메뉴 건너뛰기




Volumn 41, Issue 9, 1997, Pages 1922-1925

Alterations in ornithine decarboxylase characteristics account for tolerance of Trypanosoma brucei rhodesiense to D,L-α- difluoromethylornithine

Author keywords

[No Author keywords available]

Indexed keywords

EFLORNITHINE; ORNITHINE DECARBOXYLASE;

EID: 0030824384     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.41.9.1922     Document Type: Article
Times cited : (84)

References (26)
  • 2
    • 0024353538 scopus 로고
    • Trypanosoma brucei brucei: Regulation of ornithine decarboxylase in procyclic forms and trypomastigotes
    • Bacchi, C. J., J. Garofalo, A. Santana, J. C. Hannan, A. J. Bitonti, and P. P. McCann. 1989. Trypanosoma brucei brucei: regulation of ornithine decarboxylase in procyclic forms and trypomastigotes. Exp. Parasitol. 68:392-402.
    • (1989) Exp. Parasitol. , vol.68 , pp. 392-402
    • Bacchi, C.J.1    Garofalo, J.2    Santana, A.3    Hannan, J.C.4    Bitonti, A.J.5    McCann, P.P.6
  • 4
    • 0027182786 scopus 로고
    • Resistance to DL-α-difluoromethylornithine by clinical isolates of Trypanosoma brucei rhodesiense: Role of S-adenosylmethionine
    • Bacchi, C. J., J. Garofalo, M. Ciminelli, D. Rattendi, B. Goldberg, P. P. McCann, and N. Yarlett. 1993. Resistance to DL-α-difluoromethylornithine by clinical isolates of Trypanosoma brucei rhodesiense: role of S-adenosylmethionine. Biochem. Pharmacol. 46:471-481.
    • (1993) Biochem. Pharmacol. , 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
  • 6
    • 0000146018 scopus 로고
    • Cultivation in a semidefined medium of animal infective forms of Trypanosoma brucei, T. equiperdum, T. evansi, T. rhodesiense and T. gambiense
    • Baltz, T., D. Blatz, Ch. Giroud, and J. Crockett. 1985. Cultivation in a semidefined medium of animal infective forms of Trypanosoma brucei, T. equiperdum, T. evansi, T. rhodesiense and T. gambiense. EMBO J. 4:1273-1277.
    • (1985) EMBO J. , vol.4 , pp. 1273-1277
    • Baltz, T.1    Blatz, D.2    Giroud, Ch.3    Crockett, J.4
  • 7
    • 0023431045 scopus 로고
    • Biochemical changes associated with α-difluoromethylornithine uptake and resistance in Trypanosoma brucei
    • 6b. Bellofatto, V., A. A. Fairlamb, G. B. Henderson, and G. A. M. Cross. 1987. Biochemical changes associated with α-difluoromethylornithine uptake and resistance in Trypanosoma brucei. Mol. Biochem. Parasitol. 25:227-238.
    • (1987) Mol. Biochem. Parasitol. , vol.25 , pp. 227-238
    • Bellofatto, V.1    Fairlamb, A.A.2    Henderson, G.B.3    Cross, G.A.M.4
  • 8
  • 9
    • 0024806946 scopus 로고
    • In vitro drug sensitivity test for Trypanosoma brucei subgroup bloodstream trypomastigotes
    • Brun, R., and C. Kunz. 1989. In vitro drug sensitivity test for Trypanosoma brucei subgroup bloodstream trypomastigotes. Acta Trop. 46:361-368.
    • (1989) Acta Trop. , vol.46 , pp. 361-368
    • Brun, R.1    Kunz, C.2
  • 10
    • 0017913362 scopus 로고
    • Polyamine compartimentalization in various human disease states
    • Cooper, K. D., J. B. Shukla, and O. M. Rennert. 1978. Polyamine compartimentalization in various human disease states. Clin. Chim. Acta 82:1-7.
    • (1978) Clin. Chim. Acta , vol.82 , pp. 1-7
    • Cooper, K.D.1    Shukla, J.B.2    Rennert, O.M.3
  • 11
    • 0028936760 scopus 로고
    • Degradation of ornithine decarboxylase by the mammalian and yeast 26S proteasome complexes requires all the components of the protease
    • Elias, S., B. Bercovich, C. Kahana, P. Coffino, M. Fischer, W. Hilt, D. H. Wolf, and A. Cicchanover. 1995. Degradation of ornithine decarboxylase by the mammalian and yeast 26S proteasome complexes requires all the components of the protease. Eur. J. Biochem. 229:276-283.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 276-283
    • Elias, S.1    Bercovich, B.2    Kahana, C.3    Coffino, P.4    Fischer, M.5    Hilt, W.6    Wolf, D.H.7    Cicchanover, A.8
  • 12
    • 0025350785 scopus 로고
    • Differentiation of Trypanosoma brucei trypomastigotes from long slender to short stumpy-like forms in axcnic culture
    • Hamm, B., A. Schindler, D. Mecke, and M. Duszenko. 1990. Differentiation of Trypanosoma brucei trypomastigotes from long slender to short stumpy-like forms in axcnic culture. Mol. Biochem. Parasitol. 40:13-22.
    • (1990) Mol. Biochem. Parasitol. , vol.40 , pp. 13-22
    • Hamm, B.1    Schindler, A.2    Mecke, D.3    Duszenko, M.4
  • 13
    • 0029122226 scopus 로고
    • Innate lack of susceptibility of Ugandan Trypanosoma brucei rhodesiense to DL-α - difluoromethylornithine (DFMO)
    • Iten, M., E. Matovu, R. Brun, and R. Kaminsky. 1995. Innate lack of susceptibility of Ugandan Trypanosoma brucei rhodesiense to DL-α - difluoromethylornithine (DFMO). Trop. Med. Parasitol. 46:190-194.
    • (1995) Trop. Med. Parasitol. , vol.46 , pp. 190-194
    • Iten, M.1    Matovu, E.2    Brun, R.3    Kaminsky, R.4
  • 14
    • 0024343595 scopus 로고
    • Trypanosoma brucei brucei: Expression of drug resistance in vitro
    • Kaminsky, R., F. Chuma, and E. Zweygarth. 1989. Trypanosoma brucei brucei: expression of drug resistance in vitro. Exp. Parasitol. 69:281-289.
    • (1989) Exp. Parasitol. , vol.69 , pp. 281-289
    • Kaminsky, R.1    Chuma, F.2    Zweygarth, E.3
  • 15
    • 0014884946 scopus 로고
    • Isolation of salivarian trypanosomes from man and other mammals using DEAE-cellulose
    • Lanham, S. M., and D. G. Godfrey. 1970. Isolation of salivarian trypanosomes from man and other mammals using DEAE-cellulose. Exp. Parasitol. 28:521-534.
    • (1970) Exp. Parasitol. , vol.28 , pp. 521-534
    • Lanham, S.M.1    Godfrey, D.G.2
  • 16
    • 0019820244 scopus 로고
    • Epidemiological studies on the animal reservoir of gambiense sleeping sickness. Part I. Review of literature and description of the study areas
    • Mehlitz, D., U. Brinkmann, and L. Haller. 1981. Epidemiological studies on the animal reservoir of gambiense sleeping sickness. Part I. Review of literature and description of the study areas. Tropenmed. Parasitol. 32:129-133.
    • (1981) Tropenmed. Parasitol. , vol.32 , pp. 129-133
    • Mehlitz, D.1    Brinkmann, U.2    Haller, L.3
  • 17
    • 0004713598 scopus 로고
    • Catalytic irreversible inhibition of mammalian ornithine decarboxylase (E.C.4.1.1.17) by substrate and product analogues
    • Metcalf, B. W., P. Bey, C. Danzin, M. J. Jung, P. Casara, and J. P. Vevert. 1978. Catalytic irreversible inhibition of mammalian ornithine decarboxylase (E.C.4.1.1.17) by substrate and product analogues. J. Am. Chem. Soc. 100: 2551-2553.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 2551-2553
    • Metcalf, B.W.1    Bey, P.2    Danzin, C.3    Jung, M.J.4    Casara, P.5    Vevert, J.P.6
  • 18
    • 0027234946 scopus 로고
    • Eflornithine concentrations in serum and cerebrospinal fluid of 63 patients treated for Trypanosoma brucei gambiense sleeping sickness
    • Milord, F., L. Loko, L. Ethier, B. Mpia, and J. Pépin. 1993. Eflornithine concentrations in serum and cerebrospinal fluid of 63 patients treated for Trypanosoma brucei gambiense sleeping sickness. Trans. R. Soc. Trop. Med. Hyg. 87:473-477.
    • (1993) Trans. R. Soc. Trop. Med. Hyg. , vol.87 , pp. 473-477
    • Milord, F.1    Loko, L.2    Ethier, L.3    Mpia, B.4    Pépin, J.5
  • 19
    • 0026776758 scopus 로고
    • Destabilization of ornithine decarboxylase by transfected antizyme gene expression in hepatoma tissue culture cells
    • Murakami, Y., S. Matsufuji, Y. Miyazaki, and S. Hayash. 1992. Destabilization of ornithine decarboxylase by transfected antizyme gene expression in hepatoma tissue culture cells. J. Biol. Chem. 267:13138-13141.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13138-13141
    • Murakami, Y.1    Matsufuji, S.2    Miyazaki, Y.3    Hayash, S.4
  • 21
    • 0023219692 scopus 로고
    • Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei
    • Phillips, M. A., P. Coffino, and C. C. Wang. 1987. Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei. J. Biol. Chem. 262:8721-8727.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8721-8727
    • Phillips, M.A.1    Coffino, P.2    Wang, C.C.3
  • 22
    • 0023108444 scopus 로고
    • A Trypanosoma brucei mutant resistant to α-difluoromethylornithine
    • Phillips, M. A., and C. C. Wang. 1987. A Trypanosoma brucei mutant resistant to α-difluoromethylornithine. Mol. Biol. Parasitol. 22:9-17.
    • (1987) Mol. Biol. Parasitol. , vol.22 , pp. 9-17
    • Phillips, M.A.1    Wang, C.C.2
  • 23
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S., R. Wells, and M. Rechsteiner. 1986. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234: 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 24
    • 0031035013 scopus 로고    scopus 로고
    • Cloning of a trypanosomatid gene coding for an ornithine decarboxylase that is metabolically unstable even though it lacks the C-terminal degradation domain
    • Svensson, F., C. Ceriani, E. L. Wallström, I. Kockum, I. D. Algranati, O. Heby, and L. Persson. 1997. Cloning of a trypanosomatid gene coding for an ornithine decarboxylase that is metabolically unstable even though it lacks the C-terminal degradation domain. Proc. Natl. Acad. Sci. USA 94:397-402.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 397-402
    • Svensson, F.1    Ceriani, C.2    Wallström, E.L.3    Kockum, I.4    Algranati, I.D.5    Heby, O.6    Persson, L.7
  • 26
    • 0022194481 scopus 로고
    • Treatment of gambiense sleeping sickness in the Sudan with oral DFMO (DL-α-difluoromethylornithine), an inhibitor of ornithine decarboxylase; first field trial
    • Van Nieuwenhove, S., P. J. Schechter, J. Declercq, G. Bone, J. Burke, and A. Sjoerdsma. 1985. Treatment of gambiense sleeping sickness in the Sudan with oral DFMO (DL-α-difluoromethylornithine), an inhibitor of ornithine decarboxylase; first field trial. Trans. R. Soc. Trop. Med. Hyg. 79:692-698.
    • (1985) Trans. R. Soc. Trop. Med. Hyg. , vol.79 , pp. 692-698
    • Van Nieuwenhove, S.1    Schechter, P.J.2    Declercq, J.3    Bone, G.4    Burke, J.5    Sjoerdsma, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.