메뉴 건너뛰기




Volumn 105, Issue 2, 2003, Pages 149-158

Trypanosoma cruzi: Molecular cloning and characterization of the S-adenosylhomocysteine hydrolase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE; ADENOSYLHOMOCYSTEINASE; HOMOCYSTEINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; RECOMBINANT ENZYME;

EID: 1242315505     PISSN: 00144894     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exppara.2003.10.001     Document Type: Article
Times cited : (21)

References (45)
  • 2
    • 0033256628 scopus 로고    scopus 로고
    • Biology and ultra-structure of Trypanosoma cruzi: A 90-year old challenge for scientists
    • Araujo-Jorge T.C. Biology and ultra-structure of Trypanosoma cruzi: a 90-year old challenge for scientists. Memorias do Instituto Oswaldo Cruz. 94:1999;131-134.
    • (1999) Memorias Do Instituto Oswaldo Cruz , vol.94 , pp. 131-134
    • Araujo-Jorge, T.C.1
  • 3
    • 0030808562 scopus 로고    scopus 로고
    • Specific inhibitory effect of 3-deazaneplanocin a against several Leishmania mexicana and L. braziliensis strains
    • Avila J.L., Avila A., Polegre M.A., Marquez V.E. Specific inhibitory effect of 3-deazaneplanocin A against several Leishmania mexicana and L. braziliensis strains. American Journal of Tropical Medicine and Hygiene. 57:1997;407-412.
    • (1997) American Journal of Tropical Medicine and Hygiene , vol.57 , pp. 407-412
    • Avila, J.L.1    Avila, A.2    Polegre, M.A.3    Marquez, V.E.4
  • 5
    • 0029135322 scopus 로고
    • Copper binding to mouse liver S -adenosylhomocysteine hydrolase and the effects of copper on its levels
    • Bethin K.E., Cimato T.R., Ettinger M.J. Copper binding to mouse liver. S -adenosylhomocysteine hydrolase and the effects of copper on its levels Journal of Biological Chemistry. 270:1995;20703-20711.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 20703-20711
    • Bethin, K.E.1    Cimato, T.R.2    Ettinger, M.J.3
  • 6
    • 0025298557 scopus 로고
    • Antimalarial activity of a 4',5'-unsaturated 5'-fluoroadenosine mechanism-based inhibitor of S -adenosyl-L-homocysteine hydrolase
    • Bitonti A.J., Baumann R.J., Jarvi E.T., McCarthy J.R., McCann P.P. 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
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry. 72:1976;248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0031018917 scopus 로고    scopus 로고
    • The S -adenosyl-L-homocysteine hydrolase of Drosophila melanogaster: Identification, deduced amino acid sequence and cytological localization of the structural gene
    • Caggese C., Ragone G., Barsanti P., Moschetti R., Messina A., Massari S., Caizzi R. The. S -adenosyl-L-homocysteine hydrolase of Drosophila melanogaster: identification, deduced amino acid sequence and cytological localization of the structural gene Molecular and General Genetics. 253:1997;492-498.
    • (1997) Molecular and General Genetics , vol.253 , pp. 492-498
    • Caggese, C.1    Ragone, G.2    Barsanti, P.3    Moschetti, R.4    Messina, A.5    Massari, S.6    Caizzi, R.7
  • 9
    • 0031934077 scopus 로고    scopus 로고
    • Biological effects of inhibitors of S -adenosylhomocysteine hydrolase
    • Chiang P.K. Biological effects of inhibitors of. S -adenosylhomocysteine hydrolase Pharmacology and Therapeutics. 77:1998;115-134.
    • (1998) Pharmacology and Therapeutics , vol.77 , pp. 115-134
    • Chiang, P.K.1
  • 10
    • 0024409705 scopus 로고
    • Sequence of full length cDNA for human S -adenosylhomocysteine hydrolase
    • Coulter-Karis D.E., Hershfield M.S. Sequence of full length cDNA for human. S -adenosylhomocysteine hydrolase Annals of Human Genetics. 53:1989;169-175.
    • (1989) Annals of Human Genetics , vol.53 , pp. 169-175
    • Coulter-Karis, D.E.1    Hershfield, M.S.2
  • 11
    • 0028292569 scopus 로고
    • Plasmodium falciparum S -adenosylhomocysteine hydrolase. cDNA identification, predicted protein sequence, and expression in Escherichia coli
    • Creedon K.A., Rathod P.K., Wellems T.E. 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
  • 13
    • 0023709288 scopus 로고
    • Derivatives of epinephrine, norepinephrine, octopamine and histamine formed by homogenates of Trichostrongylus colubriformis, a nematode parasite of ruminants
    • Frandsen J.C., Bone L.W. Derivatives of epinephrine, norepinephrine, octopamine and histamine formed by homogenates of Trichostrongylus colubriformis, a nematode parasite of ruminants. Comparative Biochemistry and Physiology C. 91:1988;385-387.
    • (1988) Comparative Biochemistry and Physiology C , vol.91 , pp. 385-387
    • Frandsen, J.C.1    Bone, L.W.2
  • 14
    • 0023811730 scopus 로고
    • Discontinuously synthesized mRNA from Trypanosoma brucei contains the highly methylated 5' cap structure, m7GpppA*A*C(2'-O)mU*A
    • Freistadt M.S., Cross G.A., Robertson H.D. Discontinuously synthesized mRNA from Trypanosoma brucei contains the highly methylated 5' cap structure, m7GpppA*A*C(2'-O)mU*A. Journal of Biological Chemistry. 263:1988;15071-15075.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 15071-15075
    • Freistadt, M.S.1    Cross, G.A.2    Robertson, H.D.3
  • 15
    • 0024534958 scopus 로고
    • Rat liver S -adenosylhomocysteinase. Spectrophotometric study of coenzyme binding
    • Gomi T., Takata Y., Fujioka M. Rat liver. S -adenosylhomocysteinase. Spectrophotometric study of coenzyme binding Biochimica et Biophysica Acta. 994:1989;172-179.
    • (1989) Biochimica et Biophysica Acta , vol.994 , pp. 172-179
    • Gomi, T.1    Takata, Y.2    Fujioka, M.3
  • 17
    • 0033568609 scopus 로고    scopus 로고
    • Characterization of prenylated protein methyltransferase in Leishmania
    • Hasne M.P., Lawrence F. Characterization of prenylated protein methyltransferase in Leishmania. The Biochemical Journal. 342(Part 3):1999;513-518.
    • (1999) The Biochemical Journal , vol.342 , Issue.PART 3 , pp. 513-518
    • Hasne, M.P.1    Lawrence, F.2
  • 18
    • 0037016751 scopus 로고    scopus 로고
    • Characterization of the mRNA capping apparatus of the microsporidian parasite Encephalitozoon cuniculi
    • Hausmann S., Vivares C.P., Shuman S. Characterization of the mRNA capping apparatus of the microsporidian parasite Encephalitozoon cuniculi. Journal of Biological Chemistry. 277:2002;96-103.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 96-103
    • Hausmann, S.1    Vivares, C.P.2    Shuman, S.3
  • 20
    • 0035909837 scopus 로고    scopus 로고
    • Computational characterization of substrate binding and catalysis in S -adenosylhomocysteine hydrolase
    • Hu Y., Yang X., Yin D.H., Mahadevan J., Kuczera K., Schowen R.L., Borchardt R.T. Computational characterization of substrate binding and catalysis in. S -adenosylhomocysteine hydrolase Biochemistry. 40:2001;15143-15152.
    • (2001) Biochemistry , vol.40 , pp. 15143-15152
    • Hu, Y.1    Yang, X.2    Yin, D.H.3    Mahadevan, J.4    Kuczera, K.5    Schowen, R.L.6    Borchardt, R.T.7
  • 21
    • 0027924584 scopus 로고
    • American trypanosomiasis (Chagas' disease) - A tropical disease now in the United States
    • Kirchhoff L.V. American trypanosomiasis (Chagas' disease) - a tropical disease now in the United States. The New England Journal of Medicine. 329:1993;639-644.
    • (1993) The New England Journal of Medicine , vol.329 , pp. 639-644
    • Kirchhoff, L.V.1
  • 23
    • 0034519012 scopus 로고    scopus 로고
    • MPBLAST: Improved BLAST performance with multiplexed queries
    • Korf I., Gish W. MPBLAST: improved BLAST performance with multiplexed queries. Bioinformatics. 16:2000;1052-1053.
    • (2000) Bioinformatics , vol.16 , pp. 1052-1053
    • Korf, I.1    Gish, W.2
  • 25
    • 0031691447 scopus 로고    scopus 로고
    • Trichomonas vaginalis: Expression and characterisation of recombinant S -adenosylhomocysteinase
    • Minotto L., Ko G.A., Edwards M.R., Bagnara A.S. 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
  • 26
    • 0029914055 scopus 로고    scopus 로고
    • Inhibition of Trypanosoma cruzi growth in mammalian cells by purine and pyrimidine analogs
    • Nakajima-Shimada J., Hirota Y., Aoki T. Inhibition of Trypanosoma cruzi growth in mammalian cells by purine and pyrimidine analogs. Antimicrobial Agents and Chemotherapy. 40:1996;2455-2458.
    • (1996) Antimicrobial Agents and Chemotherapy , vol.40 , pp. 2455-2458
    • Nakajima-Shimada, J.1    Hirota, Y.2    Aoki, T.3
  • 27
    • 0018800321 scopus 로고
    • The mechanism of action of S -adenosylhomocysteinase
    • Palmer J.L., Abeles R.H. The mechanism of action of. S -adenosylhomocysteinase Journal of Biological Chemistry. 254:1979;1217-1226.
    • (1979) Journal of Biological Chemistry , vol.254 , pp. 1217-1226
    • Palmer, J.L.1    Abeles, R.H.2
  • 28
    • 0032143330 scopus 로고    scopus 로고
    • Trypanosoma cruzi has not lost its S -adenosylmethionine decarboxylase: Characterization of the gene and the encoded enzyme
    • Persson K., Aslund L., Grahn B., Hanke J., Heby O. 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
  • 32
    • 0021416988 scopus 로고
    • Progress curve analysis of adenosine deaminase-catalyzed reactions
    • Spector T. Progress curve analysis of adenosine deaminase-catalyzed reactions. Analytical Biochemistry. 138:1984;242-245.
    • (1984) Analytical Biochemistry , vol.138 , pp. 242-245
    • Spector, T.1
  • 34
    • 0029097194 scopus 로고
    • Accurate modification of the trypanosome spliced leader cap structure in a homologous cell-free system
    • Ullu E., Tschudi C. Accurate modification of the trypanosome spliced leader cap structure in a homologous cell-free system. Journal of Biological Chemistry. 270:1995;20365-20369.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 20365-20369
    • Ullu, E.1    Tschudi, C.2
  • 35
    • 0033256630 scopus 로고    scopus 로고
    • Parasitological cure of Chagas disease: Is it possible? Is it relevant?
    • Urbina J.A. Parasitological cure of Chagas disease: is it possible? Is it relevant? Memorias do Instituto Oswaldo Cruz. 94:1999;349-355.
    • (1999) Memorias Do Instituto Oswaldo Cruz , vol.94 , pp. 349-355
    • Urbina, J.A.1
  • 36
    • 0030611719 scopus 로고    scopus 로고
    • Inhibitors of delta24(25) sterol methyltransferase block sterol synthesis and cell proliferation in Pneumocystis carinii
    • Urbina J.A., Visbal G., Contreras L.M., McLaughlin G., Docampo R. Inhibitors of delta24(25) sterol methyltransferase block sterol synthesis and cell proliferation in Pneumocystis carinii. Antimicrobial Agents and Chemotherapy. 41:1997;1428-1432.
    • (1997) Antimicrobial Agents and Chemotherapy , vol.41 , pp. 1428-1432
    • Urbina, J.A.1    Visbal, G.2    Contreras, L.M.3    McLaughlin, G.4    Docampo, R.5
  • 37
    • 0029975328 scopus 로고    scopus 로고
    • Antiproliferative effects of delta 24(25) sterol methyl transferase inhibitors on Trypanosoma (Schizotrypanum) cruzi: In vitro and in vivo studies
    • Urbina J.A., Vivas J., Lazardi K., Molina J., Payares G., Piras M.M., Piras R. Antiproliferative effects of delta 24(25) sterol methyl transferase inhibitors on Trypanosoma (Schizotrypanum) cruzi: in vitro and in vivo studies. Chemotherapy. 42:1996;294-307.
    • (1996) Chemotherapy , vol.42 , pp. 294-307
    • Urbina, J.A.1    Vivas, J.2    Lazardi, K.3    Molina, J.4    Payares, G.5    Piras, M.M.6    Piras, R.7
  • 38
    • 0028783574 scopus 로고
    • Modification of the sterol composition of Trypanosoma (Schizotrypanum) cruzi epimastigotes by delta 24(25)-sterol methyl transferase inhibitors and their combinations with ketoconazole
    • Urbina J.A., Vivas J., Visbal G., Contreras L.M. Modification of the sterol composition of Trypanosoma (Schizotrypanum) cruzi epimastigotes by delta 24(25)-sterol methyl transferase inhibitors and their combinations with ketoconazole. Molecular and Biochemical Parasitology. 73:1995;199-210.
    • (1995) Molecular and Biochemical Parasitology , vol.73 , pp. 199-210
    • Urbina, J.A.1    Vivas, J.2    Visbal, G.3    Contreras, L.M.4
  • 41
    • 0003769226 scopus 로고
    • Report of a WHO Expert Committee. World Health Organization Technical Report Series 811
    • WHO, 1991. Control of Chagas disease. Report of a WHO Expert Committee. World Health Organization Technical Report Series 811, pp. 1-95.
    • (1991) Control of Chagas Disease , pp. 1-95
  • 42
    • 0034669468 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of S -adenosylhomocysteine hydrolase from Leishmania donovani
    • Yang X., Borchardt R.T. Overexpression, purification, and characterization of. S -adenosylhomocysteine hydrolase from Leishmania donovani Archives of Biochemistry and Biophysics. 383:2000;272-280.
    • (2000) Archives of Biochemistry and Biophysics , vol.383 , pp. 272-280
    • Yang, X.1    Borchardt, R.T.2
  • 43
    • 0034702809 scopus 로고    scopus 로고
    • Closer proximity between opposing domains of vertebrate calmodulin following deletion of Met(145)-Lys(148)
    • Yin D., Sun H., Ferrington D.A., Squier T.C. Closer proximity between opposing domains of vertebrate calmodulin following deletion of Met(145)-Lys(148). Biochemistry. 39:2000;10255-10268.
    • (2000) Biochemistry , vol.39 , pp. 10255-10268
    • Yin, D.1    Sun, H.2    Ferrington, D.A.3    Squier, T.C.4
  • 45
    • 0027507869 scopus 로고
    • Ligand-dependent changes in intrinsic fluorescence of S -adenosylhomocysteine hydrolase: Implications for the mechanism of inhibitor-induced inhibition
    • Yuan C.S., Yeh J., Squier T.C., Rawitch A., Borchardt R.T. Ligand-dependent changes in intrinsic fluorescence of. S -adenosylhomocysteine hydrolase: implications for the mechanism of inhibitor-induced inhibition Biochemistry. 32:1993;10414-10422.
    • (1993) Biochemistry , vol.32 , pp. 10414-10422
    • Yuan, C.S.1    Yeh, J.2    Squier, T.C.3    Rawitch, A.4    Borchardt, R.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.