메뉴 건너뛰기




Volumn 720, Issue , 2011, Pages 309-326

Genetic and Biochemical Analysis of Protozoal Polyamine Transporters

Author keywords

Confocal microscopy; Diamines; Leishmania; Localization; Parasites; Polyamines; Transporters; Trypanosoma cruzi

Indexed keywords

CARRIER PROTEIN; COMPLEMENTARY RNA; POLYAMINE; PROTOZOAL PROTEIN;

EID: 79956220791     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-61779-034-8_19     Document Type: Chapter
Times cited : (14)

References (21)
  • 1
    • 0023098372 scopus 로고
    • Decarboxylation of alpha-difluoromethylornithine by ornithine decarboxylase
    • Pegg AE, McGovern KA, Wiest L (1987) Decarboxylation of alpha-difluoromethylornithine by ornithine decarboxylase. Biochem J 241:305–307
    • (1987) Biochem J , vol.241 , pp. 305-307
    • Pegg, A.E.1    McGovern, K.A.2    Wiest, L.3
  • 3
    • 0038639784 scopus 로고    scopus 로고
    • Eflornithine for the treatment of human African trypanosomiasis
    • Supp 1
    • Burri C, Brun R (2003) Eflornithine for the treatment of human African trypanosomiasis. Parasitol Res 90(Supp 1):S49–S52
    • (2003) Parasitol Res , vol.90 , pp. S49-S52
    • Burri, C.1    Brun, R.2
  • 4
    • 0028366196 scopus 로고
    • The treatment of human African trypanosomiasis
    • Pepin J, Milord F (1994) The treatment of human African trypanosomiasis. Adv Parasitol 33:1–47
    • (1994) Adv Parasitol , vol.33 , pp. 1-47
    • Pepin, J.1    Milord, F.2
  • 5
    • 0022194481 scopus 로고
    • Treatment of gambiense sleeping sickness in the Sudan with oral DFMO (DL-alpha-difluoromethylornithine), an inhibitor of ornithine decarboxylase
    • first field trial
    • Van Nieuwenhove S, Schechter PJ, Declercq J, Bone G, Burke J, Sjoerdsma A (1985) Treatment of gambiense sleeping sickness in the Sudan with oral DFMO (DL-alpha-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
  • 7
    • 0025180260 scopus 로고
    • Cure of Trypanosoma brucei brucei and Trypanosoma brucei rhodesiense infections in mice with an irreversible inhibitor of S-adenosylmethionine decarboxylase
    • Bitonti AJ, Byers TL, Bush TL, Casara PJ, Bacchi CJ, Clarkson AB Jr, McCann PP, Sjoerdsma A (1990) Cure of Trypanosoma brucei brucei and Trypanosoma brucei rhodesiense infections in mice with an irreversible inhibitor of S-adenosylmethionine decarboxylase. Antimicrob Agents Chemother 34:1485–1490
    • (1990) Antimicrob Agents Chemother , vol.34 , pp. 1485-1490
    • Bitonti, A.J.1    Byers, T.L.2    Bush, T.L.3    Casara, P.J.4    Bacchi, C.J.5    Clarkson, A.B.6    McCann, P.P.7    Sjoerdsma, A.8
  • 8
    • 0022454288 scopus 로고
    • Characterization of Trypanosoma brucei brucei S-adenosyl-L-methionine decarboxylase and its inhibition by Berenil, pentamidine and methylglyoxal bis(guanylhydrazone)
    • Bitonti AJ, Dumont JA, McCann PP (1986) Characterization of Trypanosoma brucei brucei S-adenosyl-L-methionine decarboxylase and its inhibition by Berenil, pentamidine and methylglyoxal bis(guanylhydrazone). Biochem J 237:685–689
    • (1986) Biochem J , vol.237 , pp. 685-689
    • Bitonti, A.J.1    Dumont, J.A.2    McCann, P.P.3
  • 9
    • 0024999490 scopus 로고
    • Irreversible inhibition of rat S-adenosylmethionine decarboxylase by 5’-([(Z)-4-amino-2-butenyl] methylamino)-5’-deoxyadenosine
    • Danzin C, Marchal P, Casara P (1990) Irreversible inhibition of rat S-adenosylmethionine decarboxylase by 5’-([(Z)-4-amino-2-butenyl] methylamino)-5’-deoxyadenosine. Biochem Pharmacol 40:1499–1503
    • (1990) Biochem Pharmacol , vol.40 , pp. 1499-1503
    • Danzin, C.1    Marchal, P.2    Casara, P.3
  • 10
    • 0025812791 scopus 로고
    • Leishmania infantum: Polyamine biosynthesis and levels during the growth of pro-mastigotes
    • Balana-Fouce R, Escribano MI, Alunda JM (1991) Leishmania infantum: polyamine biosynthesis and levels during the growth of pro-mastigotes. Int J Biochem 23:1213–1217
    • (1991) Int J Biochem , vol.23 , pp. 1213-1217
    • Balana-Fouce, R.1    Escribano, M.I.2    Alunda, J.M.3
  • 11
    • 0031057528 scopus 로고    scopus 로고
    • Diamine auxotrophy may be a universal feature of Trypanosoma cruzi epimastigotes
    • Ariyanayagam MR, Fairlamb AH (1997) Diamine auxotrophy may be a universal feature of Trypanosoma cruzi epimastigotes. Mol Biochem Parasitol 84:111–121
    • (1997) Mol Biochem Parasitol , vol.84 , pp. 111-121
    • Ariyanayagam, M.R.1    Fairlamb, A.H.2
  • 12
    • 0033049344 scopus 로고    scopus 로고
    • Trypanosoma cruzi epimastigotes lack ornithine decarboxylase but can express a foreign gene encoding this enzyme
    • Carrillo C, Cejas S, Gonzalez NS, Algranati ID (1999) Trypanosoma cruzi epimastigotes lack ornithine decarboxylase but can express a foreign gene encoding this enzyme. FEBS Lett 454:192–196
    • (1999) FEBS Lett , vol.454 , pp. 192-196
    • Carrillo, C.1    Cejas, S.2    Gonzalez, N.S.3    Algranati, I.D.4
  • 13
    • 0026664221 scopus 로고
    • Poly(A)+ RNA from rabbit intestinal mucosa induces b0,+ and y+ amino acid transport activities in Xenopus laevis oocytes
    • Magagnin S, Bertran J, Werner A, Markovich D, Biber J, Palacin M, Murer H (1992) Poly(A)+ RNA from rabbit intestinal mucosa induces b0,+ and y+ amino acid transport activities in Xenopus laevis oocytes. J Biol Chem 267:15384–15390
    • (1992) J Biol Chem , vol.267 , pp. 15384-15390
    • Magagnin, S.1    Bertran, J.2    Werner, A.3    Markovich, D.4    Biber, J.5    Palacin, M.6    Murer, H.7
  • 14
    • 0037077260 scopus 로고    scopus 로고
    • Six related nucleoside/ nucleobase transporters from Trypanosoma brucei exhibit distinct biochemical functions
    • Sanchez MA, Tryon R, Green J, Boor I, Landfear SM (2002) Six related nucleoside/ nucleobase transporters from Trypanosoma brucei exhibit distinct biochemical functions. J Biol Chem 277:21499–21504
    • (2002) J Biol Chem , vol.277 , pp. 21499-21504
    • Sanchez, M.A.1    Tryon, R.2    Green, J.3    Boor, I.4    Landfear, S.M.5
  • 15
    • 17644403556 scopus 로고    scopus 로고
    • Identification and characterization of a polyamine permease from the protozoan parasite Leishmania major
    • Hasne MP, Ullman B (2005) Identification and characterization of a polyamine permease from the protozoan parasite Leishmania major. J Biol Chem 280:15188–15194
    • (2005) J Biol Chem , vol.280 , pp. 15188-15194
    • Hasne, M.P.1    Ullman, B.2
  • 17
    • 0343267840 scopus 로고    scopus 로고
    • Use of the green fluorescent protein as a marker in transfected Leishmania
    • Ha DS, Schwarz JK, Turco SJ, Beverley SM (1996) Use of the green fluorescent protein as a marker in transfected Leishmania. Mol Biochem Parasitol 77:57–64
    • (1996) Mol Biochem Parasitol , vol.77 , pp. 57-64
    • Ha, D.S.1    Schwarz, J.K.2    Turco, S.J.3    Beverley, S.M.4
  • 18
    • 0027969338 scopus 로고
    • Gene expression mediated by bacteriophage T3 and T7 RNA polymerases in transgenic trypanosomes
    • Wirtz E, Hartmann C, Clayton C (1994) Gene expression mediated by bacteriophage T3 and T7 RNA polymerases in transgenic trypanosomes. Nucleic Acids Res 22:3887–3894
    • (1994) Nucleic Acids Res , vol.22 , pp. 3887-3894
    • Wirtz, E.1    Hartmann, C.2    Clayton, C.3
  • 19
    • 0026673614 scopus 로고
    • A shuttle vector which facilitates the expression of transfected genes in Trypanosoma cruzi and Leishmania
    • Kelly JM, Ward HM, Miles MA, Kendall G (1992) A shuttle vector which facilitates the expression of transfected genes in Trypanosoma cruzi and Leishmania. Nucleic Acids Res 20:3963–3969
    • (1992) Nucleic Acids Res , vol.20 , pp. 3963-3969
    • Kelly, J.M.1    Ward, H.M.2    Miles, M.A.3    Kendall, G.4
  • 20
    • 4644292892 scopus 로고    scopus 로고
    • A functional aquaporin co-localizes with the vacuolar proton pyrophosphatase to acidocal-cisomes and the contractile vacuole complex of Trypanosoma cruzi
    • Montalvetti A, Rohloff P, Docampo R (2004) A functional aquaporin co-localizes with the vacuolar proton pyrophosphatase to acidocal-cisomes and the contractile vacuole complex of Trypanosoma cruzi. J Biol Chem 279: 38673–38682
    • (2004) J Biol Chem , vol.279 , pp. 38673-38682
    • Montalvetti, A.1    Rohloff, P.2    Docampo, R.3
  • 21
    • 0027327563 scopus 로고
    • Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family
    • Arriza JL, Kavanaugh MP, Fairman WA, Wu YN, Murdoch GH, North RA, Amara SG (1993) Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J Biol Chem 268:15329–15332
    • (1993) J Biol Chem , vol.268 , pp. 15329-15332
    • Arriza, J.L.1    Kavanaugh, M.P.2    Fairman, W.A.3    Wu, Y.N.4    Murdoch, G.H.5    North, R.A.6    Amara, S.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.