메뉴 건너뛰기




Volumn 120, Issue 6, 2000, Pages 593-600

Trichinella spiralis and Trichinella pseudospiralis: Developmental patterns of enzymes involved in thymidylate biosynthesis and pyrimidine salvage

Author keywords

Dihydrofolate reductase; dUTPase; Pyrimidine salvage; Thymidylate synthase; Trichinella pseudospiralis; Trichinella spiralis

Indexed keywords

CYTIDINE PHOSPHATE; DEOXYURIDINE PHOSPHATE; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; DIHYDROFOLATE REDUCTASE; FLUOROURACIL; OROTATE PHOSPHORIBOSYLTRANSFERASE; PEPSIN A; PLEVITREXED; PYRIMIDINE; THYMIDINE PHOSPHATE; THYMIDINE PHOSPHORYLASE; THYMIDYLATE SYNTHASE; URIDINE PHOSPHORYLASE;

EID: 0034114522     PISSN: 00311820     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0031182099005880     Document Type: Article
Times cited : (14)

References (49)
  • 1
    • 0031463610 scopus 로고    scopus 로고
    • Pyrimidine nucleotidases from human crythrocyte possess phosphotransferase activities specific for pyrimidine nucleotides
    • AMICI, A., EMANUELLI, M., MAGNI, G., RAFFAELLI, N. & RUGGIERI, S. (1997). Pyrimidine nucleotidases from human crythrocyte possess phosphotransferase activities specific for pyrimidine nucleotides. FEBS Letters 419, 263-267.
    • (1997) FEBS Letters , vol.419 , pp. 263-267
    • Amici, A.1    Emanuelli, M.2    Magni, G.3    Raffaelli, N.4    Ruggieri, S.5
  • 3
    • 0032529047 scopus 로고    scopus 로고
    • Thymidine phosphorylase, 2-deoxy-D-ribose and angiogenesis
    • BROWN, N. S. & BICKNELL., R. (1998). Thymidine phosphorylase, 2-deoxy-D-ribose and angiogenesis. The Biochemical Journal 334, 1-8.
    • (1998) The Biochemical Journal , vol.334 , pp. 1-8
    • Brown, N.S.1    Bicknell, R.2
  • 4
    • 0022908327 scopus 로고
    • The response of NIH mice to Trichinella pseudospiralis
    • CABAJ, W. (1986). The response of NIH mice to Trichinella pseudospiralis. Acta Parasitologica Polonica 31, 77-85.
    • (1986) Acta Parasitologica Polonica , vol.31 , pp. 77-85
    • Cabaj, W.1
  • 5
    • 0015813306 scopus 로고
    • Thymidylate synthetase in mutants of Drosophila melanogaster
    • CARPENTER, N. J. (1973). Thymidylate synthetase in mutants of Drosophila melanogaster. Genetics 75, 113-122.
    • (1973) Genetics , vol.75 , pp. 113-122
    • Carpenter, N.J.1
  • 6
    • 0030111238 scopus 로고    scopus 로고
    • The role of thymidylate synthase as an RNA binding protein
    • CHU, E. & ALLEGRA, C. J. (1996). The role of thymidylate synthase as an RNA binding protein. BioEssays 18, 191-198.
    • (1996) Bioessays , vol.18 , pp. 191-198
    • Chu, E.1    Allegra, C.J.2
  • 10
    • 0040719579 scopus 로고    scopus 로고
    • Trichinella spiralis thymidylate synthase: Developmental pattern, isolation, molecular properties and inhibition by substrate and cofactor analogues
    • DA̧BROWSKA, M., ZIELIŃSKI, Z., WRANICZ, M., MICHALSKI, R., PAWELŁCZAK, K. & RODE, W. (1996). Trichinella spiralis thymidylate synthase: developmental pattern, isolation, molecular properties and inhibition by substrate and cofactor analogues. Biochemical and Biophysical Research Communications 228, 440-445.
    • (1996) Biochemical and Biophysical Research Communications , vol.228 , pp. 440-445
    • Da̧browska, M.1    Zieliński, Z.2    Wranicz, M.3    Michalski, R.4    PawelŁczak, K.5    Rode, W.6
  • 11
    • 0027329557 scopus 로고
    • Trichinella spiralis and the concept of niche
    • DESPOMMIER, D. D. (1993). Trichinella spiralis and the concept of niche. Journal of Parasitology 79, 472-482.
    • (1993) Journal of Parasitology , vol.79 , pp. 472-482
    • Despommier, D.D.1
  • 12
    • 0032145865 scopus 로고    scopus 로고
    • How does Trichinella spiralis make itself at home?
    • DESPOMMIER, D. D. (1998). How does Trichinella spiralis make itself at home? Parasitology Today 14, 318-323.
    • (1998) Parasitology Today , vol.14 , pp. 318-323
    • Despommier, D.D.1
  • 13
    • 0023607101 scopus 로고
    • Interaction of 5-fluoro-4-thio-2′-deoxyuridine 5′-phosphate with mammalian tumour thymidylate synthase: Role of the pyrimidine N(3)-H dissociation
    • DZIK, J. M., KULIKOWSKI, T., ZIELIŃSKI, Z., CIEŚLA, J., RODE, W. & SHUGAR, D. (1987). Interaction of 5-fluoro-4-thio-2′-deoxyuridine 5′-phosphate with mammalian tumour thymidylate synthase: role of the pyrimidine N(3)-H dissociation. Biochemical and Biophysical Research Communications 149, 1200-1207.
    • (1987) Biochemical and Biophysical Research Communications , vol.149 , pp. 1200-1207
    • Dzik, J.M.1    Kulikowski, T.2    Zieliński, Z.3    Cieśla, J.4    Rode, W.5    Shugar, D.6
  • 14
    • 0027485458 scopus 로고
    • Interaction of 2-thio-5-fluoro-dUMP and 4-thio-5-fluoro-dUMP with mammalian normal and tumour, and helminthic, thymidylate synthases: Influence of C(4)-substituents on specificity for enzyme inactivation
    • DZIK, J. M., ZIELIŃSKI, Z., CIEŚLA, J., BRETNER, M., KULIKOWSKI, T., SHUGAR, D., BERTINO, J. R. & RODE, W. (1993). Interaction of 2-thio-5-fluoro-dUMP and 4-thio-5-fluoro-dUMP with mammalian normal and tumour, and helminthic, thymidylate synthases: influence of C(4)-substituents on specificity for enzyme inactivation. Biochemical Biophysical Research Communications 195, 1301-1308.
    • (1993) Biochemical Biophysical Research Communications , vol.195 , pp. 1301-1308
    • Dzik, J.M.1    Zieliński, Z.2    Cieśla, J.3    Bretner, M.4    Kulikowski, T.5    Shugar, D.6    Bertino, J.R.7    Rode, W.8
  • 15
    • 0029837986 scopus 로고    scopus 로고
    • Developmental control of cell cycle regulators: A fly's perspective
    • EDGAR, B. A. & LEHNER, C. F. (1996). Developmental control of cell cycle regulators: a fly's perspective. Science 274, 1646-1652.
    • (1996) Science , vol.274 , pp. 1646-1652
    • Edgar, B.A.1    Lehner, C.F.2
  • 16
    • 0017858371 scopus 로고
    • In vitro thymidine kinase activity: Present in Hymenolepis diminuta (Cestoda) and Moniliformis dubius (Acanthocephala) but apparently lacking in Ascaris lumbricoides (Nematoda)
    • FARLAND, W. H. & MACINNIS, A. J. (1978). In vitro thymidine kinase activity: present in Hymenolepis diminuta (Cestoda) and Moniliformis dubius (Acanthocephala) but apparently lacking in Ascaris lumbricoides (Nematoda). Journal of Parasitology 64, 564-565.
    • (1978) Journal of Parasitology , vol.64 , pp. 564-565
    • Farland, W.H.1    Macinnis, A.J.2
  • 17
    • 0015870362 scopus 로고
    • Thymidyate synthetase
    • FRIEDKIN, M. (1973). Thymidyate synthetase. Advances in Enzymology 38, 235-292.
    • (1973) Advances in Enzymology , vol.38 , pp. 235-292
    • Friedkin, M.1
  • 19
    • 0015411171 scopus 로고
    • Species of Trichinella isolated from wild animals
    • GARKAVI, B. L. (1972). Species of Trichinella isolated from wild animals. Veterinariya 10, 90-91.
    • (1972) Veterinariya , vol.10 , pp. 90-91
    • Garkavi, B.L.1
  • 20
    • 0030033020 scopus 로고    scopus 로고
    • Antifungal agents: Chemotherapeutic targets and immunologic strategies
    • GEORGOPAPADAKOU, N. H. & WALSH, T. J. (1996). Antifungal agents: chemotherapeutic targets and immunologic strategies. Antimicrobial Agents and Chemotherapy 40, 279-291.
    • (1996) Antimicrobial Agents and Chemotherapy , vol.40 , pp. 279-291
    • Georgopapadakou, N.H.1    Walsh, T.J.2
  • 21
    • 0033251526 scopus 로고    scopus 로고
    • An isotopic assay of dUTPase activity based on coupling with thymidylate synthase
    • GOLOS, B. & RODE, W. (1999). An isotopic assay of dUTPase activity based on coupling with thymidylate synthase. Acta Biochimica Polonica 46, 837-840.
    • (1999) Acta Biochimica Polonica , vol.46 , pp. 837-840
    • Golos, B.1    Rode, W.2
  • 22
    • 0002366750 scopus 로고
    • Clinical pathology: Diagnostic laboratory procedures
    • ed. Could, S. E. Charles C. Thomas: Springfield, USA
    • GOULD, S. E. (1970). Clinical pathology: diagnostic laboratory procedures. In Trichinosis in Man and Animals (ed. Could, S. E.), pp. 190-221. Charles C. Thomas: Springfield, USA.
    • (1970) Trichinosis in Man and Animals , pp. 190-221
    • Gould, S.E.1
  • 24
    • 0023332658 scopus 로고
    • Deoxyuridine triphosphate nucleotidohydrolase activity and its correlations with multiplication of erythroid cells in rat spleen
    • HOKARI, S., HASEGAWA, M., SAKAGISHI, Y. & KIKUCHI, G. (1987). Deoxyuridine triphosphate nucleotidohydrolase activity and its correlations with multiplication of erythroid cells in rat spleen. Biochemistry International 14, 851-857.
    • (1987) Biochemistry International , vol.14 , pp. 851-857
    • Hokari, S.1    Hasegawa, M.2    Sakagishi, Y.3    Kikuchi, G.4
  • 25
    • 0028910977 scopus 로고
    • Trichinella spiralis: Subversion of differentiated mammalian skeletal muscle cells
    • JASMER, D. P. (1995). Trichinella spiralis: subversion of differentiated mammalian skeletal muscle cells. Parasitology Today 11, 185-188.
    • (1995) Parasitology Today , vol.11 , pp. 185-188
    • Jasmer, D.P.1
  • 27
    • 0027957354 scopus 로고
    • Changes in host muscles induced by excretory/secretory products of larval Trichinella spiralis and Trichinella pseudospiralis
    • KO, R. C., FAN, L., LEE, D. L. & COMPTON, H. (1994). Changes in host muscles induced by excretory/secretory products of larval Trichinella spiralis and Trichinella pseudospiralis. Parasitology 108, 195-205.
    • (1994) Parasitology , vol.108 , pp. 195-205
    • Ko, R.C.1    Fan, L.2    Lee, D.L.3    Compton, H.4
  • 28
    • 0027937754 scopus 로고
    • 5-Fluoro-2′-deoxycytidine 5′-monophosphate is a mechanism-based inhibitor of thymidylate synthase
    • LIU, L. & SANTI, D. V. (1994). 5-Fluoro-2′-deoxycytidine 5′-monophosphate is a mechanism-based inhibitor of thymidylate synthase. Biochimica et Biophysica Acta 1209, 89-94.
    • (1994) Biochimica et Biophysica Acta , vol.1209 , pp. 89-94
    • Liu, L.1    Santi, D.V.2
  • 30
    • 0001396685 scopus 로고
    • The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions
    • MORRISON, J. F. (1982). The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions. Trends in Biochemical Sciences 7, 102-105.
    • (1982) Trends in Biochemical Sciences , vol.7 , pp. 102-105
    • Morrison, J.F.1
  • 31
    • 0021282047 scopus 로고
    • Structure-activity relationship of pyrimidine base analogs as ligands of orotate phosphoribosyltransferase
    • NIEDZWICKI, J. G., ILTZSCH, M. H., EL KOUNI, M. H. & CHA, S. (1984). Structure-activity relationship of pyrimidine base analogs as ligands of orotate phosphoribosyltransferase. Biochemical Pharmacology 33, 2383-2395.
    • (1984) Biochemical Pharmacology , vol.33 , pp. 2383-2395
    • Niedzwicki, J.G.1    Iltzsch, M.H.2    El Kouni, M.H.3    Cha, S.4
  • 33
    • 0029021602 scopus 로고
    • Increased thymidylate synthase protein levels are principally associated with proliferation but not cell cycle phase in asynchronous human cancer cells
    • PESTALOZZI, B. C., MCGINN, C. J., KINSELLA, T. J., DRAKE, J. C., GLENNON, M. C., ALLEGRA, C. J. & JOHNSTON, P. G. (1995). Increased thymidylate synthase protein levels are principally associated with proliferation but not cell cycle phase in asynchronous human cancer cells. British Journal of Cancer 71, 1151-1157.
    • (1995) British Journal of Cancer , vol.71 , pp. 1151-1157
    • Pestalozzi, B.C.1    McGinn, C.J.2    Kinsella, T.J.3    Drake, J.C.4    Glennon, M.C.5    Allegra, C.J.6    Johnston, P.G.7
  • 34
    • 0030976693 scopus 로고    scopus 로고
    • Antimalarial agents directed at thymidylate synthase
    • RATHOD, P. K. (1997). Antimalarial agents directed at thymidylate synthase. Journal of Pharmacy and Pharmacology 49 (Suppl. 2), 704-711.
    • (1997) Journal of Pharmacy and Pharmacology , vol.49 , Issue.SUPPL. 2 , pp. 704-711
    • Rathod, P.K.1
  • 36
    • 0013668888 scopus 로고
    • Developmental pattern of thymidylate synthetase activity in silkworm: Bombyx mori L
    • RODE, W. & SZYMANOWSKA, H. (1976). Developmental pattern of thymidylate synthetase activity in silkworm: Bombyx mori L. Insect Biochemistry 6, 333-337.
    • (1976) Insect Biochemistry , vol.6 , pp. 333-337
    • Rode, W.1    Szymanowska, H.2
  • 38
    • 0030046306 scopus 로고    scopus 로고
    • Meiotic metaphase arrest in animal oocytes : Its mechanisms and biological significance
    • SAGATA, N. (1996). Meiotic metaphase arrest in animal oocytes : its mechanisms and biological significance. Trends in Cell Biology 6, 22-28.
    • (1996) Trends in Cell Biology , vol.6 , pp. 22-28
    • Sagata, N.1
  • 39
    • 0000299873 scopus 로고
    • Folates in pyrimidine biosynthesis
    • ed. Blakley, R. L. & Benkovic, S. J. Wiley, New York
    • SANTl, D. V. & DANENBERG, P. V. (1984). Folates in pyrimidine biosynthesis. In Folates and Pterines (ed. Blakley, R. L. & Benkovic, S. J.), vol. 1, pp. 345-398. Wiley, New York.
    • (1984) Folates and Pterines , vol.1 , pp. 345-398
    • Santl, D.V.1    Danenberg, P.V.2
  • 41
    • 0002230517 scopus 로고
    • Phosphorylating enzymes involved in activation of chemotherapeutic nucleosides and nucleotides
    • ed. Shugar, D., Rode, W. & Borowski, K. Polish Scientific Publishers PWN and Springer Verlag: Warszawa and Berlin
    • SHUGAR, D. (1992). Phosphorylating enzymes involved in activation of chemotherapeutic nucleosides and nucleotides. In Molecular Aspects of Chemotherapy (ed. Shugar, D., Rode, W. & Borowski, K.), pp. 239-270. Polish Scientific Publishers PWN and Springer Verlag: Warszawa and Berlin.
    • (1992) Molecular Aspects of Chemotherapy , pp. 239-270
    • Shugar, D.1
  • 42
    • 0026724026 scopus 로고
    • Precursors of pyrimidine nucleotide biosynthesis for gravid Angiostrongylus cantonensis (Nematoda: Metastrongyloidea)
    • SO, N. N. C., WONG, P. R. L. & KO, R. C. (1992). Precursors of pyrimidine nucleotide biosynthesis for gravid Angiostrongylus cantonensis (Nematoda: Metastrongyloidea). International Journal for Parasitology 22, 427-433.
    • (1992) International Journal for Parasitology , vol.22 , pp. 427-433
    • So, N.N.C.1    Wong, P.R.L.2    Ko, R.C.3
  • 43
    • 0000423843 scopus 로고
    • Biochemistry
    • ed. Campbell, W. C. Plenum Press: New York
    • STEWART, G. L. (1983). Biochemistry. In Trichinella and Trichinosis (ed. Campbell, W. C.), pp. 153-172. Plenum Press: New York.
    • (1983) Trichinella and Trichinosis , pp. 153-172
    • Stewart, G.L.1
  • 44
    • 0015611002 scopus 로고
    • Deoxyribonucleic acid metabolism in mouse trichinosis
    • STEWART, G. L. & READ, C. P. (1973). Deoxyribonucleic acid metabolism in mouse trichinosis. Journal of Parasitology 59, 264-267.
    • (1973) Journal of Parasitology , vol.59 , pp. 264-267
    • Stewart, G.L.1    Read, C.P.2
  • 45
    • 0023757412 scopus 로고
    • Collection of newborn larvae of Trichinella spiralis in vitro
    • TAKADA, N. & TADA, T. (1988). Collection of newborn larvae of Trichinella spiralis in vitro. Japan Journal of Parasitology 37, 251-253.
    • (1988) Japan Journal of Parasitology , vol.37 , pp. 251-253
    • Takada, N.1    Tada, T.2
  • 46
    • 0031052281 scopus 로고    scopus 로고
    • Folate-based thymidylate synthase inhibitors in cancer chemotherapy
    • TAKEMURA, Y. & JACKMAN, A. L. (1997). Folate-based thymidylate synthase inhibitors in cancer chemotherapy. Anti-Cancer Drugs 8, 3-16.
    • (1997) Anti-cancer Drugs , vol.8 , pp. 3-16
    • Takemura, Y.1    Jackman, A.L.2
  • 47
    • 0025912077 scopus 로고
    • Purification and characterization of thymidine kinase from regenerating rat liver
    • TSUKAMOTO, I., TANIGUCHI, Y., MIYOSHI, M. & KOJO, S. (1991). Purification and characterization of thymidine kinase from regenerating rat liver. Biochimica et Biophysica Acta 1079, 348-352.
    • (1991) Biochimica et Biophysica Acta , vol.1079 , pp. 348-352
    • Tsukamoto, I.1    Taniguchi, Y.2    Miyoshi, M.3    Kojo, S.4
  • 48
    • 0020581181 scopus 로고
    • Mitogen induction of deoxyuridine triphosphatase activity in human T and B lymphocytes
    • VILPO, J. A. (1983). Mitogen induction of deoxyuridine triphosphatase activity in human T and B lymphocytes. Medical Biology 61, 54-58.
    • (1983) Medical Biology , vol.61 , pp. 54-58
    • Vilpo, J.A.1
  • 49
    • 0018722112 scopus 로고
    • Changes in activities of thymidylate synthetase and dihydrofolate reductase in sea urchin eggs after fertilization
    • YASUMASU, I., SAITOH, M., FUJIMOTO, N. & KUSUNOKI, S. (1979). Changes in activities of thymidylate synthetase and dihydrofolate reductase in sea urchin eggs after fertilization. Development Growth and Differentiation 21, 237-243.
    • (1979) Development Growth and Differentiation , vol.21 , pp. 237-243
    • Yasumasu, I.1    Saitoh, M.2    Fujimoto, N.3    Kusunoki, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.