메뉴 건너뛰기




Volumn 77, Issue 3, 2010, Pages 658-671

Trypanosoma brucei pteridine reductase 1 is essential for survival in vitro and for virulence in mice

Author keywords

[No Author keywords available]

Indexed keywords

DIGITONIN; OXIDOREDUCTASE; PTERIDINE REDUCTASE 1; PTERIN; TETRAHYDROBIOPTERIN; UNCLASSIFIED DRUG; PROTOZOAL PROTEIN; PTERIDINE REDUCTASE;

EID: 77954837542     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07236.x     Document Type: Article
Times cited : (50)

References (74)
  • 1
    • 11144327213 scopus 로고    scopus 로고
    • A doubly inducible system for RNA interference and rapid RNAi plasmid construction in Trypanosoma brucei
    • Alibu, V.P., Storm, L., Haile, S., Clayton, C. Horn, D. (2005) A doubly inducible system for RNA interference and rapid RNAi plasmid construction in Trypanosoma brucei. Mol Biochem Parasitol 139 : 75 82.
    • (2005) Mol Biochem Parasitol , vol.139 , pp. 75-82
    • Alibu, V.P.1    Storm, L.2    Haile, S.3    Clayton, C.4    Horn, D.5
  • 2
    • 0020758761 scopus 로고
    • 2H]7,8(6H)-dihydropterin and 2,6-diamino-5-iminopyrimidin-4-one with dihydropteridine reductase
    • 2H]7,8(6H)-dihydropterin and 2,6-diamino-5-iminopyrimidin-4-one with dihydropteridine reductase. Biochem J 211 : 357 361.
    • (1983) Biochem J , vol.211 , pp. 357-361
    • Armarego, W.L.F.1    Randles, D.2    Taguchi, H.3
  • 3
    • 19344364714 scopus 로고    scopus 로고
    • Identification of trypanosomatid PEX19: Functional characterization reveals impact on cell growth and glycosome size and number
    • Banerjee, S.K., Kessler, P.S., Saveria, T. Parsons, M. (2005) Identification of trypanosomatid PEX19: functional characterization reveals impact on cell growth and glycosome size and number. Mol Biochem Parasitol 142 : 47 55.
    • (2005) Mol Biochem Parasitol , vol.142 , pp. 47-55
    • Banerjee, S.K.1    Kessler, P.S.2    Saveria, T.3    Parsons, M.4
  • 4
    • 0027996240 scopus 로고
    • PTR1: A reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major
    • Bello, A.R., Nare, B., Freedman, D., Hardy, L. Beverley, S.M. (1994) PTR1: a reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major. Proc Natl Acad Sci USA 91 : 11442 11446.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11442-11446
    • Bello, A.R.1    Nare, B.2    Freedman, D.3    Hardy, L.4    Beverley, S.M.5
  • 6
    • 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. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 : 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0026459643 scopus 로고
    • A member of the aldoketo reductase family confers methotrexate resistance in Leishmania
    • Callahan, H.L. Beverley, S.M. (1992) A member of the aldoketo reductase family confers methotrexate resistance in Leishmania. J Biol Chem 267 : 24165 24168.
    • (1992) J Biol Chem , vol.267 , pp. 24165-24168
    • Callahan, H.L.1    Beverley, S.M.2
  • 8
    • 40349108458 scopus 로고    scopus 로고
    • Discovery of potent pteridine reductase inhibitors to guide antiparasite drug development
    • Cavazzuti, A., Paglietti, G., Hunter, W.N., Gamarro, F., Piras, S., Loriga, M., et al. (2008) Discovery of potent pteridine reductase inhibitors to guide antiparasite drug development. Proc Natl Acad Sci USA 105 : 1448 1453.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1448-1453
    • Cavazzuti, A.1    Paglietti, G.2    Hunter, W.N.3    Gamarro, F.4    Piras, S.5    Loriga, M.6
  • 9
    • 0037330751 scopus 로고    scopus 로고
    • Development of RNA interference revertants in Trypanosoma brucei cell lines generated with a double stranded RNA expression construct driven by two opposing promoters
    • Chen, Y.L., Hung, C.H., Burderer, T. Lee, G.S.M. (2003) Development of RNA interference revertants in Trypanosoma brucei cell lines generated with a double stranded RNA expression construct driven by two opposing promoters. Mol Biochem Parasitol 126 : 275 279.
    • (2003) Mol Biochem Parasitol , vol.126 , pp. 275-279
    • Chen, Y.L.1    Hung, C.H.2    Burderer, T.3    Lee, G.S.M.4
  • 10
    • 0027410144 scopus 로고
    • Plasticity in chromosome number and testing of essential genes in Leishmania by targeting
    • Cruz, A.K., Titus, R. Beverley, S.M. (1993) Plasticity in chromosome number and testing of essential genes in Leishmania by targeting. Proc Natl Acad Sci USA 90 : 1599 1603.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1599-1603
    • Cruz, A.K.1    Titus, R.2    Beverley, S.M.3
  • 11
    • 0035815312 scopus 로고    scopus 로고
    • Pteridine salvage throughout the Leishmania infectious cycle: Implications for antifolate chemotherapy
    • Cunningham, M.L. Beverley, S.M. (2001) Pteridine salvage throughout the Leishmania infectious cycle: implications for antifolate chemotherapy. Mol Biochem Parasitol 113 : 199 213.
    • (2001) Mol Biochem Parasitol , vol.113 , pp. 199-213
    • Cunningham, M.L.1    Beverley, S.M.2
  • 12
    • 0035853522 scopus 로고    scopus 로고
    • Regulation of differentiation to the infective stage of the protozoan parasite Leishmania major by tetrahydrobiopterin
    • Cunningham, M.L., Titus, R.G., Turco, S.J. Beverley, S.M. (2001) Regulation of differentiation to the infective stage of the protozoan parasite Leishmania major by tetrahydrobiopterin. Science 292 : 285 287.
    • (2001) Science , vol.292 , pp. 285-287
    • Cunningham, M.L.1    Titus, R.G.2    Turco, S.J.3    Beverley, S.M.4
  • 13
    • 33748486972 scopus 로고    scopus 로고
    • Structure and reactivity of Trypanosoma brucei pteridine reductase: Inhibition by the archetypal antifolate methotrexate
    • Dawson, A., Gibellini, F., Sienkiewicz, N., Tulloch, L.B., Fyfe, P.K., McLuskey, K., et al. (2006) Structure and reactivity of Trypanosoma brucei pteridine reductase: inhibition by the archetypal antifolate methotrexate. Mol Microbiol 61 : 1457 1468.
    • (2006) Mol Microbiol , vol.61 , pp. 1457-1468
    • Dawson, A.1    Gibellini, F.2    Sienkiewicz, N.3    Tulloch, L.B.4    Fyfe, P.K.5    McLuskey, K.6
  • 14
    • 0018868814 scopus 로고
    • Analysis of reduced forms of biopterin in biological tissues and fluids
    • Fukushima, T. Nixon, J.C. (1980) Analysis of reduced forms of biopterin in biological tissues and fluids. Anal Biochem 102 : 176 188.
    • (1980) Anal Biochem , vol.102 , pp. 176-188
    • Fukushima, T.1    Nixon, J.C.2
  • 17
    • 0031282556 scopus 로고    scopus 로고
    • Biochemical and genetic tests for inhibitors of Leishmania pteridine pathways
    • Hardy, L.W., Matthews, W., Nare, B. Beverley, S.M. (1997) Biochemical and genetic tests for inhibitors of Leishmania pteridine pathways. Exp Parasitol 87 : 157 169.
    • (1997) Exp Parasitol , vol.87 , pp. 157-169
    • Hardy, L.W.1    Matthews, W.2    Nare, B.3    Beverley, S.M.4
  • 18
    • 0030845186 scopus 로고    scopus 로고
    • The dihydroxyacetonephosphate pathway for biosynthesis of ether lipids in Leishmania mexicana promastigotes
    • Heise, N. Opperdoes, F.R. (1997) The dihydroxyacetonephosphate pathway for biosynthesis of ether lipids in Leishmania mexicana promastigotes. Mol Biochem Parasitol 89 : 61 72.
    • (1997) Mol Biochem Parasitol , vol.89 , pp. 61-72
    • Heise, N.1    Opperdoes, F.R.2
  • 20
    • 64149090456 scopus 로고    scopus 로고
    • The cell cycle as a therapeutic target against Trypanosoma brucei: Hesperadin inhibits Aurora kinase-1 and blocks mitotic progression in bloodstream forms
    • Jetton, N., Rothberg, K.G., Hubbard, J.G., Wise, J., Li, Y., Ball, H.L. Ruben, L. (2009) The cell cycle as a therapeutic target against Trypanosoma brucei: hesperadin inhibits Aurora kinase-1 and blocks mitotic progression in bloodstream forms. Mol Microbiol 72 : 442 458.
    • (2009) Mol Microbiol , vol.72 , pp. 442-458
    • Jetton, N.1    Rothberg, K.G.2    Hubbard, J.G.3    Wise, J.4    Li, Y.5    Ball, H.L.6    Ruben, L.7
  • 21
    • 0024521456 scopus 로고
    • Trypanothione reductase from Trypanosoma cruzi: Catalytic properties of the enzyme and inhibition studies with trypanocidal compounds
    • Jockers-Scherubl, M.C., Schirmer, R.H. Krauth-Siegel, R.L. (1989) Trypanothione reductase from Trypanosoma cruzi: catalytic properties of the enzyme and inhibition studies with trypanocidal compounds. Eur J Biochem 180 : 267 272.
    • (1989) Eur J Biochem , vol.180 , pp. 267-272
    • Jockers-Scherubl, M.C.1    Schirmer, R.H.2    Krauth-Siegel, R.L.3
  • 22
    • 78651125086 scopus 로고
    • The structure of the phenylalanine-hydroxylation cofactor
    • Kaufman, S. (1963) The structure of the phenylalanine-hydroxylation cofactor. Proc Natl Acad Sci USA 50 : 1085 1093.
    • (1963) Proc Natl Acad Sci USA , vol.50 , pp. 1085-1093
    • Kaufman, S.1
  • 23
    • 0025316436 scopus 로고
    • Dependence of an alkyl glycol-ether monooxygenase activity upon tetrahydropterins
    • Kaufman, S., Pollock, R.J., Summer, G.K., Das, A.K. Hajra, A.K. (1990) Dependence of an alkyl glycol-ether monooxygenase activity upon tetrahydropterins. Biochim Biophys Acta 1040 : 19 27.
    • (1990) Biochim Biophys Acta , vol.1040 , pp. 19-27
    • Kaufman, S.1    Pollock, R.J.2    Summer, G.K.3    Das, A.K.4    Hajra, A.K.5
  • 24
    • 0002324004 scopus 로고
    • The growth and nutrition of Crithidia fasciulata
    • Kidder, G.W. Dutta, B.N. (1958) The growth and nutrition of Crithidia fasciulata. J Gen Microbiol 18 : 621 638.
    • (1958) J Gen Microbiol , vol.18 , pp. 621-638
    • Kidder, G.W.1    Dutta, B.N.2
  • 25
    • 32144455889 scopus 로고    scopus 로고
    • Identification and characterization of three peroxins - PEX6, PEX10 and PEX12 - Involved in glycosome biogenesis in Trypanosoma brucei
    • Krazy, H. Michels, P.A.M. (2006) Identification and characterization of three peroxins - PEX6, PEX10 and PEX12 - involved in glycosome biogenesis in Trypanosoma brucei. Biochim Biophys Acta 1763 : 6 17.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 6-17
    • Krazy, H.1    Michels, P.A.M.2
  • 26
    • 34247092486 scopus 로고    scopus 로고
    • Degradation of pteridine reductase 1 (PTR1) enzyme during growth phase in the protozoan parasite Leishmania donovani
    • Kumar, P., Sundar, S. Singh, N. (2007) Degradation of pteridine reductase 1 (PTR1) enzyme during growth phase in the protozoan parasite Leishmania donovani. Exp Parasitol 116 : 182 189.
    • (2007) Exp Parasitol , vol.116 , pp. 182-189
    • Kumar, P.1    Sundar, S.2    Singh, N.3
  • 27
    • 0242698082 scopus 로고    scopus 로고
    • Increased transport of pteridines compensates for mutations in the high affinity folate transporter and contributes to methotrexate resistance in the protozoan parasite Leishmania tarentolae
    • Kundig, C., Haimeur, A., Legare, D., Papadopoulou, B. Ouellette, M. (1999) Increased transport of pteridines compensates for mutations in the high affinity folate transporter and contributes to methotrexate resistance in the protozoan parasite Leishmania tarentolae. EMBO J 18 : 2342 2351.
    • (1999) EMBO J , vol.18 , pp. 2342-2351
    • Kundig, C.1    Haimeur, A.2    Legare, D.3    Papadopoulou, B.4    Ouellette, M.5
  • 29
    • 33746268564 scopus 로고    scopus 로고
    • Changing roles of aurora-B kinase in two life cycle stages of Trypanosoma brucei
    • Li, Z.Y. Wang, C.C. (2006) Changing roles of aurora-B kinase in two life cycle stages of Trypanosoma brucei. Eukaryotic Cell 5 : 1026 1035.
    • (2006) Eukaryotic Cell , vol.5 , pp. 1026-1035
    • Li, Z.Y.1    Wang, C.C.2
  • 30
    • 0032125799 scopus 로고    scopus 로고
    • Elongation and clustering of glycosomes in Trypanosoma brucei overexpressing the glycosomal Pex11p
    • Lorenz, P., Maier, A.G., Baumgart, E., Erdmann, R. Clayton, C. (1998) Elongation and clustering of glycosomes in Trypanosoma brucei overexpressing the glycosomal Pex11p. EMBO J 17 : 3542 3555.
    • (1998) EMBO J , vol.17 , pp. 3542-3555
    • Lorenz, P.1    Maier, A.G.2    Baumgart, E.3    Erdmann, R.4    Clayton, C.5
  • 31
    • 0000533384 scopus 로고    scopus 로고
    • Leishmania major pteridine reductase 1 belongs to the short chain dehydrogenase family: Stereochemical and kinetic evidence
    • Luba, J., Nare, B., Liang, P.H., Anderson, K.S., Beverley, S.M. Hardy, L.W. (1998) Leishmania major pteridine reductase 1 belongs to the short chain dehydrogenase family: stereochemical and kinetic evidence. Biochemistry 37 : 4093 4104.
    • (1998) Biochemistry , vol.37 , pp. 4093-4104
    • Luba, J.1    Nare, B.2    Liang, P.H.3    Anderson, K.S.4    Beverley, S.M.5    Hardy, L.W.6
  • 32
    • 0033758270 scopus 로고    scopus 로고
    • Ether-lipid (alkyl-phospholipid) metabolism and the mechanism of action of ether-lipid analogues in Leishmania
    • Lux, H., Heise, N., Klenner, T., Hart, D. Opperdoes, F.R. (2000) Ether-lipid (alkyl-phospholipid) metabolism and the mechanism of action of ether-lipid analogues in Leishmania. Mol Biochem Parasitol 111 : 1 14.
    • (2000) Mol Biochem Parasitol , vol.111 , pp. 1-14
    • Lux, H.1    Heise, N.2    Klenner, T.3    Hart, D.4    Opperdoes, F.R.5
  • 33
    • 0037064086 scopus 로고    scopus 로고
    • Characterization of quinonoid-dihydropteridine reductase (QDPR) from the lower eukaryote Leishmania major
    • Lye, L.F., Cunningham, M.L. Beverley, S.M. (2002) Characterization of quinonoid-dihydropteridine reductase (QDPR) from the lower eukaryote Leishmania major. J Biol Chem 277 : 38245 38253.
    • (2002) J Biol Chem , vol.277 , pp. 38245-38253
    • Lye, L.F.1    Cunningham, M.L.2    Beverley, S.M.3
  • 34
    • 0030599418 scopus 로고    scopus 로고
    • Leishmania donovani possess a NADPH-dependent alkylglycerol cleavage enzyme
    • Ma, D.Q., Beverley, S.M. Turco, S.J. (1996) Leishmania donovani possess a NADPH-dependent alkylglycerol cleavage enzyme. Biochem Biophys Res Commun 227 : 885 889.
    • (1996) Biochem Biophys Res Commun , vol.227 , pp. 885-889
    • Ma, D.Q.1    Beverley, S.M.2    Turco, S.J.3
  • 36
    • 0033567436 scopus 로고    scopus 로고
    • Involvement of nitric oxide and biopterin in proinflammatory cytokine-induced apoptotic cell death in mouse osteoblastic cell line MC3T3-E1
    • Mogi, M., Kinpara, K., Kondo, A. Togari, A. (1999) Involvement of nitric oxide and biopterin in proinflammatory cytokine-induced apoptotic cell death in mouse osteoblastic cell line MC3T3-E1. Biochem Pharmacol 58 : 649 654.
    • (1999) Biochem Pharmacol , vol.58 , pp. 649-654
    • Mogi, M.1    Kinpara, K.2    Kondo, A.3    Togari, A.4
  • 37
    • 58149101954 scopus 로고    scopus 로고
    • The role of reduced pterins in resistance to reactive oxygen and nitrogen intermediates in the protozoan parasite Leishmania
    • Moreira, W., Leblanc, E. Ouellette, M. (2009) The role of reduced pterins in resistance to reactive oxygen and nitrogen intermediates in the protozoan parasite Leishmania. Free Radic Biol Med 46 : 367 375.
    • (2009) Free Radic Biol Med , vol.46 , pp. 367-375
    • Moreira, W.1    Leblanc, E.2    Ouellette, M.3
  • 38
    • 0037691903 scopus 로고    scopus 로고
    • Characterization of Trypanosoma brucei PEX14 and its role in the import of glycosomal matrix proteins
    • Moyersoen, J., Choe, J., Kumar, A., Voncken, F.G.J., Hol, W.G.J. Michels, P.A.M. (2003) Characterization of Trypanosoma brucei PEX14 and its role in the import of glycosomal matrix proteins. Eur J Biochem 270 : 2059 2067.
    • (2003) Eur J Biochem , vol.270 , pp. 2059-2067
    • Moyersoen, J.1    Choe, J.2    Kumar, A.3    Voncken, F.G.J.4    Hol, W.G.J.5    Michels, P.A.M.6
  • 39
    • 67650754042 scopus 로고    scopus 로고
    • One scaffold, three binding modes: Novel and selective pteridine reductase 1 Inhibitors derived from fragment hits discovered by virtual screening
    • Mpamhanga, C.P., Spinks, D., Tulloch, L.B., Shanks, E.J., Robinson, D.A., Collie, I.T., et al. (2009) One scaffold, three binding modes: novel and selective pteridine reductase 1 Inhibitors derived from fragment hits discovered by virtual screening. J Med Chem 52 : 4454 4465.
    • (2009) J Med Chem , vol.52 , pp. 4454-4465
    • Mpamhanga, C.P.1    Spinks, D.2    Tulloch, L.B.3    Shanks, E.J.4    Robinson, D.A.5    Collie, I.T.6
  • 40
    • 0030921824 scopus 로고    scopus 로고
    • New approaches to Leishmania chemotherapy: Pteridine reductase 1 (PTR1) as a target and modulator of antifolate sensitivity
    • Nare, B., Luba, J., Hardy, L.W. Beverley, S.M. (1997) New approaches to Leishmania chemotherapy: pteridine reductase 1 (PTR1) as a target and modulator of antifolate sensitivity. Parasitol 114 : S101 S110.
    • (1997) Parasitol , vol.114
    • Nare, B.1    Luba, J.2    Hardy, L.W.3    Beverley, S.M.4
  • 41
    • 67349132416 scopus 로고    scopus 로고
    • PTR1-dependent synthesis of tetrahydrobiopterin contributes to oxidant susceptibility in the trypanosomatid protozoan parasite Leishmania major
    • Nare, B., Garraway, L.A., Vickers, T.J. Beverley, S.M. (2009) PTR1-dependent synthesis of tetrahydrobiopterin contributes to oxidant susceptibility in the trypanosomatid protozoan parasite Leishmania major. Curr Genet 55 : 287 299.
    • (2009) Curr Genet , vol.55 , pp. 287-299
    • Nare, B.1    Garraway, L.A.2    Vickers, T.J.3    Beverley, S.M.4
  • 42
    • 0242648530 scopus 로고
    • Biosynthesis of tetrahydrobiopterin by de novo and salvage pathways in adrenal-medulla extracts, mammalian-cell cultures, and rat-brain in vivo
    • Nichol, C.A., Lee, C.L., Edelstein, M.P., Chao, J.Y. Duch, D.S. (1983) Biosynthesis of tetrahydrobiopterin by de novo and salvage pathways in adrenal-medulla extracts, mammalian-cell cultures, and rat-brain in vivo. Proc Natl Acad Sci USA 80 : 1546 1550.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 1546-1550
    • Nichol, C.A.1    Lee, C.L.2    Edelstein, M.P.3    Chao, J.Y.4    Duch, D.S.5
  • 43
    • 70349974373 scopus 로고    scopus 로고
    • Cell morphogenesis of Trypanosoma brucei requires the paralogous, differentially expressed calpain-related proteins CAP5.5 and CAP5.5V
    • Olego-Fernandez, S., Vaughan, S., Shaw, M.K., Gull, K. Ginger, M.L. (2009) Cell morphogenesis of Trypanosoma brucei requires the paralogous, differentially expressed calpain-related proteins CAP5.5 and CAP5.5V. Protist 160 : 576 590.
    • (2009) Protist , vol.160 , pp. 576-590
    • Olego-Fernandez, S.1    Vaughan, S.2    Shaw, M.K.3    Gull, K.4    Ginger, M.L.5
  • 44
    • 33646074032 scopus 로고    scopus 로고
    • In silico prediction of the glycosomal enzymes of Leishmania major and trypanosomes
    • Opperdoes, F.R. Szikora, J.P. (2006) In silico prediction of the glycosomal enzymes of Leishmania major and trypanosomes. Mol Biochem Parasitol 147 : 193 206.
    • (2006) Mol Biochem Parasitol , vol.147 , pp. 193-206
    • Opperdoes, F.R.1    Szikora, J.P.2
  • 45
    • 0021142570 scopus 로고
    • Purification, morphometric analysis, and characterization of the glycosomes (microbodies) of the protozoan hemoflagellate Trypanosoma brucei
    • Opperdoes, F.R., Baudhuin, P., Coppens, I., de Roe, C., Edwards, S.W., Weijers, P.J. Misset, O. (1984) Purification, morphometric analysis, and characterization of the glycosomes (microbodies) of the protozoan hemoflagellate Trypanosoma brucei. J Cell Biol 98 : 1178 1184.
    • (1984) J Cell Biol , vol.98 , pp. 1178-1184
    • Opperdoes, F.R.1    Baudhuin, P.2    Coppens, I.3    De Roe, C.4    Edwards, S.W.5    Weijers, P.J.6    Misset, O.7
  • 48
    • 0026779424 scopus 로고
    • A novel antifolate resistance gene on the amplified H circle of Leishmania
    • Papadopoulou, B., Roy, G. Ouellette, M. (1992) A novel antifolate resistance gene on the amplified H circle of Leishmania. EMBO J 11 : 3601 3608.
    • (1992) EMBO J , vol.11 , pp. 3601-3608
    • Papadopoulou, B.1    Roy, G.2    Ouellette, M.3
  • 49
  • 50
    • 33749528009 scopus 로고    scopus 로고
    • Trypanin, a component of the flagellar dynein regulatory complex, is essential in bloodstream form African trypanosomes
    • Ralston, K.S. Hill, K.L. (2006) Trypanin, a component of the flagellar dynein regulatory complex, is essential in bloodstream form African trypanosomes. PLoS Pathog 2 : 873 882.
    • (2006) PLoS Pathog , vol.2 , pp. 873-882
    • Ralston, K.S.1    Hill, K.L.2
  • 51
    • 0345550308 scopus 로고    scopus 로고
    • Bfsp2 mutation found in mouse 129 strains causes the loss of CP49 and induces vimentin-dependent changes in the lens fibre cell cytoskeleton
    • Sandilands, A., Wang, X., Hutcheson, A.M., James, J., Prescott, A.R., Wegener, A., et al. (2004) Bfsp2 mutation found in mouse 129 strains causes the loss of CP49 and induces vimentin-dependent changes in the lens fibre cell cytoskeleton. Exp Eye Res 78 : 109 123.
    • (2004) Exp Eye Res , vol.78 , pp. 109-123
    • Sandilands, A.1    Wang, X.2    Hutcheson, A.M.3    James, J.4    Prescott, A.R.5    Wegener, A.6
  • 52
    • 17644393919 scopus 로고    scopus 로고
    • Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei
    • Schlecker, T., Schmidt, A., Dirdjaja, N., Voncken, F., Clayton, C. Krauth-Siegel, R.L. (2005) Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei. J Biol Chem 280 : 14385 14394.
    • (2005) J Biol Chem , vol.280 , pp. 14385-14394
    • Schlecker, T.1    Schmidt, A.2    Dirdjaja, N.3    Voncken, F.4    Clayton, C.5    Krauth-Siegel, R.L.6
  • 53
    • 34447536457 scopus 로고    scopus 로고
    • Mechanisms for the role of tetrahydrobiopterin in endothelial function and vascular disease
    • Schmidt, T.S. Alp, N.J. (2007) Mechanisms for the role of tetrahydrobiopterin in endothelial function and vascular disease. Clin Sci 113 : 47 63.
    • (2007) Clin Sci , vol.113 , pp. 47-63
    • Schmidt, T.S.1    Alp, N.J.2
  • 54
    • 25644437208 scopus 로고    scopus 로고
    • Crystal structure of Trypanosoma cruzi pteridine reductase 2 in complex with a substrate and an inhibitor
    • Schormann, N., Pal, B., Senkovich, O., Carson, M., Howard, A., Smith, C., et al. (2005) Crystal structure of Trypanosoma cruzi pteridine reductase 2 in complex with a substrate and an inhibitor. J Struct Biol 152 : 64 75.
    • (2005) J Struct Biol , vol.152 , pp. 64-75
    • Schormann, N.1    Pal, B.2    Senkovich, O.3    Carson, M.4    Howard, A.5    Smith, C.6
  • 55
    • 23944516742 scopus 로고    scopus 로고
    • Structures of Leishmania major pteridine reductase complexes reveal the active site features important for ligand binding and to guide inhibitor design
    • Schuttelkopf, A.W., Hardy, L.W., Beverley, S.M. Hunter, W.N. (2005) Structures of Leishmania major pteridine reductase complexes reveal the active site features important for ligand binding and to guide inhibitor design. J Mol Biol 352 : 105 116.
    • (2005) J Mol Biol , vol.352 , pp. 105-116
    • Schuttelkopf, A.W.1    Hardy, L.W.2    Beverley, S.M.3    Hunter, W.N.4
  • 57
    • 70449729390 scopus 로고    scopus 로고
    • Development and validation of a cytochrome c coupled assay for pteridine reductase 1 and dihydrofolate reductase
    • Shanks, E.J., Ong, H.B., Robinson, D.A., Thompson, S., Sienkiewicz, N., Fairlamb, A.H. Frearson, J.A. (2010) Development and validation of a cytochrome c coupled assay for pteridine reductase 1 and dihydrofolate reductase. Anal Biochem 396 : 194 203.
    • (2010) Anal Biochem , vol.396 , pp. 194-203
    • Shanks, E.J.1    Ong, H.B.2    Robinson, D.A.3    Thompson, S.4    Sienkiewicz, N.5    Fairlamb, A.H.6    Frearson, J.A.7
  • 58
    • 20844442483 scopus 로고    scopus 로고
    • Variant surface glycoprotein RNA interference triggers a precytokinesis cell cycle arrest in African trypanosomes
    • Sheader, K., Vaughan, S., Minchin, J., Hughes, K., Gull, K. Rudenko, G. (2005) Variant surface glycoprotein RNA interference triggers a precytokinesis cell cycle arrest in African trypanosomes. Proc Natl Acad Sci USA 102 : 8716 8721.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8716-8721
    • Sheader, K.1    Vaughan, S.2    Minchin, J.3    Hughes, K.4    Gull, K.5    Rudenko, G.6
  • 59
    • 47249120852 scopus 로고    scopus 로고
    • Chemical and genetic validation of dihydrofolate reductase-thymidylate synthase as a drug target in African trypanosomes
    • Sienkiewicz, N., Jaroslawski, S., Wyllie, S. Fairlamb, A.H. (2008) Chemical and genetic validation of dihydrofolate reductase-thymidylate synthase as a drug target in African trypanosomes. Mol Microbiol 69 : 520 533.
    • (2008) Mol Microbiol , vol.69 , pp. 520-533
    • Sienkiewicz, N.1    Jaroslawski, S.2    Wyllie, S.3    Fairlamb, A.H.4
  • 60
    • 0025820934 scopus 로고
    • Subcellular distribution of trypanothione reductase in bloodstream and procyclic forms of Trypanosoma brucei
    • Smith, K., Opperdoes, F.R. Fairlamb, A.H. (1991) Subcellular distribution of trypanothione reductase in bloodstream and procyclic forms of Trypanosoma brucei. Mol Biochem Parasitol 48 : 109 112.
    • (1991) Mol Biochem Parasitol , vol.48 , pp. 109-112
    • Smith, K.1    Opperdoes, F.R.2    Fairlamb, A.H.3
  • 61
    • 0034176921 scopus 로고    scopus 로고
    • Tetrahydrobiopterin biosynthesis, regeneration and functions
    • Thony, B., Auerbach, G. Blau, N. (2000) Tetrahydrobiopterin biosynthesis, regeneration and functions. Biochem J 347 : 1 16.
    • (2000) Biochem J , vol.347 , pp. 1-16
    • Thony, B.1    Auerbach, G.2    Blau, N.3
  • 62
    • 74849120225 scopus 로고    scopus 로고
    • Structure-based design of pteridine reductase inhibitors targeting African sleeping sickness and the Leishmaniases
    • Tulloch, L.B., Martini, V.P., Iulek, J., Huggan, J.K., Lee, J.H., Gibson, C.L., et al. (2010) Structure-based design of pteridine reductase inhibitors targeting African sleeping sickness and the Leishmaniases. J Med Chem 53 : 221 229.
    • (2010) J Med Chem , vol.53 , pp. 221-229
    • Tulloch, L.B.1    Martini, V.P.2    Iulek, J.3    Huggan, J.K.4    Lee, J.H.5    Gibson, C.L.6
  • 63
    • 2442436725 scopus 로고    scopus 로고
    • RNA interference in protozoan parasites
    • Ullu, E., Tschudi, C. Chakraborty, T. (2004) RNA interference in protozoan parasites. Cell Microbiol 6 : 509 519.
    • (2004) Cell Microbiol , vol.6 , pp. 509-519
    • Ullu, E.1    Tschudi, C.2    Chakraborty, T.3
  • 64
    • 60549110196 scopus 로고    scopus 로고
    • Identification, characterization and essentiality of the unusual peroxin 13 from Trypanosoma brucei
    • Verplaetse, E., Rigden, D.J. Michels, P.A.M. (2009) Identification, characterization and essentiality of the unusual peroxin 13 from Trypanosoma brucei. Biochim Biophys Acta 1793 : 516 527.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 516-527
    • Verplaetse, E.1    Rigden, D.J.2    Michels, P.A.M.3
  • 65
    • 39049118320 scopus 로고    scopus 로고
    • Differential expression of glycosomal and mitochondrial proteins in the two major life-cycle stages of Trypanosoma brucei
    • Vertommen, D., Van Roy, J., Szikora, J.P., Rider, M.H., Michels, P.A.M. Opperdoes, F.R. (2008) Differential expression of glycosomal and mitochondrial proteins in the two major life-cycle stages of Trypanosoma brucei. Mol Biochem Parasitol 158 : 189 201.
    • (2008) Mol Biochem Parasitol , vol.158 , pp. 189-201
    • Vertommen, D.1    Van Roy, J.2    Szikora, J.P.3    Rider, M.H.4    Michels, P.A.M.5    Opperdoes, F.R.6
  • 66
    • 3042641848 scopus 로고    scopus 로고
    • Trypanothione S-transferase activity in a trypanosomatid ribosomal elongation factor 1B
    • Vickers, T.J. Fairlamb, A.H. (2004) Trypanothione S-transferase activity in a trypanosomatid ribosomal elongation factor 1B. J Biol Chem 279 : 27246 27256.
    • (2004) J Biol Chem , vol.279 , pp. 27246-27256
    • Vickers, T.J.1    Fairlamb, A.H.2
  • 67
    • 0041816190 scopus 로고    scopus 로고
    • Depletion of GIM5 causes cellular fragility, a decreased glycosome number, and reduced levels of ether-linked phospholipids in trypanosomes
    • Voncken, F., Van Hellemond, J.J., Pfisterer, I., Maier, A., Hillmer, S. Clayton, C. (2003) Depletion of GIM5 causes cellular fragility, a decreased glycosome number, and reduced levels of ether-linked phospholipids in trypanosomes. J Biol Chem 278 : 35299 35310.
    • (2003) J Biol Chem , vol.278 , pp. 35299-35310
    • Voncken, F.1    Van Hellemond, J.J.2    Pfisterer, I.3    Maier, A.4    Hillmer, S.5    Clayton, C.6
  • 68
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders, R.J.A. Waterham, H.R. (2006) Biochemistry of mammalian peroxisomes revisited. Annu Rev Biochem 75 : 295 332.
    • (2006) Annu Rev Biochem , vol.75 , pp. 295-332
    • Wanders, R.J.A.1    Waterham, H.R.2
  • 69
    • 58249097083 scopus 로고    scopus 로고
    • Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence
    • Watschinger, K., Keller, M.A., Hermetter, A., Golderer, G., Werner-Felmayer, G. Werner, E.R. (2009) Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence. Biol Chem 390 : 3 10.
    • (2009) Biol Chem , vol.390 , pp. 3-10
    • Watschinger, K.1    Keller, M.A.2    Hermetter, A.3    Golderer, G.4    Werner-Felmayer, G.5    Werner, E.R.6
  • 70
    • 0036225777 scopus 로고    scopus 로고
    • Tetrahydrobiopterin biosynthesis, utilization and pharmacological effects
    • Werner-Felmayer, G., Golderer, G. Werner, E.R. (2002) Tetrahydrobiopterin biosynthesis, utilization and pharmacological effects. Curr Drug Metab 3 : 159 173.
    • (2002) Curr Drug Metab , vol.3 , pp. 159-173
    • Werner-Felmayer, G.1    Golderer, G.2    Werner, E.R.3
  • 71
    • 0028046144 scopus 로고
    • Amplification of the inosinate dehydrogenase gene in Trypanosoma brucei gambiense due to an increase in chromosome copy number
    • Wilson, K., Berens, R.L., Sifri, C.D. Ullman, B. (1994) Amplification of the inosinate dehydrogenase gene in Trypanosoma brucei gambiense due to an increase in chromosome copy number. J Biol Chem 269 : 28979 28987.
    • (1994) J Biol Chem , vol.269 , pp. 28979-28987
    • Wilson, K.1    Berens, R.L.2    Sifri, C.D.3    Ullman, B.4
  • 72
    • 0033525524 scopus 로고    scopus 로고
    • A tightly regulated inducible expression system for conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei
    • Wirtz, E., Leal, S., Ochatt, C. Cross, G.A.M. (1999) A tightly regulated inducible expression system for conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei. Mol Biochem Parasitol 99 : 89 101.
    • (1999) Mol Biochem Parasitol , vol.99 , pp. 89-101
    • Wirtz, E.1    Leal, S.2    Ochatt, C.3    Cross, G.A.M.4
  • 73
    • 0024369960 scopus 로고
    • Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies
    • Woods, A., Sherwin, T., Sasse, R., Macrae, T.H., Baines, A.J. Gull, K. (1989) Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies. J Cell Sci 93 : 491 500.
    • (1989) J Cell Sci , vol.93 , pp. 491-500
    • Woods, A.1    Sherwin, T.2    Sasse, R.3    MacRae, T.H.4    Baines, A.J.5    Gull, K.6
  • 74
    • 0033839281 scopus 로고    scopus 로고
    • Alterations of tetrahydrobiopterin biosynthesis and pteridine levels in mouse tissues during growth and aging
    • Yoshida, Y.I., Eda, S. Masada, M. (2000) Alterations of tetrahydrobiopterin biosynthesis and pteridine levels in mouse tissues during growth and aging. Brain Dev S45 S49.
    • (2000) Brain Dev
    • Yoshida, Y.I.1    Eda, S.2    Masada, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.