    Kussmaul, L.2    Gutterer, J.M.3    Hirrlinger, J.4    Hamprecht, B.5
  • 84
    • 26844466518 scopus 로고
    • Preparation and properties of S-adenosyl-l-homocysteine, S-adenosyl-l-homocysteine sulfoxide and S-ribosyl-l-homocysteine
    • J.A. Duerre Preparation and properties of S-adenosyl-l-homocysteine, S-adenosyl-l-homocysteine sulfoxide and S-ribosyl-l-homocysteine Archives of Biochemistry and Biophysics 96 1962 70 76
    • (1962) Archives of Biochemistry and Biophysics , vol.96 , pp. 70-76
    • Duerre, J.A.1
  • 85
    • 0022410467 scopus 로고
    • Cysteine eliminates the feeder cell requirement for cultivation of Trypanosoma brucei bloodstream forms in vitro
    • M. Duszenko, M.A. Ferguson, G.S. Lamont, M.R. Rifkin, and G.A. Cross Cysteine eliminates the feeder cell requirement for cultivation of Trypanosoma brucei bloodstream forms in vitro Journal of Experimental Medicine 162 1985 1256 1263
    • (1985) Journal of Experimental Medicine , vol.162 , pp. 1256-1263
    • Duszenko, M.1    Ferguson, M.A.2    Lamont, G.S.3    Rifkin, M.R.4    Cross, G.A.5
  • 86
    • 0026593156 scopus 로고
    • Cysteine is an essential growth factor for Trypanosoma brucei bloodstream forms
    • M. Duszenko, K. Muhlstadt, and A. Broder Cysteine is an essential growth factor for Trypanosoma brucei bloodstream forms Molecular and Biochemical Parasitology 50 1992 269 273
    • (1992) Molecular and Biochemical Parasitology , vol.50 , pp. 269-273
    • Duszenko, M.1    Muhlstadt, K.2    Broder, A.3
  • 87
  • 88
    • 3943113663 scopus 로고    scopus 로고
    • Pyridoxal phosphate enzymes: Mechanistic, structural, and evolutionary considerations
    • A.C. Eliot, and J.F. Kirsch Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations Annual Review of Biochemistry 73 2004 383 415
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 383-415
    • Eliot, A.C.1    Kirsch, J.F.2
  • 90
    • 0023081007 scopus 로고
    • L-Methionine γ-lyase from Pseudomonas putida and Aeromonas
    • N. Esaki, and K. Soda l-Methionine γ-lyase from Pseudomonas putida and Aeromonas Methods in Enzymology 143 1987 459 465
    • (1987) Methods in Enzymology , vol.143 , pp. 459-465
    • Esaki, N.1    Soda, K.2
  • 92
    • 0024342966 scopus 로고
    • Novel biochemical pathways in parasitic protozoa
    • Fairlamb, A.H. (1989). Novel biochemical pathways in parasitic protozoa. Parasitology 99, supplement, S93-S112.
    • (1989) Parasitology , vol.99 , Issue.SUPPL.
    • Fairlamb, A.H.1
  • 93
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the Kinetoplastida
    • A.H. Fairlamb, and A. Cerami Metabolism and functions of trypanothione in the Kinetoplastida Annual Review of Microbiology 46 1992 695 729
    • (1992) Annual Review of Microbiology , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 94
    • 0001815479 scopus 로고
    • Metabolism of trypanothione and glutathionylspermidine in trypanosomatids
    • (K.P. Chang and D. Snary, eds). Berlin: Springer-Verlag/NATO ASI Series.
    • Fairlamb, A.H. and Henderson, G.B. (1987). Metabolism of trypanothione and glutathionylspermidine in trypanosomatids. In: Host-Parasite Cellular and Molecular Interactions in Protozoal Infections (K.P. Chang and D. Snary, eds). Vol. H11, pp. 29-40. Berlin: Springer-Verlag/NATO ASI Series.
    • (1987) Host-Parasite Cellular and Molecular Interactions in Protozoal Infections , vol.H11 , pp. 29-40
    • Fairlamb, A.H.1    Henderson, G.B.2
  • 95
    • 0002486260 scopus 로고    scopus 로고
    • Polyamine metabolism in trypanosomes
    • G. Hide J.C. Mottram G.H. Coombs P.H. Holmes CAB International Wallingford, UK
    • A.H. Fairlamb, and S.A. LeQuesne Polyamine metabolism in trypanosomes G. Hide J.C. Mottram G.H. Coombs P.H. Holmes Trypanosomiasis and Leishmaniasis: Biology and Control vol. 9 1997 CAB International Wallingford, UK 149 161
    • (1997) Trypanosomiasis and Leishmaniasis: Biology and Control , vol.9 , pp. 149-161
    • Fairlamb, A.H.1    Lequesne, S.A.2
  • 96
    • 0022002912 scopus 로고
    • Trypanothione: A novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids
    • A.H. Fairlamb, P. Blackburn, P. Ulrich, B.T. Chait, and A. Cerami Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids Science 227 1985 1485 1487
    • (1985) Science , vol.227 , pp. 1485-1487
    • Fairlamb, A.H.1    Blackburn, P.2    Ulrich, P.3    Chait, B.T.4    Cerami, A.5
  • 97
    • 0023253710 scopus 로고
    • In vivo effects of difluoromethylornithine on trypanothione and polyamine levels in bloodstream forms of Trypanosoma brucei
    • A.H. Fairlamb, G.B. Henderson, C.J. Bacchi, and A. Cerami In vivo effects of difluoromethylornithine on trypanothione and polyamine levels in bloodstream forms of Trypanosoma brucei Molecular and Biochemical Parasitology 24 1987 185 191
    • (1987) Molecular and Biochemical Parasitology , vol.24 , pp. 185-191
    • Fairlamb, A.H.1    Henderson, G.B.2    Bacchi, C.J.3    Cerami, A.4
  • 99
    • 0014028001 scopus 로고
    • Serine biosynthesis in rat liver. Regulation of enzyme concentration by dietary factors
    • H.J. Fallon, E.J. Hackney, and W.L. Byrne Serine biosynthesis in rat liver. Regulation of enzyme concentration by dietary factors Journal of Biological Chemistry 241 1966 4157 4167
    • (1966) Journal of Biological Chemistry , vol.241 , pp. 4157-4167
    • Fallon, H.J.1    Hackney, E.J.2    Byrne, W.L.3
  • 100
    • 0023774924 scopus 로고
    • Control analysis of mammalian serine biosynthesis. Feedback inhibition on the final step
    • D.A. Fell, and K. Snell Control analysis of mammalian serine biosynthesis. Feedback inhibition on the final step Biochemical Journal 256 1988 97 101
    • (1988) Biochemical Journal , vol.256 , pp. 97-101
    • Fell, D.A.1    Snell, K.2
  • 101
    • 0017157209 scopus 로고
    • Kinetic properties and the effect of substrate analogues on 5′-methylthioadenosine nucleosidase from Escherichia coli
    • A.J. Ferro, A. Barrett, and S.K. Shapiro Kinetic properties and the effect of substrate analogues on 5′-methylthioadenosine nucleosidase from Escherichia coli Biochimica et Biophysica Acta 438 1976 487 494
    • (1976) Biochimica et Biophysica Acta , vol.438 , pp. 487-494
    • Ferro, A.J.1    Barrett, A.2    Shapiro, S.K.3
  • 102
    • 0018166816 scopus 로고
    • 5-Methylthioribose kinase. a new enzyme involved in the formation of methionine from 5-methylthioribose
    • A.J. Ferro, A. Barrett, and S.K. Shapiro 5-Methylthioribose kinase. A new enzyme involved in the formation of methionine from 5-methylthioribose Journal of Biological Chemistry 253 1978 6021 6025
    • (1978) Journal of Biological Chemistry , vol.253 , pp. 6021-6025
    • Ferro, A.J.1    Barrett, A.2    Shapiro, S.K.3
  • 103
    • 0033710968 scopus 로고    scopus 로고
    • Early lateral transfer of genes encoding malic enzyme acetyl-CoA synthetase and alcohol dehydrogenases from anaerobic prokaryotes to Entamoeba histolytica
    • J. Field, B. Rosenthal, and J. Samuelson Early lateral transfer of genes encoding malic enzyme acetyl-CoA synthetase and alcohol dehydrogenases from anaerobic prokaryotes to Entamoeba histolytica Molecular Microbiology 38 2000 446 455
    • (2000) Molecular Microbiology , vol.38 , pp. 446-455
    • Field, J.1    Rosenthal, B.2    Samuelson, J.3
  • 104
    • 0016380187 scopus 로고
    • Methionine metabolism in mammals: The biochemical basis for homocysteinuria
    • J.D. Finkelstein Methionine metabolism in mammals: the biochemical basis for homocysteinuria Metabolism 23 1974 387 398
    • (1974) Metabolism , vol.23 , pp. 387-398
    • Finkelstein, J.D.1
  • 105
    • 0023032002 scopus 로고
    • Methionine metabolism in mammals. Adaptation to methionine excess
    • J.D. Finkelstein, and J.J. Martin Methionine metabolism in mammals. Adaptation to methionine excess Journal of Biological Chemistry 261 1986 1582 1587
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 1582-1587
    • Finkelstein, J.D.1    Martin, J.J.2
  • 106
    • 0015116983 scopus 로고
    • Methionine metabolism in mammals. Regulation of homocysteine methyltransferases in rat tissue
    • J.D. Finkelstein, W. Kyle, and B.J. Harris Methionine metabolism in mammals. Regulation of homocysteine methyltransferases in rat tissue Archives of Biochemistry and Biophysics 146 1971 84 92
    • (1971) Archives of Biochemistry and Biophysics , vol.146 , pp. 84-92
    • Finkelstein, J.D.1    Kyle, W.2    Harris, B.J.3
  • 108
    • 0033230579 scopus 로고    scopus 로고
    • Glutathione and trypanothione in parasitic hydroperoxide metabolism
    • L. Flohe, H.J. Hecht, and P. Steinert Glutathione and trypanothione in parasitic hydroperoxide metabolism Free Radical Biology and Medicine 27 1999 966 984
    • (1999) Free Radical Biology and Medicine , vol.27 , pp. 966-984
    • Flohe, L.1    Hecht, H.J.2    Steinert, P.3
  • 110
    • 0018781349 scopus 로고
    • Studies of ethylene-forming system in rat liver extract
    • P.C. Fu, V. Zic, and K. Ozimy Studies of ethylene-forming system in rat liver extract Biochimica et Biophysica Acta 585 1979 427 434
    • (1979) Biochimica et Biophysica Acta , vol.585 , pp. 427-434
    • Fu, P.C.1    Zic, V.2    Ozimy, K.3
  • 111
    • 0035450912 scopus 로고    scopus 로고
    • The role of serine hydroxymethyltransferase isozymes in one-carbon metabolism in MCF-7 cells as determined by (13)C NMR
    • T.F. Fu, J.P. Rife, and V. Schirch The role of serine hydroxymethyltransferase isozymes in one-carbon metabolism in MCF-7 cells as determined by (13)C NMR Archives of Biochemistry and Biophysics 393 2001 42 50
    • (2001) Archives of Biochemistry and Biophysics , vol.393 , pp. 42-50
    • Fu, T.F.1    Rife, J.P.2    Schirch, V.3
  • 112
    • 0023718385 scopus 로고
    • Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae
    • E.S. Furfine, and R.H. Abeles Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae Journal of Biological Chemistry 263 1988 9598 9606
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 9598-9606
    • Furfine, E.S.1    Abeles, R.H.2
  • 114
    • 0027407222 scopus 로고
    • Toxicity of Bordetella avium β-cystathionase toward MC3T3-E1 osteogenic cells
    • C.R. Gentry-Weeks, J.M. Keith, and J. Thompson Toxicity of Bordetella avium β-cystathionase toward MC3T3-E1 osteogenic cells Journal of Biological Chemistry 268 1993 7298 7314
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 7298-7314
    • Gentry-Weeks, C.R.1    Keith, J.M.2    Thompson, J.3
  • 117
    • 0031983077 scopus 로고    scopus 로고
    • Kinetic analysis and tissue distribution of human d-glycerate dehydrogenase/glyoxylate reductase and its relevance to the diagnosis of primary hyperoxaluria type 2
    • C.F. Giafi, and G. Rumsby Kinetic analysis and tissue distribution of human d-glycerate dehydrogenase/glyoxylate reductase and its relevance to the diagnosis of primary hyperoxaluria type 2 Annals of Clinical Biochemistry 35 1998 104 109
    • (1998) Annals of Clinical Biochemistry , vol.35 , pp. 104-109
    • Giafi, C.F.1    Rumsby, G.2
  • 118
    • 0018948310 scopus 로고
    • Attachment and short-term maintenance of motility and viability of Entamoeba histolytica in a defined medium
    • F.D. Gillin, and L.S. Diamond Attachment and short-term maintenance of motility and viability of Entamoeba histolytica in a defined medium Journal of Protozoology 27 1980 220 225
    • (1980) Journal of Protozoology , vol.27 , pp. 220-225
    • Gillin, F.D.1    Diamond, L.S.2
  • 119
    • 0019253877 scopus 로고
    • Attachment of Entamoeba histolytica to glass in a defined maintenance medium: Specific requirement for cysteine and ascorbic acid
    • F.D. Gillin, and L.S. Diamond Attachment of Entamoeba histolytica to glass in a defined maintenance medium: specific requirement for cysteine and ascorbic acid Journal of Protozoology 27 1980 474 478
    • (1980) Journal of Protozoology , vol.27 , pp. 474-478
    • Gillin, F.D.1    Diamond, L.S.2
  • 120
    • 0019830957 scopus 로고
    • Entamoeba histolytica and Giardia lamblia: Effects of cysteine and oxygen tension on trophozoite attachment to glass and survival in culture media
    • F.D. Gillin, and L.S. Diamond Entamoeba histolytica and Giardia lamblia: effects of cysteine and oxygen tension on trophozoite attachment to glass and survival in culture media Experimental Parasitology 52 1981 9 17
    • (1981) Experimental Parasitology , vol.52 , pp. 9-17
    • Gillin, F.D.1    Diamond, L.S.2
  • 121
    • 0019464089 scopus 로고
    • Entamoeba histolytica and Giardia lamblia: Growth responses to reducing agents
    • F.D. Gillin, and L.S. Diamond Entamoeba histolytica and Giardia lamblia: growth responses to reducing agents Experimental Parasitology 51 1981 382 391
    • (1981) Experimental Parasitology , vol.51 , pp. 382-391
    • Gillin, F.D.1    Diamond, L.S.2
  • 122
    • 0019834327 scopus 로고
    • Inhibition of clonal growth of Giardia lamblia and Entamoeba histolytica by metronidazole, quinacrine, and other antimicrobial agents
    • F.D. Gillin, and L.S. Diamond Inhibition of clonal growth of Giardia lamblia and Entamoeba histolytica by metronidazole, quinacrine, and other antimicrobial agents Journal of Antimicrobial Chemotherapy 8 1981 305 316
    • (1981) Journal of Antimicrobial Chemotherapy , vol.8 , pp. 305-316
    • Gillin, F.D.1    Diamond, L.S.2
  • 123
    • 0020051039 scopus 로고
    • Attachment of the flagellate Giardia lamblia: Role of reducing agents, serum, temperature, and ionic composition
    • F.D. Gillin, and D.S. Reiner Attachment of the flagellate Giardia lamblia: role of reducing agents, serum, temperature, and ionic composition Molecular and Cellular Biology 2 1982 369 377
    • (1982) Molecular and Cellular Biology , vol.2 , pp. 369-377
    • Gillin, F.D.1    Reiner, D.S.2
  • 125
    • 0000527974 scopus 로고
    • Sulfur amino acids of plants: An overview
    • J. Giovanelli Sulfur amino acids of plants: an overview Methods in Enzymology 143 1987 419 426
    • (1987) Methods in Enzymology , vol.143 , pp. 419-426
    • Giovanelli, J.1
  • 126
    • 0030993577 scopus 로고    scopus 로고
    • A unique transporter of S-adenosylmethionine in African trypanosomes
    • B. Goldberg, N. Yarlett, J. Sufrin, D. Lloyd, and C.J. Bacchi A unique transporter of S-adenosylmethionine in African trypanosomes FASEB Journal 11 1997 256 260
    • (1997) FASEB Journal , vol.11 , pp. 256-260
    • Goldberg, B.1    Yarlett, N.2    Sufrin, J.3    Lloyd, D.4    Bacchi, C.J.5
  • 127
    • 0031753347 scopus 로고    scopus 로고
    • Effects of intermediates of methionine metabolism and nucleoside analogs on S-adenosylmethionine transport by Trypanosoma brucei brucei and a drug-resistant Trypanosoma brucei rhodesiense
    • B. Goldberg, D. Rattendi, D. Lloyd, J.R. Sufrin, and C.J. Bacchi Effects of intermediates of methionine metabolism and nucleoside analogs on S-adenosylmethionine transport by Trypanosoma brucei brucei and a drug-resistant Trypanosoma brucei rhodesiense Biochemical Pharmacology 56 1998 95 103
    • (1998) Biochemical Pharmacology , vol.56 , pp. 95-103
    • Goldberg, B.1    Rattendi, D.2    Lloyd, D.3    Sufrin, J.R.4    Bacchi, C.J.5
  • 128
    • 0033117817 scopus 로고    scopus 로고
    • Kinetics of S-adenosylmethionine cellular transport and protein methylation in Trypanosoma brucei brucei and Trypanosoma brucei rhodesiense
    • B. Goldberg, D. Rattendi, D. Lloyd, N. Yarlett, and C.J. Bacchi Kinetics of S-adenosylmethionine cellular transport and protein methylation in Trypanosoma brucei brucei and Trypanosoma brucei rhodesiense Archives of Biochemistry and Biophysics 364 1999 13 18
    • (1999) Archives of Biochemistry and Biophysics , vol.364 , pp. 13-18
    • Goldberg, B.1    Rattendi, D.2    Lloyd, D.3    Yarlett, N.4    Bacchi, C.J.5
  • 129
    • 0034192316 scopus 로고    scopus 로고
    • Kinetics of methionine transport and metabolism by Trypanosoma brucei brucei and Trypanosoma brucei rhodesiense
    • B. Goldberg, D. Rattendi, D. Lloyd, N. Yarlett, and C.J. Bacchi Kinetics of methionine transport and metabolism by Trypanosoma brucei brucei and Trypanosoma brucei rhodesiense Archives of Biochemistry and Biophysics 377 2000 49 57
    • (2000) Archives of Biochemistry and Biophysics , vol.377 , pp. 49-57
    • Goldberg, B.1    Rattendi, D.2    Lloyd, D.3    Yarlett, N.4    Bacchi, C.J.5
  • 130
    • 0026630973 scopus 로고
    • Comparison of cobalamin-independent and cobalamin-dependent methionine synthases from Escherichia coli: Two solutions to the same chemical problem
    • J.C. Gonzalez, R.V. Banerjee, S. Huang, J.S. Sumner, and R.G. Matthews Comparison of cobalamin-independent and cobalamin-dependent methionine synthases from Escherichia coli: two solutions to the same chemical problem Biochemistry 31 1992 6045 6056
    • (1992) Biochemistry , vol.31 , pp. 6045-6056
    • Gonzalez, J.C.1    Banerjee, R.V.2    Huang, S.3    Sumner, J.S.4    Matthews, R.G.5
  • 131
    • 0024718893 scopus 로고
    • Isolation, characterization and sequence analysis of a full-length cDNA clone encoding NADH-dependent hydroxypyruvate reductase from cucumber
    • J.M. Greenler, J.S. Sloan, B.W. Schwartz, and W.M. Becker Isolation, characterization and sequence analysis of a full-length cDNA clone encoding NADH-dependent hydroxypyruvate reductase from cucumber Plant Molecular Biology 13 1989 139 150
    • (1989) Plant Molecular Biology , vol.13 , pp. 139-150
    • Greenler, J.M.1    Sloan, J.S.2    Schwartz, B.W.3    Becker, W.M.4
  • 132
    • 0023068040 scopus 로고
    • Mammalian sulfur amino acid metabolism: An overview
    • O.W. Griffith Mammalian sulfur amino acid metabolism: an overview Methods in Enzymology 143 1987 366 376
    • (1987) Methods in Enzymology , vol.143 , pp. 366-376
    • Griffith, O.W.1
  • 133
    • 0031849275 scopus 로고    scopus 로고
    • Immunonutrition: Role of sulfur amino acids, related amino acids, and polyamines
    • R.F. Grimble, and G.K. Grimble Immunonutrition: role of sulfur amino acids, related amino acids, and polyamines Nutrition 14 1998 605 610
    • (1998) Nutrition , vol.14 , pp. 605-610
    • Grimble, R.F.1    Grimble, G.K.2
  • 134
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein
    • J.L. Guan, J.E. Trevithick, and R.O. Hynes Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein Cell Regulation 2 1991 951 964
    • (1991) Cell Regulation , vol.2 , pp. 951-964
    • Guan, J.L.1    Trevithick, J.E.2    Hynes, R.O.3
  • 135
    • 0022539595 scopus 로고
    • The reactions of the phosphorylated pathway of l-serine biosynthesis: Thermodynamic relationships in rat liver in vivo
    • R.W. Guynn, D.K. Merrill, and K. Lund The reactions of the phosphorylated pathway of l-serine biosynthesis: thermodynamic relationships in rat liver in vivo Archives of Biochemistry and Biophysics 245 1986 204 211
    • (1986) Archives of Biochemistry and Biophysics , vol.245 , pp. 204-211
    • Guynn, R.W.1    Merrill, D.K.2    Lund, K.3
  • 136
    • 0027408857 scopus 로고
    • Branched chain aminotransferase isoenzymes. Purification and characterization of the rat brain isoenzyme
    • T.R. Hall, R. Wallin, G.D. Reinhart, and S.M. Hutson Branched chain aminotransferase isoenzymes. Purification and characterization of the rat brain isoenzyme Journal of Biological Chemistry 268 1993 3092 3098
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 3092-3098
    • Hall, T.R.1    Wallin, R.2    Reinhart, G.D.3    Hutson, S.M.4
  • 138
    • 0027509267 scopus 로고
    • Stable transformation of Trypanosoma cruzi: Inactivation of the PUB12.5 polyubiquitin gene by targeted gene disruption
    • S. Hariharan, J. Ajioka, and J. Swindle Stable transformation of Trypanosoma cruzi: inactivation of the PUB12.5 polyubiquitin gene by targeted gene disruption Molecular and Biochemical Parasitology 57 1993 15 30
    • (1993) Molecular and Biochemical Parasitology , vol.57 , pp. 15-30
    • Hariharan, S.1    Ajioka, J.2    Swindle, J.3
  • 139
    • 0037396384 scopus 로고    scopus 로고
    • Polyamine biosynthetic enzymes as drug targets in parasitic protozoa
    • O. Heby, S.C. Roberts, and B. Ullman Polyamine biosynthetic enzymes as drug targets in parasitic protozoa Biochemical Society Transactions 31 2003 415 419
    • (2003) Biochemical Society Transactions , vol.31 , pp. 415-419
    • Heby, O.1    Roberts, S.C.2    Ullman, B.3
  • 140
    • 0033028593 scopus 로고    scopus 로고
    • Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae
    • J. Heilbronn, J. Wilson, and B.J. Berger Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae Journal of Bacteriology 181 1999 1739 1747
    • (1999) Journal of Bacteriology , vol.181 , pp. 1739-1747
    • Heilbronn, J.1    Wilson, J.2    Berger, B.J.3
  • 141
    • 0028025227 scopus 로고
    • Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana
    • R. Hell, C. Bork, N. Bogdanova, I. Frolov, and R. Hauschild Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana FEBS Letters 351 1994 257 262
    • (1994) FEBS Letters , vol.351 , pp. 257-262
    • Hell, R.1    Bork, C.2    Bogdanova, N.3    Frolov, I.4    Hauschild, R.5
  • 143
    • 0037064008 scopus 로고    scopus 로고
    • Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosynthesis
    • K. Herbig, E.P. Chiang, L.R. Lee, J. Hills, B. Shane, and P.J. Stover Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosynthesis Journal of Biological Chemistry 277 2002 38381 38389
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 38381-38389
    • Herbig, K.1    Chiang, E.P.2    Lee, L.R.3    Hills, J.4    Shane, B.5    Stover, P.J.6
  • 144
    • 1242318563 scopus 로고    scopus 로고
    • Decarboxylases involved in polyamine biosynthesis and their inactivation by nitric oxide
    • R.A. Hillary, and A.E. Pegg Decarboxylases involved in polyamine biosynthesis and their inactivation by nitric oxide Biochimica et Biophysica Acta 1647 2003 161 166
    • (2003) Biochimica et Biophysica Acta , vol.1647 , pp. 161-166
    • Hillary, R.A.1    Pegg, A.E.2
  • 145
    • 0014198212 scopus 로고
    • Studies on phosphoserine aminotransferase of sheep brain
    • H. Hirsch, and D.M. Greenberg Studies on phosphoserine aminotransferase of sheep brain Journal of Biological Chemistry 242 1967 2283 2287
    • (1967) Journal of Biological Chemistry , vol.242 , pp. 2283-2287
    • Hirsch, H.1    Greenberg, D.M.2
  • 146
    • 0035094322 scopus 로고    scopus 로고
    • Molecular biology of the plastidic phosphorylated serine biosynthetic pathway in Arabidopsis thaliana
    • C.L. Ho, and K. Saito Molecular biology of the plastidic phosphorylated serine biosynthetic pathway in Arabidopsis thaliana Amino Acids 20 2001 243 259
    • (2001) Amino Acids , vol.20 , pp. 243-259
    • Ho, C.L.1    Saito, K.2
  • 147
    • 0032213901 scopus 로고    scopus 로고
    • Molecular characterization of plastidic phosphoserine aminotransferase in serine biosynthesis from Arabidopsis
    • C.L. Ho, M. Noji, M. Saito, M. Yamazaki, and K. Saito Molecular characterization of plastidic phosphoserine aminotransferase in serine biosynthesis from Arabidopsis Plant Journal 16 1998 443 452
    • (1998) Plant Journal , vol.16 , pp. 443-452
    • Ho, C.L.1    Noji, M.2    Saito, M.3    Yamazaki, M.4    Saito, K.5
  • 148
    • 0033574431 scopus 로고    scopus 로고
    • Plastidic pathway of serine biosynthesis. Molecular cloning and expression of 3-phosphoserine phosphatase from Arabidopsis thaliana
    • C.L. Ho, M. Noji, and K. Saito Plastidic pathway of serine biosynthesis. Molecular cloning and expression of 3-phosphoserine phosphatase from Arabidopsis thaliana Journal of Biological Chemistry 274 1999 11007 11012
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 11007-11012
    • Ho, C.L.1    Noji, M.2    Saito, K.3
  • 149
    • 0032898091 scopus 로고    scopus 로고
    • Regulation of serine biosynthesis in Arabidopsis. Crucial role of plastidic 3-phosphoglycerate dehydrogenase in non-photosynthetic tissues
    • C.L. Ho, M. Noji, M. Saito, and K. Saito Regulation of serine biosynthesis in Arabidopsis. Crucial role of plastidic 3-phosphoglycerate dehydrogenase in non-photosynthetic tissues Journal of Biological Chemistry 274 1999 397 402
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 397-402
    • Ho, C.L.1    Noji, M.2    Saito, M.3    Saito, K.4
  • 150
    • 0019599669 scopus 로고
    • Microsomal phosphatidylethanolamine methyltransferase: Inhibition by S-adenosylhomocysteine
    • D.R. Hoffman, J.A. Haning, and W.E. Cornatzer Microsomal phosphatidylethanolamine methyltransferase: inhibition by S-adenosylhomocysteine Lipids 16 1981 561 567
    • (1981) Lipids , vol.16 , pp. 561-567
    • Hoffman, D.R.1    Haning, J.A.2    Cornatzer, W.E.3
  • 152
  • 153
    • 0017195534 scopus 로고
    • Purification and characterization of methioninase from Pseudomonas putida
    • S. Ito, T. Nakamura, and Y. Eguchi Purification and characterization of methioninase from Pseudomonas putida Journal of Biochemistry (Tokyo) 79 1976 1263 1272
    • (1976) Journal of Biochemistry (Tokyo) , vol.79 , pp. 1263-1272
    • Ito, S.1    Nakamura, T.2    Eguchi, Y.3
  • 154
    • 0025365841 scopus 로고
    • Purification and characterization of hydroxypyruvate reductase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2
    • Y. Izumi, T. Yoshida, H. Kanzaki, S. Toki, S.S. Miyazaki, and H. Yamada Purification and characterization of hydroxypyruvate reductase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2 European Journal of Biochemistry 190 1990 279 284
    • (1990) European Journal of Biochemistry , vol.190 , pp. 279-284
    • Izumi, Y.1    Yoshida, T.2    Kanzaki, H.3    Toki, S.4    Miyazaki, S.S.5    Yamada, H.6
  • 159
    • 0037368219 scopus 로고    scopus 로고
    • Spermidine metabolism in parasitic protozoa. a comparison to the situation in prokaryotes, viruses, plants and fungi
    • A.E. Kaiser, A.M. Gottwald, C.S. Wiersch, W.A. Maier, and H.M. Seitz Spermidine metabolism in parasitic protozoa. A comparison to the situation in prokaryotes, viruses, plants and fungi Folia Parasitologia (Praha) 50 2003 3 18
    • (2003) Folia Parasitologia (Praha) , vol.50 , pp. 3-18
    • Kaiser, A.E.1    Gottwald, A.M.2    Wiersch, C.S.3    Maier, W.A.4    Seitz, H.M.5
  • 160
    • 0014011385 scopus 로고
    • Cystathionine γ-synthetase of Salmonella. Catalytic properties of a new enzyme in bacterial methionine biosynthesis
    • M.M. Kaplan, and M. Flavin Cystathionine γ-synthetase of
    • (1966) Journal of Biological Chemistry , vol.241 , pp. 4463-4471
    • Kaplan, M.M.1    Flavin, M.2
  • 161
    • 0022400737 scopus 로고
    • Irreversible inhibition of putrescine-stimulated S-adenosyl-l-methionine decarboxylase by Berenil and pentamidine
    • E. Karvonen, L. Kauppinen, T. Partanen, and H. Poso Irreversible inhibition of putrescine-stimulated S-adenosyl-l-methionine decarboxylase by Berenil and pentamidine Biochemical Journal 231 1985 165 169
    • (1985) Biochemical Journal , vol.231 , pp. 165-169
    • Karvonen, E.1    Kauppinen, L.2    Partanen, T.3    Poso, H.4
  • 162
    • 0032998601 scopus 로고    scopus 로고
    • Cloning and kinetic characterization of the Trypanosoma cruzi S-adenosylmethionine decarboxylase
    • L.N. Kinch, J.R. Scott, B. Ullman, and M.A. Phillips Cloning and kinetic characterization of the Trypanosoma cruzi S-adenosylmethionine decarboxylase Molecular and Biochemical Parasitology 101 1999 1 11
    • (1999) Molecular and Biochemical Parasitology , vol.101 , pp. 1-11
    • Kinch, L.N.1    Scott, J.R.2    Ullman, B.3    Phillips, M.A.4
  • 164
    • 0142243323 scopus 로고    scopus 로고
    • Synthesis of carbocyclic and acyclic nucleosides possessing 2-fluoroadenine derivatives and their inhibitory activities against Plasmodium falciparum SAH hydrolase
    • Kitade, Y., Kojima, H., Zulfiqur, F., Yabe, S., Yamagiwa, D., Ito, Y., Nakanishi, M., Ueno, Y., Kim, H.S. and Wataya, Y. (2003). Synthesis of carbocyclic and acyclic nucleosides possessing 2-fluoroadenine derivatives and their inhibitory activities against Plasmodium falciparum SAH hydrolase. Nucleic Acids Research, supplement 3, 5-6.
    • (2003) Nucleic Acids Research , Issue.3 SUPPL. , pp. 5-6
    • Kitade, Y.1    Kojima, H.2    Zulfiqur, F.3    Yabe, S.4    Yamagiwa, D.5    Ito, Y.6    Nakanishi, M.7    Ueno, Y.8    Kim, H.S.9    Wataya, Y.10
  • 166
    • 0028111376 scopus 로고
    • The intracellular amino acid pools of Giardia intestinalis, Trichomonas vaginalis, and Crithidia luciliae
    • L.A. Knodler, M.R. Edwards, and P.J. Schofield The intracellular amino acid pools of Giardia intestinalis, Trichomonas vaginalis, and Crithidia luciliae Experimental Parasitology 79 1994 117 125
    • (1994) Experimental Parasitology , vol.79 , pp. 117-125
    • Knodler, L.A.1    Edwards, M.R.2    Schofield, P.J.3
  • 167
    • 0014541341 scopus 로고
    • Phosphoserine phosphatase distribution in normal and neoplastic rat tissues
    • W.E. Knox, A. Herzfeld, and J. Hudson Phosphoserine phosphatase distribution in normal and neoplastic rat tissues Archives of Biochemistry and Biophysics 132 1969 397 403
    • (1969) Archives of Biochemistry and Biophysics , vol.132 , pp. 397-403
    • Knox, W.E.1    Herzfeld, A.2    Hudson, J.3
  • 169
    • 0041818073 scopus 로고    scopus 로고
    • Synthesis of noraristeromycin analogues possessing SAH hydrolase inhibitory activity for the development of antimalaria agents
    • Kojima, H., Yamaguchi, T., Kozaki, A., Nakanishi, M., Ueno, Y. and Kitade, Y. (2002). Synthesis of noraristeromycin analogues possessing SAH hydrolase inhibitory activity for the development of antimalaria agents. Nucleic Acids Research, supplement 2, 141-142.
    • (2002) Nucleic Acids Research , Issue.2 SUPPL. , pp. 141-142
    • Kojima, H.1    Yamaguchi, T.2    Kozaki, A.3    Nakanishi, M.4    Ueno, Y.5    Kitade, Y.6
  • 170
    • 0027429225 scopus 로고
    • Methionine adenosyltransferase: Structure and function
    • M. Kotb, and A.M. Geller Methionine adenosyltransferase: structure and function Pharmacological Therapy 59 1993 125 143
    • (1993) Pharmacological Therapy , vol.59 , pp. 125-143
    • Kotb, M.1    Geller, A.M.2
  • 171
    • 0021944125 scopus 로고
    • S-adenosylmethionine synthetase from human lymphocytes. Purification and characterization
    • M. Kotb, and N.M. Kredich S-adenosylmethionine synthetase from human lymphocytes. Purification and characterization Journal of Biological Chemistry 260 1985 3923 3930
    • (1985) Journal of Biological Chemistry , vol.260 , pp. 3923-3930
    • Kotb, M.1    Kredich, N.M.2
  • 173
    • 0034534695 scopus 로고    scopus 로고
    • The ornithine decarboxylase domain of the bifunctional ornithine decarboxylase/S-adenosylmethionine decarboxylase of Plasmodium falciparum: Recombinant expression and catalytic properties of two different constructs
    • T. Krause, K. Luersen, C. Wrenger, T.W. Gilberger, S. Muller, and R.D. Walter The ornithine decarboxylase domain of the bifunctional ornithine decarboxylase/S-adenosylmethionine decarboxylase of Plasmodium falciparum: recombinant expression and catalytic properties of two different constructs Biochemical Journal 352 2000 287 292
    • (2000) Biochemical Journal , vol.352 , pp. 287-292
    • Krause, T.1    Luersen, K.2    Wrenger, C.3    Gilberger, T.W.4    Muller, S.5    Walter, R.D.6
  • 174
    • 0037963699 scopus 로고    scopus 로고
    • Parasite-specific trypanothione reductase as a drug target molecule
    • Krauth-Siegel, R.L.and Inhoff, O. (2003). Parasite-specific trypanothione reductase as a drug target molecule. Parasitology Research 90, supplement 2, S77-S85.
    • (2003) Parasitology Research , vol.90 , Issue.2 SUPPL.
    • Krauth-Siegel, R.L.1    Inhoff, O.2
  • 175
    • 0014011576 scopus 로고
    • The enzymic synthesis of l-cysteine in Escherichia coli and Salmonella typhimurium
    • N.M. Kredich, and G.M. Tomkins The enzymic synthesis of l-cysteine in Escherichia coli and Salmonella typhimurium Journal of Biological Chemistry 241 1966 4955 4965
    • (1966) Journal of Biological Chemistry , vol.241 , pp. 4955-4965
    • Kredich, N.M.1    Tomkins, G.M.2
  • 177
    • 0015798572 scopus 로고
    • Isolation and purification of l-methionine-α-deamino-γ- mercaptomethane-lyase (l-methioninase) from Clostridium sporogenes
    • W. Kreis, and C. Hession Isolation and purification of l-methionine-α-deamino-γ-mercaptomethane-lyase (l-methioninase) from Clostridium sporogenes Cancer Research 33 1973 1862 1865
    • (1973) Cancer Research , vol.33 , pp. 1862-1865
    • Kreis, W.1    Hession, C.2
  • 178
    • 0024372119 scopus 로고
    • Characterization of cobalamin-dependent methionine synthase purified from the human malarial parasite, Plasmodium falciparum
    • J. Krungkrai, H.K. Webster, and Y. Yuthavong Characterization of cobalamin-dependent methionine synthase purified from the human malarial parasite, Plasmodium falciparum Parasitology Research 75 1989 512 517
    • (1989) Parasitology Research , vol.75 , pp. 512-517
    • Krungkrai, J.1    Webster, H.K.2    Yuthavong, Y.3
  • 179
    • 0347513216 scopus 로고    scopus 로고
    • Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum
    • M.J. LaGier, J. Tachezy, F. Stejskal, K. Kutisova, and J.S. Keithly Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum Microbiology 149 2003 3519 3530
    • (2003) Microbiology , vol.149 , pp. 3519-3530
    • Lagier, M.J.1    Tachezy, J.2    Stejskal, F.3    Kutisova, K.4    Keithly, J.S.5
  • 180
    • 0030307281 scopus 로고    scopus 로고
    • Exposure of periodontal ligament cells to methyl mercaptan reduces intracellular pH and inhibits cell migration
    • H. Lancero, J. Niu, and P.W. Johnson Exposure of periodontal ligament cells to methyl mercaptan reduces intracellular pH and inhibits cell migration Journal of Dental Research 75 1996 1994 2002
    • (1996) Journal of Dental Research , vol.75 , pp. 1994-2002
    • Lancero, H.1    Niu, J.2    Johnson, P.W.3
  • 181
    • 0005688528 scopus 로고
    • Enzymes related to serine synthesis in spinach chloroplasts
    • C. Larsson, and E. Albertsson Enzymes related to serine synthesis in spinach chloroplasts Physiologia Plantarum 45 1979 7 10
    • (1979) Physiologia Plantarum , vol.45 , pp. 7-10
    • Larsson, C.1    Albertsson, E.2
  • 183
    • 0040784159 scopus 로고    scopus 로고
    • Cloning, expression, and functional characterization of the β regulatory subunit of human methionine adenosyltransferase (MAT II)
    • H.L. LeGros jr, A.B. Halim, A.M. Geller, and M. Kotb Cloning, expression, and functional characterization of the β regulatory subunit of human methionine adenosyltransferase (MAT II) Journal of Biological Chemistry 275 2000 2359 2366
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 2359-2366
    • LeGros Jr., H.L.1    Halim, A.B.2    Geller, A.M.3    Kotb, M.4
  • 186
    • 0025947233 scopus 로고
    • Purification and characterization of methionine γ-lyase from Trichomonas vaginalis
    • B.C. Lockwood, and G.H. Coombs Purification and characterization of methionine γ-lyase from Trichomonas vaginalis Biochemical Journal 279 1991 675 682
    • (1991) Biochemical Journal , vol.279 , pp. 675-682
    • Lockwood, B.C.1    Coombs, G.H.2
  • 188
    • 0028384696 scopus 로고
    • The uptake and metabolism of cysteine by Giardia lamblia trophozoites
    • H.D. Lujan, and T.E. Nash The uptake and metabolism of cysteine by Giardia lamblia trophozoites Journal of Eukaryotic Microbiology 41 1994 169 175
    • (1994) Journal of Eukaryotic Microbiology , vol.41 , pp. 169-175
    • Lujan, H.D.1    Nash, T.E.2
  • 190
    • 0028310414 scopus 로고
    • The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249
    • G.X. Luo, and P.M. Horowitz The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249 Journal of Biological Chemistry 269 1994 8220 8225
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 8220-8225
    • Luo, G.X.1    Horowitz, P.M.2
  • 191
    • 0033020661 scopus 로고    scopus 로고
    • Hsp60 is targeted to a cryptic mitochondrion-derived organelle ('crypton') in the microaerophilic protozoan parasite Entamoeba histolytica
    • Z. Mai, S. Ghosh, M. Frisardi, B. Rosenthal, R. Rogers, and J. Samuelson Hsp60 is targeted to a cryptic mitochondrion-derived organelle ('crypton') in the microaerophilic protozoan parasite Entamoeba histolytica Molecular and Cellular Biology 19 1999 2198 2205
    • (1999) Molecular and Cellular Biology , vol.19 , pp. 2198-2205
    • Mai, Z.1    Ghosh, S.2    Frisardi, M.3    Rosenthal, B.4    Rogers, R.5    Samuelson, J.6
  • 192
    • 0022412459 scopus 로고
    • The metabolism of 5′-methylthioadenosine and 5-methylthioribose 1-phosphate in Saccharomyces cerevisiae
    • K.S. Marchitto, and A.J. Ferro The metabolism of 5′- methylthioadenosine and 5-methylthioribose 1-phosphate in Saccharomyces cerevisiae Journal of General Microbiology 131 1985 2153 2164
    • (1985) Journal of General Microbiology , vol.131 , pp. 2153-2164
    • Marchitto, K.S.1    Ferro, A.J.2
  • 194
    • 0031850228 scopus 로고    scopus 로고
    • Cytosolic β-cyanoalanine synthase activity attributed to cysteine synthases in cocklebur seeds. Purification and characterization of cytosolic cysteine synthases
    • A. Maruyama, K. Ishizawa, T. Takagi, and Y. Esashi Cytosolic β-cyanoalanine synthase activity attributed to cysteine synthases in cocklebur seeds. Purification and characterization of cytosolic cysteine synthases Plant Cell Physiology 39 1998 671 680
    • (1998) Plant Cell Physiology , vol.39 , pp. 671-680
    • Maruyama, A.1    Ishizawa, K.2    Takagi, T.3    Esashi, Y.4
  • 195
    • 0025644673 scopus 로고
    • Mechanisms and consequences of the impaired trans-sulphuration pathway in liver disease: Part I. Biochemical implications
    • Mato, J.M., Corrales, F., Martin-Duce, A., Ortiz, P., Pajares, M.A. and Cabrero, C. (1990). Mechanisms and consequences of the impaired trans-sulphuration pathway in liver disease: Part I. Biochemical implications. Drugs 40, supplement 3, 58-64.
    • (1990) Drugs , vol.40 , Issue.3 SUPPL. , pp. 58-64
    • Mato, J.M.1    Corrales, F.2    Martin-Duce, A.3    Ortiz, P.4    Pajares, M.A.5    Cabrero, C.6
  • 196
    • 0032489551 scopus 로고    scopus 로고
    • The primitive protozoon Trichomonas vaginalis contains two methionine γ-lyase genes that encode members of the γ-family of pyridoxal 5′-phosphate-dependent enzymes
    • A.E. McKie, T. Edlind, J. Walker, J.C. Mottram, and G.H. Coombs The primitive protozoon Trichomonas vaginalis contains two methionine γ-lyase genes that encode members of the γ-family of pyridoxal 5′-phosphate-dependent enzymes Journal of Biological Chemistry 273 1998 5549 5556
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 5549-5556
    • McKie, A.E.1    Edlind, T.2    Walker, J.3    Mottram, J.C.4    Coombs, G.H.5
  • 197
    • 0021842685 scopus 로고
    • The biochemistry and functional morphology of the Entamoeba
    • J. McLaughlin, and S. Aley The biochemistry and functional morphology of the Entamoeba Journal of Protozoology 32 1985 221 240
    • (1985) Journal of Protozoology , vol.32 , pp. 221-240
    • McLaughlin, J.1    Aley, S.2
  • 198
    • 0030458544 scopus 로고    scopus 로고
    • Antioxidant defense mechanisms in parasitic protozoa
    • R.K. Mehlotra Antioxidant defense mechanisms in parasitic protozoa Critical Reviews in Microbiology 22 1996 295 314
    • (1996) Critical Reviews in Microbiology , vol.22 , pp. 295-314
    • Mehlotra, R.K.1
  • 202
    • 0033005334 scopus 로고    scopus 로고
    • Homocysteine and Alzheimer's disease
    • J.W. Miller Homocysteine and Alzheimer's disease Nutrition Review 57 1999 126 129
    • (1999) Nutrition Review , vol.57 , pp. 126-129
    • Miller, J.W.1
  • 203
    • 0024151430 scopus 로고
    • MTA phosphorylase in protozoa: A potential target for chemotherapeutic attack
    • R.L. Miller, and D.P. Toorchen MTA phosphorylase in protozoa: a potential target for chemotherapeutic attack Advances in Experimental Medicine and Biology 250 1988 211 218
    • (1988) Advances in Experimental Medicine and Biology , vol.250 , pp. 211-218
    • Miller, R.L.1    Toorchen, D.P.2
  • 205
    • 0031691447 scopus 로고    scopus 로고
    • Trichomonas vaginalis: Expression and characterisation of recombinant S-adenosylhomocysteinase
    • L. Minotto, G.A. Ko, M.R. Edwards, and A.S. Bagnara Trichomonas vaginalis: expression and characterisation of recombinant S- adenosylhomocysteinase Experimental Parasitology 90 1998 175 180
    • (1998) Experimental Parasitology , vol.90 , pp. 175-180
    • Minotto, L.1    Ko, G.A.2    Edwards, M.R.3    Bagnara, A.S.4
  • 207
    • 0016722112 scopus 로고
    • Labile methyl balances for normal humans on various dietary regimens
    • S.H. Mudd, and J.R. Poole Labile methyl balances for normal humans on various dietary regimens Metabolism 24 1975 721 735
    • (1975) Metabolism , vol.24 , pp. 721-735
    • Mudd, S.H.1    Poole, J.R.2
  • 209
    • 0024151128 scopus 로고
    • Energy metabolism of protozoa without mitochondria
    • M. Muller Energy metabolism of protozoa without mitochondria Annual Review of Microbiology 42 1988 465 488
    • (1988) Annual Review of Microbiology , vol.42 , pp. 465-488
    • Muller, M.1
  • 210
    • 0027057393 scopus 로고
    • Energy metabolism of ancestral eukaryotes: A hypothesis based on the biochemistry of amitochondriate parasitic protists
    • M. Muller Energy metabolism of ancestral eukaryotes: a hypothesis based on the biochemistry of amitochondriate parasitic protists Biosystems 28 1992 33 40
    • (1992) Biosystems , vol.28 , pp. 33-40
    • Muller, M.1
  • 211
    • 0039765384 scopus 로고    scopus 로고
    • In the human malaria parasite Plasmodium falciparum, polyamines are synthesized by a bifunctional ornithine decarboxylase, S-adenosylmethionine decarboxylase
    • S. Muller, A. Da'dara, K. Luersen, C. Wrenger, R. Das Gupta, R. Madhubala, and R.D. Walter In the human malaria parasite Plasmodium falciparum, polyamines are synthesized by a bifunctional ornithine decarboxylase, S-adenosylmethionine decarboxylase Journal of Biological Chemistry 275 2000 8097 8102
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 8097-8102
    • Muller, S.1    Da'Dara, A.2    Luersen, K.3    Wrenger, C.4    Das Gupta, R.5    Madhubala, R.6    Walter, R.D.7
  • 212
    • 0035017334 scopus 로고    scopus 로고
    • Targeting polyamines of parasitic protozoa in chemotherapy
    • S. Muller, G.H. Coombs, and R.D. Walter Targeting polyamines of parasitic protozoa in chemotherapy Trends in Parasitology 17 2001 242 249
    • (2001) Trends in Parasitology , vol.17 , pp. 242-249
    • Muller, S.1    Coombs, G.H.2    Walter, R.D.3
  • 214
    • 0015293175 scopus 로고
    • Transport of S-adenosylmethionine in Saccharomyces cerevisiae
    • J.T. Murphy, and K.D. Spence Transport of S-adenosylmethionine in Saccharomyces cerevisiae Journal of Bacteriology 109 1972 499 504
    • (1972) Journal of Bacteriology , vol.109 , pp. 499-504
    • Murphy, J.T.1    Spence, K.D.2
  • 215
    • 0027367423 scopus 로고
    • Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae
    • R.W. Myers, J.W. Wray, S. Fish, and R.H. Abeles Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae Journal of Biological Chemistry 268 1993 24785 24791
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 24785-24791
    • Myers, R.W.1    Wray, J.W.2    Fish, S.3    Abeles, R.H.4
  • 216
    • 0014198939 scopus 로고
    • Acetylhomoserine. An intermediate in the fungal biosynthesis of methionine
    • S. Nagai, and M. Flavin Acetylhomoserine. An intermediate in the fungal biosynthesis of methionine Journal of Biological Chemistry 242 1967 3884 3895
    • (1967) Journal of Biological Chemistry , vol.242 , pp. 3884-3895
    • Nagai, S.1    Flavin, M.2
  • 217
    • 0021090902 scopus 로고
    • Evidence that thiosulfate assimilation by Salmonella typhimurium is catalyzed by cysteine synthase B
    • T. Nakamura, Y. Kon, H. Iwahashi, and Y. Eguchi Evidence that thiosulfate assimilation by Salmonella typhimurium is catalyzed by cysteine synthase B Journal of Bacteriology 156 1983 656 662
    • (1983) Journal of Bacteriology , vol.156 , pp. 656-662
    • Nakamura, T.1    Kon, Y.2    Iwahashi, H.3    Eguchi, Y.4
  • 218
    • 0035122340 scopus 로고    scopus 로고
    • Purification and properties of recombinant Plasmodium falciparum S-adenosyl-l-homocysteine hydrolase
    • M. Nakanishi, A. Iwata, C. Yatome, and Y. Kitade Purification and properties of recombinant Plasmodium falciparum S-adenosyl-l-homocysteine hydrolase Journal of Biochemistry (Tokyo) 129 2001 101 105
    • (2001) Journal of Biochemistry (Tokyo) , vol.129 , pp. 101-105
    • Nakanishi, M.1    Iwata, A.2    Yatome, C.3    Kitade, Y.4
  • 219
    • 0011390211 scopus 로고    scopus 로고
    • Contents of sulfur amino acids and cystathionine β-synthase, and γ-lyase activities in various tissues from Agkistroden blomhoffi (mamushi)
    • K. Nakayama, S. Awata, J. Zhang, H. Ebinuma, T. Mariyama, and H. Kodama Contents of sulfur amino acids and cystathionine β-synthase, and γ-lyase activities in various tissues from Agkistroden blomhoffi (mamushi) Physiological Chemistry and Physical Medicine NMR 32 2000 21 26
    • (2000) Physiological Chemistry and Physical Medicine NMR , vol.32 , pp. 21-26
    • Nakayama, K.1    Awata, S.2    Zhang, J.3    Ebinuma, H.4    Mariyama, T.5    Kodama, H.6
  • 222
    • 0021469191 scopus 로고
    • Effect of hydrogen sulfide and methyl mercaptan on the permeability of oral mucosa
    • W. Ng, and J. Tonzetich Effect of hydrogen sulfide and methyl mercaptan on the permeability of oral mucosa Journal of Dental Research 63 1984 994 997
    • (1984) Journal of Dental Research , vol.63 , pp. 994-997
    • Ng, W.1    Tonzetich, J.2
  • 223
    • 0036034808 scopus 로고    scopus 로고
    • Transcriptional analysis of genes encoding enzymes of the folate pathway in the human malaria parasite Plasmodium falciparum
    • N. Nirmalan, P. Wang, P.F. Sims, and J.E. Hyde Transcriptional analysis of genes encoding enzymes of the folate pathway in the human malaria parasite Plasmodium falciparum Molecular Microbiology 46 2002 179 190
    • (2002) Molecular Microbiology , vol.46 , pp. 179-190
    • Nirmalan, N.1    Wang, P.2    Sims, P.F.3    Hyde, J.E.4
  • 224
    • 0016365223 scopus 로고
    • Enzymatic synthesis of 3-(3-amino-3-carboxypropyl)uridine in Escherichia coli phenylalanine transfer RNA: Transfer of the 3-amino-acid-3-carboxypropyl group from S-adenosylmethionine
    • S. Nishimura, Y. Taya, Y. Kuchino, and Z. Oashi Enzymatic synthesis of 3-(3-amino-3-carboxypropyl)uridine in Escherichia coli phenylalanine transfer RNA: transfer of the 3-amino-acid-3-carboxypropyl group from S-adenosylmethionine Biochemical and Biophysical Research Communications 57 1974 702 708
    • (1974) Biochemical and Biophysical Research Communications , vol.57 , pp. 702-708
    • Nishimura, S.1    Taya, Y.2    Kuchino, Y.3    Oashi, Z.4
  • 225
    • 0036549786 scopus 로고    scopus 로고
    • Evidence for lateral transfer of genes encoding ferredoxins, nitroreductases, NADH oxidase, and alcohol dehydrogenase 3 from anaerobic prokaryotes to Giardia lamblia and Entamoeba histolytica
    • J.E. Nixon, A. Wang, J. Field, H.G. Morrison, A.G. McArthur, M.L. Sogin, B.J. Loftus, and J. Samuelson Evidence for lateral transfer of genes encoding ferredoxins, nitroreductases, NADH oxidase, and alcohol dehydrogenase 3 from anaerobic prokaryotes to Giardia lamblia and Entamoeba histolytica Eukaryotic Cell 1 2002 181 190
    • (2002) Eukaryotic Cell , vol.1 , pp. 181-190
    • Nixon, J.E.1    Wang, A.2    Field, J.3    Morrison, H.G.4    McArthur, A.G.5    Sogin, M.L.6    Loftus, B.J.7    Samuelson, J.8
  • 226
    • 0000116618 scopus 로고    scopus 로고
    • Manipulation of glutathione and amino acid biosynthesis in the chloroplast
    • G. Noctor, A.C. Arisi, L. Jouanin, and C.H. Foyer Manipulation of glutathione and amino acid biosynthesis in the chloroplast Plant Physiology 118 1998 471 482
    • (1998) Plant Physiology , vol.118 , pp. 471-482
    • Noctor, G.1    Arisi, A.C.2    Jouanin, L.3    Foyer, C.H.4
  • 227
    • 0035989828 scopus 로고    scopus 로고
    • Molecular and biochemical analysis of serine acetyltransferase and cysteine synthase towards sulfur metabolic engineering in plants
    • M. Noji, and K. Saito Molecular and biochemical analysis of serine acetyltransferase and cysteine synthase towards sulfur metabolic engineering in plants Amino Acids 22 2002 231 243
    • (2002) Amino Acids , vol.22 , pp. 231-243
    • Noji, M.1    Saito, K.2
  • 228
    • 0028229630 scopus 로고
    • Molecular cloning of a cysteine synthase cDNA from Citrullus vulgaris (watermelon) by genetic complementation in an E. coli Cys-auxotroph
    • M. Noji, I. Murakoshi, and K. Saito Molecular cloning of a cysteine synthase cDNA from Citrullus vulgaris (watermelon) by genetic complementation in an E. coli Cys-auxotroph Molecular and General Genetics 244 1994 57 66
    • (1994) Molecular and General Genetics , vol.244 , pp. 57-66
    • Noji, M.1    Murakoshi, I.2    Saito, K.3
  • 229
    • 0032483994 scopus 로고    scopus 로고
    • Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana
    • M. Noji, K. Inoue, N. Kimura, A. Gouda, and K. Saito Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana Journal of Biological Chemistry 273 1998 32739 32745
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 32739-32745
    • Noji, M.1    Inoue, K.2    Kimura, N.3    Gouda, A.4    Saito, K.5
  • 230
    • 0032583190 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the genes encoding two isoforms of cysteine synthase in the enteric protozoan parasite Entamoeba histolytica
    • T. Nozaki, T. Asai, S. Kobayashi, F. Ikegami, M. Noji, K. Saito, and T. Takeuchi Molecular cloning and characterization of the genes encoding two isoforms of cysteine synthase in the enteric protozoan parasite Entamoeba histolytica Molecular and Biochemical Parasitology 97 1998 33 44
    • (1998) Molecular and Biochemical Parasitology , vol.97 , pp. 33-44
    • Nozaki, T.1    Asai, T.2    Kobayashi, S.3    Ikegami, F.4    Noji, M.5    Saito, K.6    Takeuchi, T.7
  • 231
    • 0033527657 scopus 로고    scopus 로고
    • Characterization of the gene encoding serine acetyltransferase, a regulated enzyme of cysteine biosynthesis from the protist parasites Entamoeba histolytica and Entamoeba dispar. Regulation and possible function of the cysteine biosynthetic pathway in Entamoeba
    • T. Nozaki, T. Asai, L.B. Sanchez, S. Kobayashi, M. Nakazawa, and T. Takeuchi Characterization of the gene encoding serine acetyltransferase, a regulated enzyme of cysteine biosynthesis from the protist parasites Entamoeba histolytica and Entamoeba dispar. Regulation and possible function of the cysteine biosynthetic pathway in Entamoeba Journal of Biological Chemistry 274 1999 32445 32452
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 32445-32452
    • Nozaki, T.1    Asai, T.2    Sanchez, L.B.3    Kobayashi, S.4    Nakazawa, M.5    Takeuchi, T.6
  • 233
    • 0035794209 scopus 로고    scopus 로고
    • Characterization of transsulfuration and cysteine biosynthetic pathways in the protozoan hemoflagellate, Trypanosoma cruzi. Isolation and molecular characterization of cystathionine β-synthase and serine acetyltransferase from Trypanosoma
    • T. Nozaki, Y. Shigeta, Y. Saito-Nakano, M. Imada, and W.D. Kruger Characterization of transsulfuration and cysteine biosynthetic pathways in the protozoan hemoflagellate, Trypanosoma cruzi. Isolation and molecular characterization of cystathionine β-synthase and serine acetyltransferase from Trypanosoma Journal of Biological Chemistry 276 2001 6516 6523
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 6516-6523
    • Nozaki, T.1    Shigeta, Y.2    Saito-Nakano, Y.3    Imada, M.4    Kruger, W.D.5
  • 234
    • 0028700721 scopus 로고
    • Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin
    • N. Ogasawara, S. Nakai, and H. Yoshikawa Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin DNA Research 1 1994 1 14
    • (1994) DNA Research , vol.1 , pp. 1-14
    • Ogasawara, N.1    Nakai, S.2    Yoshikawa, H.3
  • 235
    • 0034719118 scopus 로고    scopus 로고
    • Characterization of the NifU and NifS Fe-S cluster formation proteins essential for viability in Helicobacter pylori
    • J.W. Olson, J.N. Agar, M.K. Johnson, and R.J. Maier Characterization of the NifU and NifS Fe-S cluster formation proteins essential for viability in Helicobacter pylori Biochemistry 39 2000 16213 16219
    • (2000) Biochemistry , vol.39 , pp. 16213-16219
    • Olson, J.W.1    Agar, J.N.2    Johnson, M.K.3    Maier, R.J.4
  • 238
    • 0023644783 scopus 로고
    • DNA sequences of the cysB regions of Salmonella typhimurium and Escherichia coli
    • J. Ostrowski, G. Jagura-Burdzy, and N.M. Kredich DNA sequences of the cysB regions of Salmonella typhimurium and Escherichia coli Journal of Biological Chemistry 262 1987 5999 6005
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 5999-6005
    • Ostrowski, J.1    Jagura-Burdzy, G.2    Kredich, N.M.3
  • 239
    • 0026228688 scopus 로고
    • Wound-regulated accumulation of specific transcripts in tomato fruit: Interactions with fruit development, ethylene and light
    • B.L. Parsons, and A.K. Mattoo Wound-regulated accumulation of specific transcripts in tomato fruit: interactions with fruit development, ethylene and light Plant Molecular Biology 17 1991 453 464
    • (1991) Plant Molecular Biology , vol.17 , pp. 453-464
    • Parsons, B.L.1    Mattoo, A.K.2
  • 241
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy
    • A.E. Pegg Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy Cancer Research 48 1988 759 774
    • (1988) Cancer Research , vol.48 , pp. 759-774
    • Pegg, A.E.1
  • 242
    • 0014690197 scopus 로고
    • On the role of S-adenosyl-l-methionine in the biosynthesis of spermidine by rat prostate
    • A.E. Pegg, and H.G. Williams-Ashman On the role of S-adenosyl-l- methionine in the biosynthesis of spermidine by rat prostate Journal of Biological Chemistry 244 1969 682 693
    • (1969) Journal of Biological Chemistry , vol.244 , pp. 682-693
    • Pegg, A.E.1    Williams-Ashman, H.G.2
  • 243
    • 0018862647 scopus 로고
    • Schizophrenia-like psychosis caused by a metabolic disorder
    • L. Pepplinkhuizen, J. Bruinvels, W. Blom, and P. Moleman Schizophrenia-like psychosis caused by a metabolic disorder Lancet 1 1980 454 456
    • (1980) Lancet , vol.1 , pp. 454-456
    • Pepplinkhuizen, L.1    Bruinvels, J.2    Blom, W.3    Moleman, P.4
  • 245
    • 0032143330 scopus 로고    scopus 로고
    • Trypanosoma cruzi has not lost its S-adenosylmethionine decarboxylase: Characterization of the gene and the encoded enzyme
    • K. Persson, L. Aslund, B. Grahn, J. Hanke, and O. Heby Trypanosoma cruzi has not lost its S-adenosylmethionine decarboxylase: characterization of the gene and the encoded enzyme Biochemical Journal 333 1998 527 537
    • (1998) Biochemical Journal , vol.333 , pp. 527-537
    • Persson, K.1    Aslund, L.2    Grahn, B.3    Hanke, J.4    Heby, O.5
  • 246
    • 0028854807 scopus 로고
    • Sinefungin shares AdoMet-uptake system to enter Leishmania donovani promastigotes
    • M.A. Phelouzat, M. Basselin, F. Lawrence, and M. Robert-Gero Sinefungin shares AdoMet-uptake system to enter Leishmania donovani promastigotes Biochemical Journal 305 1995 133 137
    • (1995) Biochemical Journal , vol.305 , pp. 133-137
    • Phelouzat, M.A.1    Basselin, M.2    Lawrence, F.3    Robert-Gero, M.4
  • 247
    • 0036153388 scopus 로고    scopus 로고
    • Mucosal protection against sulphide: Importance of the enzyme rhodanese
    • R. Picton, M.C. Eggo, G.A. Merrill, M.J. Langman, and S. Singh Mucosal protection against sulphide: importance of the enzyme rhodanese Gut 50 2002 201 205
    • (2002) Gut , vol.50 , pp. 201-205
    • Picton, R.1    Eggo, M.C.2    Merrill, G.A.3    Langman, M.J.4    Singh, S.5
  • 248
    • 0015934089 scopus 로고
    • An Aspergillus nidulans mutant lacking cystathionine β-synthase: Identity of l-serine sulfhydrylase with cystathionine β-synthase and its distinctness from O-acetyl-l-serine sulfhydrylase
    • N. Pieniazek, P.P. Stepien, and A. Paszewski An Aspergillus nidulans mutant lacking cystathionine β-synthase: identity of l-serine sulfhydrylase with cystathionine β-synthase and its distinctness from O-acetyl-l-serine sulfhydrylase Biochimica et Biophysica Acta 297 1973 37 47
    • (1973) Biochimica et Biophysica Acta , vol.297 , pp. 37-47
    • Pieniazek, N.1    Stepien, P.P.2    Paszewski, A.3
  • 249
    • 0017284993 scopus 로고
    • Adenosylmethionine decarboxylase from various organisms: Relation of the putrescine activation of the enzyme to the ability of the organism to synthesize spermine
    • H. Poso, P. Hannonen, J.J. Himberg, and J. Janne Adenosylmethionine decarboxylase from various organisms: relation of the putrescine activation of the enzyme to the ability of the organism to synthesize spermine Biochemical and Biophysical Research Communications 68 1976 227 234
    • (1976) Biochemical and Biophysical Research Communications , vol.68 , pp. 227-234
    • Poso, H.1    Hannonen, P.2    Himberg, J.J.3    Janne, J.4
  • 251
    • 0023240406 scopus 로고
    • Plasmodium falciparum: S-adenosyl-l-methionine decarboxylase
    • S. Rathaur, and R.D. Walter Plasmodium falciparum: S-adenosyl-l- methionine decarboxylase Experimental Parasitology 63 1987 227 232
    • (1987) Experimental Parasitology , vol.63 , pp. 227-232
    • Rathaur, S.1    Walter, R.D.2
  • 252
    • 0026510588 scopus 로고
    • Molecular targets of 5-fluoroorotate in the human malaria parasite, Plasmodium falciparum
    • P.K. Rathod, N.P. Leffers, and R.D. Young Molecular targets of 5-fluoroorotate in the human malaria parasite, Plasmodium falciparum Antimicrobial Agents and Chemotherapy 36 1992 704 711
    • (1992) Antimicrobial Agents and Chemotherapy , vol.36 , pp. 704-711
    • Rathod, P.K.1    Leffers, N.P.2    Young, R.D.3
  • 253
    • 0029278661 scopus 로고
    • Stimulation of enzyme and cytokine production by methyl mercaptan in human gingival fibroblast and monocyte cell cultures
    • L.G. Ratkay, J.D. Waterfield, and J. Tonzetich Stimulation of enzyme and cytokine production by methyl mercaptan in human gingival fibroblast and monocyte cell cultures Archives of Oral Biology 40 1995 337 344
    • (1995) Archives of Oral Biology , vol.40 , pp. 337-344
    • Ratkay, L.G.1    Waterfield, J.D.2    Tonzetich, J.3
  • 256
    • 0021729633 scopus 로고
    • Metabolism of Entamoeba histolytica Schaudinn, 1903
    • R.E. Reeves Metabolism of Entamoeba histolytica Schaudinn, 1903 Advances in Parasitology 23 1984 105 142
    • (1984) Advances in Parasitology , vol.23 , pp. 105-142
    • Reeves, R.E.1
  • 257
    • 0017615796 scopus 로고
    • An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvate synthase and a new acetate thiokinase
    • R.E. Reeves, L.G. Warren, B. Susskind, and H.S. Lo An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvate synthase and a new acetate thiokinase Journal of Biological Chemistry 252 1977 726 731
    • (1977) Journal of Biological Chemistry , vol.252 , pp. 726-731
    • Reeves, R.E.1    Warren, L.G.2    Susskind, B.3    Lo, H.S.4
  • 261
    • 0032530853 scopus 로고    scopus 로고
    • The crystal structure of human cytosolic serine hydroxymethyltransferase: A target for cancer chemotherapy
    • S.B. Renwick, K. Snell, and U. Baumann The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy Structure 6 1998 1105 1116
    • (1998) Structure , vol.6 , pp. 1105-1116
    • Renwick, S.B.1    Snell, K.2    Baumann, U.3
  • 263
    • 0024416959 scopus 로고
    • Methionine recycling as a target for antiprotozoal drug development
    • M.K. Riscoe, A.J. Ferro, and J.H. Fitchen Methionine recycling as a target for antiprotozoal drug development Parasitology Today 5 1989 330 333
    • (1989) Parasitology Today , vol.5 , pp. 330-333
    • Riscoe, M.K.1    Ferro, A.J.2    Fitchen, J.H.3
  • 264
    • 0037155190 scopus 로고    scopus 로고
    • S-adenosylmethionine decarboxylase from Leishmania donovani. Molecular, genetic, and biochemical characterization of null mutants and overproducers
    • S.C. Roberts, J. Scott, J.E. Gasteier, Y. Jiang, B. Brooks, A. Jardim, N.S. Carter, O. Heby, and B. Ullman S-adenosylmethionine decarboxylase from Leishmania donovani. Molecular, genetic, and biochemical characterization of null mutants and overproducers Journal of Biological Chemistry 277 2002 5902 5909
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 5902-5909
    • Roberts, S.C.1    Scott, J.2    Gasteier, J.E.3    Jiang, Y.4    Brooks, B.5    Jardim, A.6    Carter, N.S.7    Heby, O.8    Ullman, B.9
  • 265
    • 0342561564 scopus 로고    scopus 로고
    • Cloning and characterization of the Entamoeba histolytica pyruvate:ferredoxin oxidoreductase gene
    • M.A. Rodriguez, M.E. Hidalgo, T. Sanchez, and E. Orozco Cloning and characterization of the Entamoeba histolytica pyruvate:ferredoxin oxidoreductase gene Molecular and Biochemical Parasitology 78 1996 273 277
    • (1996) Molecular and Biochemical Parasitology , vol.78 , pp. 273-277
    • Rodriguez, M.A.1    Hidalgo, M.E.2    Sanchez, T.3    Orozco, E.4
  • 266
    • 0026699665 scopus 로고
    • Cysteine synthase from Capsicum annuum chromoplasts. Characterization and cDNA cloning of an up-regulated enzyme during fruit development
    • S. Romer, A. d'Harlingue, B. Camara, R. Schantz, and M. Kuntz Cysteine synthase from Capsicum annuum chromoplasts. Characterization and cDNA cloning of an up-regulated enzyme during fruit development Journal of Biological Chemistry 267 1992 17966 17970
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 17966-17970
    • Romer, S.1    D'Harlingue, A.2    Camara, B.3    Schantz, R.4    Kuntz, M.5
  • 268
    • 0014622999 scopus 로고
    • Liver-l-alanine-glyoxylate and l-serine-pyruvate aminotransferase activities: An apparent association with gluconeogenesis
    • E.V. Rowsell, K. Snell, J.A. Carnie, and A.H. Al-Tai Liver-l-alanine- glyoxylate and l-serine-pyruvate aminotransferase activities: an apparent association with gluconeogenesis Biochemical Journal 115 1969 1071 1073
    • (1969) Biochemical Journal , vol.115 , pp. 1071-1073
    • Rowsell, E.V.1    Snell, K.2    Carnie, J.A.3    Al-Tai, A.H.4
  • 269
    • 0024596559 scopus 로고
    • Serine hydroxymethyltransferase from pyrimethamine-sensitive and -resistant strains of Plasmodium chabaudi
    • P. Ruenwongsa, M. Luanvararat, and W.J. O'Sullivan Serine hydroxymethyltransferase from pyrimethamine-sensitive and -resistant strains of Plasmodium chabaudi Molecular and Biochemical Parasitology 33 1989 265 271
    • (1989) Molecular and Biochemical Parasitology , vol.33 , pp. 265-271
    • Ruenwongsa, P.1    Luanvararat, M.2    O'Sullivan, W.J.3
  • 271
    • 0027288172 scopus 로고
    • CDNA cloning and expression of cysteine synthase B localized in chloroplasts of Spinacia oleracea
    • K. Saito, K. Tatsuguchi, I. Murakoshi, and H. Hirano cDNA cloning and expression of cysteine synthase B localized in chloroplasts of Spinacia oleracea FEBS Letters 324 1993 247 252
    • (1993) FEBS Letters , vol.324 , pp. 247-252
    • Saito, K.1    Tatsuguchi, K.2    Murakoshi, I.3    Hirano, H.4
  • 272
    • 0029028281 scopus 로고
    • Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon
    • K. Saito, H. Yokoyama, M. Noji, and I. Murakoshi Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon Journal of Biological Chemistry 270 1995 16321 16326
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 16321-16326
    • Saito, K.1    Yokoyama, H.2    Noji, M.3    Murakoshi, I.4
  • 273
    • 0030932754 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression of cDNA encoding phosphoserine aminotransferase involved in phosphorylated pathway of serine biosynthesis from spinach
    • K. Saito, Y. Takagi, H.C. Ling, H. Takahashi, and M. Noji Molecular cloning, characterization and expression of cDNA encoding phosphoserine aminotransferase involved in phosphorylated pathway of serine biosynthesis from spinach Plant Molecular Biology 33 1997 359 366
    • (1997) Plant Molecular Biology , vol.33 , pp. 359-366
    • Saito, K.1    Takagi, Y.2    Ling, H.C.3    Takahashi, H.4    Noji, M.5
  • 275
    • 0016631221 scopus 로고
    • Regulatory properties of purified 3-phosphoglycerate dehydrogenase from Bacillus subtilis
    • R. Saski, and L.I. Pizer Regulatory properties of purified 3-phosphoglycerate dehydrogenase from Bacillus subtilis European Journal of Biochemistry 51 1975 415 427
    • (1975) European Journal of Biochemistry , vol.51 , pp. 415-427
    • Saski, R.1    Pizer, L.I.2
  • 276
    • 26844546567 scopus 로고
    • The mechanism of utilization of thiomethyladenosine in the biosynthesis of methionine
    • M. Schwartz, and S.K. Shapiro The mechanism of utilization of thiomethyladenosine in the biosynthesis of methionine Journal of Bacteriology 67 1954 98 102
    • (1954) Journal of Bacteriology , vol.67 , pp. 98-102
    • Schwartz, M.1    Shapiro, S.K.2
  • 277
    • 0036710572 scopus 로고    scopus 로고
    • Biogenesis of iron-sulphur clusters in amitochondriate and apicomplexan protists
    • F. Seeber Biogenesis of iron-sulphur clusters in amitochondriate and apicomplexan protists International Journal for Parasitology 32 2002 1207 1217
    • (2002) International Journal for Parasitology , vol.32 , pp. 1207-1217
    • Seeber, F.1
  • 279
    • 0018633747 scopus 로고
    • Biochemistry of Plasmodium (malarial parasites)
    • I.W. Sherman Biochemistry of Plasmodium (malarial parasites) Microbiology Reviews 43 1979 453 495
    • (1979) Microbiology Reviews , vol.43 , pp. 453-495
    • Sherman, I.W.1
  • 280
    • 0037204012 scopus 로고    scopus 로고
    • New neplanocin analogues. 12. Alternative synthesis and antimalarial effect of (6′R)-6′-C-methylneplanocin A, a potent AdoHcy hydrolase inhibitor
    • S. Shuto, N. Minakawa, S. Niizuma, H.S. Kim, Y. Wataya, and A. Matsuda New neplanocin analogues. 12. Alternative synthesis and antimalarial effect of (6′R)-6′-C-methylneplanocin A, a potent AdoHcy hydrolase inhibitor Journal of Medicinal Chemistry 45 2002 748 751
    • (2002) Journal of Medicinal Chemistry , vol.45 , pp. 748-751
    • Shuto, S.1    Minakawa, N.2    Niizuma, S.3    Kim, H.S.4    Wataya, Y.5    Matsuda, A.6
  • 281
    • 0021344078 scopus 로고
    • Chemotherapeutic implications of polyamine biosynthesis inhibition
    • A. Sjoerdsma, and P.J. Schechter Chemotherapeutic implications of polyamine biosynthesis inhibition Clinical Pharmacology and Therapy 35 1984 287 300
    • (1984) Clinical Pharmacology and Therapy , vol.35 , pp. 287-300
    • Sjoerdsma, A.1    Schechter, P.J.2
  • 282
    • 0642302965 scopus 로고    scopus 로고
    • Characterization of S-adenosylmethionine synthetase in Cryptosporidium parvum (Apicomplexa)
    • J. Slapeta, F. Stejskal, and J.S. Keithly Characterization of S-adenosylmethionine synthetase in Cryptosporidium parvum (Apicomplexa) FEMS Microbiology Letters 225 2003 271 277
    • (2003) FEMS Microbiology Letters , vol.225 , pp. 271-277
    • Slapeta, J.1    Stejskal, F.2    Keithly, J.S.3
  • 283
    • 0014343674 scopus 로고
    • Inhibition of 3-phosphoglycerate dehydrogenase by l-serine
    • J.C. Slaughter, and D.D. Davies Inhibition of 3-phosphoglycerate dehydrogenase by l-serine Biochemical Journal 109 1968 749 755
    • (1968) Biochemical Journal , vol.109 , pp. 749-755
    • Slaughter, J.C.1    Davies, D.D.2
  • 286
    • 0021191196 scopus 로고
    • Enzymes of serine metabolism in normal, developing and neoplastic rat tissues
    • K. Snell Enzymes of serine metabolism in normal, developing and neoplastic rat tissues Advances in Enzyme Regulation 22 1984 325 400
    • (1984) Advances in Enzyme Regulation , vol.22 , pp. 325-400
    • Snell, K.1
  • 287
    • 0000124671 scopus 로고
    • The duality of pathways for serine biosynthesis is a fallacy
    • K. Snell The duality of pathways for serine biosynthesis is a fallacy Trends in Biochemical Sciences 11 1986 241 243
    • (1986) Trends in Biochemical Sciences , vol.11 , pp. 241-243
    • Snell, K.1
  • 288
    • 0025069755 scopus 로고
    • Metabolic control analysis of mammalian serine metabolism
    • K. Snell, and D.A. Fell Metabolic control analysis of mammalian serine metabolism Advances in Enzyme Regulation 30 1990 13 32
    • (1990) Advances in Enzyme Regulation , vol.30 , pp. 13-32
    • Snell, K.1    Fell, D.A.2
  • 290
    • 0023066723 scopus 로고
    • Microbial sulfur amino acids: An overview
    • K. Soda Microbial sulfur amino acids: an overview Methods in Enzymology 143 1987 453 459
    • (1987) Methods in Enzymology , vol.143 , pp. 453-459
    • Soda, K.1
  • 292
    • 0018693347 scopus 로고
    • The metabolism of 3-methylthiopropionate in rat liver homogenates
    • R.D. Steele, and N.J. Benevenga The metabolism of 3-methylthiopropionate in rat liver homogenates Journal of Biological Chemistry 254 1979 8885 8890
    • (1979) Journal of Biological Chemistry , vol.254 , pp. 8885-8890
    • Steele, R.D.1    Benevenga, N.J.2
  • 293
    • 0036194123 scopus 로고    scopus 로고
    • Trypanosomal antioxidants and emerging aspects of redox regulation in the trypanosomatids
    • D.J. Steenkamp Trypanosomal antioxidants and emerging aspects of redox regulation in the trypanosomatids Antioxidative Redox Signaling 4 2002 105 121
    • (2002) Antioxidative Redox Signaling , vol.4 , pp. 105-121
    • Steenkamp, D.J.1
  • 294
    • 0017697981 scopus 로고
    • Cultivation of Leishmania donovani and Leishmania braziliensis in defined media: Nutritional requirements
    • R.F. Steiger, and E. Steiger Cultivation of Leishmania donovani and Leishmania braziliensis in defined media: nutritional requirements Journal of Protozoology 24 1977 437 441
    • (1977) Journal of Protozoology , vol.24 , pp. 437-441
    • Steiger, R.F.1    Steiger, E.2
  • 295
    • 0015908281 scopus 로고
    • The use of the l-serine sulfhydrylase assay for the estimation of cystathionine β-synthase
    • P.P. Stepien, and N.J. Pieniazek The use of the l-serine sulfhydrylase assay for the estimation of cystathionine β-synthase Analytical Biochemistry 54 1973 294 299
    • (1973) Analytical Biochemistry , vol.54 , pp. 294-299
    • Stepien, P.P.1    Pieniazek, N.J.2
  • 296
    • 0022464168 scopus 로고
    • Metabolism of sulfur-containing amino acids
    • M.H. Stipanuk Metabolism of sulfur-containing amino acids Annual Review of Nutrition 6 1986 179 209
    • (1986) Annual Review of Nutrition , vol.6 , pp. 179-209
    • Stipanuk, M.H.1
  • 297
    • 3142729014 scopus 로고    scopus 로고
    • Sulfur amino acid metabolism: Pathways for production and removal of homocysteine and cysteine
    • M.H. Stipanuk Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine Annual Review of Nutrition 24 2004 539 577
    • (2004) Annual Review of Nutrition , vol.24 , pp. 539-577
    • Stipanuk, M.H.1
  • 298
    • 0023630758 scopus 로고
    • Pharmacologic aspects of S-adenosylmethionine. Pharmacokinetics and pharmacodynamics
    • G. Stramentinoli Pharmacologic aspects of S-adenosylmethionine. Pharmacokinetics and pharmacodynamics American Journal of Medicine 83 1987 35 42
    • (1987) American Journal of Medicine , vol.83 , pp. 35-42
    • Stramentinoli, G.1
  • 300
    • 0014409133 scopus 로고
    • The mechanism of end product inhibition of serine biosynthesis. I. Purification and kinetics of phosphoglycerate dehydrogenase
    • E. Sugimoto, and L.I. Pizer The mechanism of end product inhibition of serine biosynthesis. I. Purification and kinetics of phosphoglycerate dehydrogenase Journal of Biological Chemistry 243 1968 2081 2089
    • (1968) Journal of Biological Chemistry , vol.243 , pp. 2081-2089
    • Sugimoto, E.1    Pizer, L.I.2
  • 301
    • 0033524399 scopus 로고    scopus 로고
    • Repair of oxidized calmodulin by methionine sulfoxide reductase restores ability to activate the plasma membrane Ca-ATPase
    • H. Sun, J. Gao, D.A. Ferrington, H. Biesiada, T.D. Williams, and T.C. Squier Repair of oxidized calmodulin by methionine sulfoxide reductase restores ability to activate the plasma membrane Ca-ATPase Biochemistry 38 1999 105 112
    • (1999) Biochemistry , vol.38 , pp. 105-112
    • Sun, H.1    Gao, J.2    Ferrington, D.A.3    Biesiada, H.4    Williams, T.D.5    Squier, T.C.6
  • 303
    • 0034804608 scopus 로고    scopus 로고
    • Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS
    • J. Tachezy, L.B. Sanchez, and M. Muller Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS Molecular Biology and Evolution 18 2001 1919 1928
    • (2001) Molecular Biology and Evolution , vol.18 , pp. 1919-1928
    • Tachezy, J.1    Sanchez, L.B.2    Muller, M.3
  • 304
    • 0025951254 scopus 로고
    • Differences in genomic DNA sequences between pathogenic and nonpathogenic isolates of Entamoeba histolytica identified by polymerase chain reaction
    • H. Tachibana, S. Ihara, S. Kobayashi, Y. Kaneda, T. Takeuchi, and Y. Watanabe Differences in genomic DNA sequences between pathogenic and nonpathogenic isolates of Entamoeba histolytica identified by polymerase chain reaction Journal of Clinical Microbiology 10 1991 2234 2239
    • (1991) Journal of Clinical Microbiology , vol.10 , pp. 2234-2239
    • Tachibana, H.1    Ihara, S.2    Kobayashi, S.3    Kaneda, Y.4    Takeuchi, T.5    Watanabe, Y.6
  • 307
    • 0029876208 scopus 로고    scopus 로고
    • Structure and function of S-adenosylmethionine synthetase: Crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution
    • F. Takusagawa, S. Kamitori, and G.D. Markham Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution Biochemistry 35 1996 2586 2596
    • (1996) Biochemistry , vol.35 , pp. 2586-2596
    • Takusagawa, F.1    Kamitori, S.2    Markham, G.D.3
  • 309
    • 0026492878 scopus 로고
    • Putrescine activated S-adenosylmethionine decarboxylase from Trypanosoma brucei brucei
    • B.L. Tekwani, C.J. Bacchi, and A.E. Pegg Putrescine activated S-adenosylmethionine decarboxylase from Trypanosoma brucei brucei Molecular and Cellular Biochemistry 117 1992 53 61
    • (1992) Molecular and Cellular Biochemistry , vol.117 , pp. 53-61
    • Tekwani, B.L.1    Bacchi, C.J.2    Pegg, A.E.3
  • 310
    • 0026738158 scopus 로고
    • Irreversible inhibition of S-adenosylmethionine decarboxylase of Trypanosoma brucei brucei by S-adenosylmethionine analogues
    • B.L. Tekwani, C.J. Bacchi, J.A. Secrist III, and A.E. Pegg Irreversible inhibition of S-adenosylmethionine decarboxylase of Trypanosoma brucei brucei by S-adenosylmethionine analogues Biochemical Pharmacology 44 1992 905 911
    • (1992) Biochemical Pharmacology , vol.44 , pp. 905-911
    • Tekwani, B.L.1    Bacchi, C.J.2    Secrist III, J.A.3    Pegg, A.E.4
  • 312
    • 0021848513 scopus 로고
    • L-Serine sulphydrase activity in trichomonads
    • K.W. Thong, and G.H. Coombs l-Serine sulphydrase activity in trichomonads IRCS Medical Science 13 1985 495 496
    • (1985) IRCS Medical Science , vol.13 , pp. 495-496
    • Thong, K.W.1    Coombs, G.H.2
  • 313
    • 0023190215 scopus 로고
    • Trichomonas species: Homocysteine desulphurase and serine sulphydrase activities
    • K.W. Thong, and G.H. Coombs Trichomonas species: homocysteine desulphurase and serine sulphydrase activities Experimental Parasitology 63 1987 143 151
    • (1987) Experimental Parasitology , vol.63 , pp. 143-151
    • Thong, K.W.1    Coombs, G.H.2
  • 314
    • 0022003044 scopus 로고
    • S-adenosylhomocysteine hydrolase activity in Trichomonas vaginalis and other trichomonads
    • K.W. Thong, G.H. Coombs, and B.E. Sanderson S-adenosylhomocysteine hydrolase activity in Trichomonas vaginalis and other trichomonads Molecular and Biochemical Parasitology 17 1985 35 44
    • (1985) Molecular and Biochemical Parasitology , vol.17 , pp. 35-44
    • Thong, K.W.1    Coombs, G.H.2    Sanderson, B.E.3
  • 315
    • 0023192742 scopus 로고
    • S-adenosylmethionine and transmethylation reactions in trichomonads
    • K.W. Thong, G.H. Coombs, and B.E. Sanderson S-adenosylmethionine and transmethylation reactions in trichomonads Parasitology Research 73 1987 193 198
    • (1987) Parasitology Research , vol.73 , pp. 193-198
    • Thong, K.W.1    Coombs, G.H.2    Sanderson, B.E.3
  • 317
    • 0142180049 scopus 로고    scopus 로고
    • Identification and characterization of two isoenzymes of methionine γ-lyase from Entamoeba histolytica: A key enzyme of sulfur-amino acid degradation in an anaerobic parasitic protist that lacks forward and reverse trans-sulfuration pathways
    • M. Tokoro, T. Asai, S. Kobayashi, T. Takeuchi, and T. Nozaki Identification and characterization of two isoenzymes of methionine γ-lyase from Entamoeba histolytica: a key enzyme of sulfur-amino acid degradation in an anaerobic parasitic protist that lacks forward and reverse trans-sulfuration pathways Journal of Biological Chemistry 278 2003 42717 42727
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 42717-42727
    • Tokoro, M.1    Asai, T.2    Kobayashi, S.3    Takeuchi, T.4    Nozaki, T.5
  • 319
    • 0032988857 scopus 로고    scopus 로고
    • The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica
    • J. Tovar, A. Fischer, and C.G. Clark The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica Molecular Microbiology 32 1999 1013 1021
    • (1999) Molecular Microbiology , vol.32 , pp. 1013-1021
    • Tovar, J.1    Fischer, A.2    Clark, C.G.3
  • 322
    • 0021099574 scopus 로고
    • Methionine synthesis from 5′-S-methylthioadenosine. Resolution of enzyme activities and identification of 1-phospho-5-S methylthioribulose
    • P.C. Trackman, and R.H. Abeles Methionine synthesis from 5′-S-methylthioadenosine. Resolution of enzyme activities and identification of 1-phospho-5-S methylthioribulose Journal of Biological Chemistry 258 1983 6717 6720
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 6717-6720
    • Trackman, P.C.1    Abeles, R.H.2
  • 323
    • 0017891669 scopus 로고
    • Antimalarial activity of S-isobutyl adenosine against Plasmodium falciparum in culture
    • W. Trager, M. Robert-Gero, and E. Lederer Antimalarial activity of S-isobutyl adenosine against Plasmodium falciparum in culture FEBS Letters 85 1978 264 266
    • (1978) FEBS Letters , vol.85 , pp. 264-266
    • Trager, W.1    Robert-Gero, M.2    Lederer, E.3
  • 324
    • 0018935181 scopus 로고
    • Plasmodium falciparum: Antimalarial activity in culture of sinefungin and other methylation inhibitors
    • W. Trager, M. Tershakovec, P.K. Chiang, and G.L. Cantoni Plasmodium falciparum: antimalarial activity in culture of sinefungin and other methylation inhibitors Experimental Parasitology 50 1980 83 89
    • (1980) Experimental Parasitology , vol.50 , pp. 83-89
    • Trager, W.1    Tershakovec, M.2    Chiang, P.K.3    Cantoni, G.L.4
  • 326
    • 1642504719 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant defenses: A target for the treatment of diseases caused by parasitic protozoa
    • J.F. Turrens Oxidative stress and antioxidant defenses: a target for the treatment of diseases caused by parasitic protozoa Molecular Aspects of Medicine 25 2004 211 220
    • (2004) Molecular Aspects of Medicine , vol.25 , pp. 211-220
    • Turrens, J.F.1
  • 328
    • 0023066978 scopus 로고
    • Cystathionine β-lyase from Escherichia coli
    • J. Uren Cystathionine β-lyase from Escherichia coli Methods in Enzymology 143 1987 483 486
    • (1987) Methods in Enzymology , vol.143 , pp. 483-486
    • Uren, J.1
  • 334
    • 0037164375 scopus 로고    scopus 로고
    • Homocysteine and cardiovascular disease: Evidence on causality from a meta-analysis
    • D.S. Wald, M. Law, and J.K. Morris Homocysteine and cardiovascular disease: evidence on causality from a meta-analysis British Medical Journal 325 2002 1202
    • (2002) British Medical Journal , vol.325 , pp. 1202
    • Wald, D.S.1    Law, M.2    Morris, J.K.3
  • 336
  • 337
    • 0013784861 scopus 로고
    • Purification and properties of chicken liver d-3-phosphoglycerate dehydrogenase
    • D.A. Walsh, and H.J. Sallach Purification and properties of chicken liver d-3-phosphoglycerate dehydrogenase Biochemistry 4 1965 1076 1085
    • (1965) Biochemistry , vol.4 , pp. 1076-1085
    • Walsh, D.A.1    Sallach, H.J.2
  • 338
    • 0028949538 scopus 로고
    • Molecular mechanisms and therapeutic approaches to the treatment of African trypanosomiasis
    • C.C. Wang Molecular mechanisms and therapeutic approaches to the treatment of African trypanosomiasis Annual Review of Pharmacology and Toxicology 35 1995 93 127
    • (1995) Annual Review of Pharmacology and Toxicology , vol.35 , pp. 93-127
    • Wang, C.C.1
  • 340
    • 0020512051 scopus 로고
    • Plasma serine to cysteine ratio as a biological marker for psychosis
    • R. Waziri, R. Wilson, and A.D. Sherman Plasma serine to cysteine ratio as a biological marker for psychosis British Journal of Psychiatry 143 1983 69 73
    • (1983) British Journal of Psychiatry , vol.143 , pp. 69-73
    • Waziri, R.1    Wilson, R.2    Sherman, A.D.3
  • 342
    • 0032847477 scopus 로고    scopus 로고
    • Sulfur metabolism in bacteria associated with cheese
    • B. Weimer, K. Seefeldt, and B. Dias Sulfur metabolism in bacteria associated with cheese Antonie Van Leeuwenhoek 76 1999 247 261
    • (1999) Antonie Van Leeuwenhoek , vol.76 , pp. 247-261
    • Weimer, B.1    Seefeldt, K.2    Dias, B.3
  • 346
    • 0014961271 scopus 로고
    • Purification and properties of 5-methyltetrahydropteroyltriglutamate- homocysteine transmethylase
    • C.D. Whitfield, E.J. Steers jr, and H. Weisbach Purification and properties of 5-methyltetrahydropteroyltriglutamate-homocysteine transmethylase Journal of Biological Chemistry 245 1970 390 401
    • (1970) Journal of Biological Chemistry , vol.245 , pp. 390-401
    • Whitfield, C.D.1    Steers Jr., E.J.2    Weisbach, H.3
  • 348
    • 0027378886 scopus 로고
    • A bacterial enzyme that catalyzes formation of carbon monoxide
    • J.W. Wray, and R.H. Abeles A bacterial enzyme that catalyzes formation of carbon monoxide Journal of Biological Chemistry 268 1993 21466 21469
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 21466-21469
    • Wray, J.W.1    Abeles, R.H.2
  • 349
    • 0028850881 scopus 로고
    • The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases
    • J.W. Wray, and R.H. Abeles The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases Journal of Biological Chemistry 270 1995 3147 3153
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 3147-3153
    • Wray, J.W.1    Abeles, R.H.2
  • 350
    • 0025780218 scopus 로고
    • Irreversible inhibition of S-adenosylmethionine decarboxylase in Plasmodium falciparum-infected erythrocytes: Growth inhibition in vitro
    • P.S. Wright, T.L. Byers, D.E. Cross-Doersen, P.P. McCann, and A.J. Bitonti Irreversible inhibition of S-adenosylmethionine decarboxylase in Plasmodium falciparum-infected erythrocytes: growth inhibition in vitro Biochemical Pharmacology 41 1991 1713 1718
    • (1991) Biochemical Pharmacology , vol.41 , pp. 1713-1718
    • Wright, P.S.1    Byers, T.L.2    Cross-Doersen, D.E.3    McCann, P.P.4    Bitonti, A.J.5
  • 353
    • 0033523088 scopus 로고    scopus 로고
    • Flux of the l-serine metabolism in rabbit, human, and dog livers. Substantial contributions of both mitochondrial and peroxisomal serine:pyruvate/alanine:glyoxylate aminotransferase
    • H.H. Xue, T. Sakaguchi, M. Fujie, H. Ogawa, and A. Ichiyama Flux of the l-serine metabolism in rabbit, human, and dog livers. Substantial contributions of both mitochondrial and peroxisomal serine:pyruvate/alanine:glyoxylate aminotransferase Journal of Biological Chemistry 274 1999 16028 16033
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 16028-16033
    • Xue, H.H.1    Sakaguchi, T.2    Fujie, M.3    Ogawa, H.4    Ichiyama, A.5
  • 354
    • 0027198139 scopus 로고
    • Inhibition of S-adenosyl-l-methionine (AdoMet) decarboxylase by the decarboxylated AdoMet analog 5′-([(Z)-4-amino-2-butenyl]methylamino)- 5′-deoxyadenosine (MDL 73811) decreases the capacities of Trypanosoma cruzi to infect and multiply within a mammalian host cell
    • M.A. Yakubu, S. Majumder, and F. Kierszenbaum Inhibition of S-adenosyl-l-methionine (AdoMet) decarboxylase by the decarboxylated AdoMet analog 5′-([(Z)-4-amino-2-butenyl]methylamino)-5′-deoxyadenosine (MDL 73811) decreases the capacities of Trypanosoma cruzi to infect and multiply within a mammalian host cell Journal of Parasitology 79 1993 525 532
    • (1993) Journal of Parasitology , vol.79 , pp. 525-532
    • Yakubu, M.A.1    Majumder, S.2    Kierszenbaum, F.3
  • 356
    • 0023778503 scopus 로고
    • Effect of dl-α-difluoromethylornithine on methionine cycle intermediates in Trypanosoma brucei brucei
    • N. Yarlett, and C.J. Bacchi Effect of dl-α-difluoromethylornithine on methionine cycle intermediates in Trypanosoma brucei brucei Molecular and Biochemical Parasitology 27 1988 1 10
    • (1988) Molecular and Biochemical Parasitology , vol.27 , pp. 1-10
    • Yarlett, N.1    Bacchi, C.J.2
  • 357
    • 0023778503 scopus 로고
    • Effect of dl-α-difluoromethylornithine on polyamine synthesis and interconversion in Trichomonas vaginalis grown in a semi-defined medium
    • N. Yarlett, and C.J. Bacchi Effect of dl-α-difluoromethylornithine on polyamine synthesis and interconversion in Trichomonas vaginalis grown in a semi-defined medium Molecular and Biochemical Parasitology 31 1988 1 9
    • (1988) Molecular and Biochemical Parasitology , vol.31 , pp. 1-9
    • Yarlett, N.1    Bacchi, C.J.2
  • 358
    • 0028077240 scopus 로고
    • Parasite polyamine metabolism: Targets for chemotherapy
    • N. Yarlett, and C.J. Bacchi Parasite polyamine metabolism: targets for chemotherapy Biochemical Society Transactions 22 1994 875 879
    • (1994) Biochemical Society Transactions , vol.22 , pp. 875-879
    • Yarlett, N.1    Bacchi, C.J.2
  • 359
    • 0026740472 scopus 로고
    • Inhibition of Trichomonas vaginalis ornithine decarboxylase by amino acid analogs
    • N. Yarlett, B. Goldberg, M.A. Moharrami, and C.J. Bacchi Inhibition of Trichomonas vaginalis ornithine decarboxylase by amino acid analogs Biochemical Pharmacology 44 1992 243 250
    • (1992) Biochemical Pharmacology , vol.44 , pp. 243-250
    • Yarlett, N.1    Goldberg, B.2    Moharrami, M.A.3    Bacchi, C.J.4
  • 361
    • 0018628116 scopus 로고
    • 1-Aminocyclopropanecarboxylate synthase, a key enzyme in ethylene biosynthesis
    • Y.B. Yu, D.O. Adams, and S.F. Yang 1-Aminocyclopropanecarboxylate synthase, a key enzyme in ethylene biosynthesis Archives of Biochemistry and Biophysics 198 1979 280 286
    • (1979) Archives of Biochemistry and Biophysics , vol.198 , pp. 280-286
    • Yu, Y.B.1    Adams, D.O.2    Yang, S.F.3
  • 362
    • 0024473905 scopus 로고
    • Isolation, various physico-chemical and catalytic properties of l-methionine-γ-lyase from Pseudomonas taetrolens
    • [In Russian; English Summary.]
    • Zanin, V.A., Lukina, V.I., and Berezov, T.T. (1989). [Isolation, various physico-chemical and catalytic properties of l-methionine-γ-lyase from Pseudomonas taetrolens.] Voprosy Meditsinskoi Khimii 35, 84-89. [In Russian; English Summary.]
    • (1989) Voprosy Meditsinskoi Khimii , vol.35 , pp. 84-89
    • Zanin, V.A.1    Lukina, V.I.2    Berezov, T.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.