메뉴 건너뛰기




Volumn 396, Issue 2, 2010, Pages 194-203

Development and validation of a cytochrome c-coupled assay for pteridine reductase 1 and dihydrofolate reductase

Author keywords

Dihydrofolate reductase; Drug discovery; Pteridine reductase; Screening

Indexed keywords

SCREENING;

EID: 70449729390     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.09.003     Document Type: Article
Times cited : (25)

References (46)
  • 2
    • 0032441598 scopus 로고    scopus 로고
    • Drug development output from 1975 to 1996: what proportion for tropical diseases?
    • Trouiller O., and Olliaro P.L. Drug development output from 1975 to 1996: what proportion for tropical diseases?. Intl. J. Infect. Dis. 3 (1999) 61-63
    • (1999) Intl. J. Infect. Dis. , vol.3 , pp. 61-63
    • Trouiller, O.1    Olliaro, P.L.2
  • 3
    • 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., and Beverley S. New approaches to Leishmania chemotherapy: Pteridine reductase 1 (PTR1) as a target and modulator of antifolate sensitivity. Parasitology 114 (1997) 101-110
    • (1997) Parasitology , vol.114 , pp. 101-110
    • Nare, B.1    Luba, J.2    Hardy, L.W.3    Beverley, S.4
  • 6
    • 38049148752 scopus 로고    scopus 로고
    • The role of the mitochondrial glycine cleavage complex in the metabolism and virulence of the protozoan parasite Leishmania major
    • Scott D.A., Hickerson S.M., Vickers T.J., and Beverley S.M. The role of the mitochondrial glycine cleavage complex in the metabolism and virulence of the protozoan parasite Leishmania major. J. Biol. Chem. 283 (2008) 155-165
    • (2008) J. Biol. Chem. , vol.283 , pp. 155-165
    • Scott, D.A.1    Hickerson, S.M.2    Vickers, T.J.3    Beverley, S.M.4
  • 7
    • 0025882658 scopus 로고
    • Double targeted gene replacement for creating null mutants
    • Cruz A., Coburn C.M., and Beverley S.M. Double targeted gene replacement for creating null mutants. Proc. Natl. Acad. Sci. USA 88 (1991) 7170-7174
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7170-7174
    • Cruz, A.1    Coburn, C.M.2    Beverley, S.M.3
  • 8
    • 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., and Fairlamb A.H. Chemical and genetic validation of dihydrofolate reductase-thymidylate synthase as a drug target in African trypanosomes. Mol. Microbiol. 69 (2008) 520-533
    • (2008) Mol. Microbiol. , vol.69 , pp. 520-533
    • Sienkiewicz, N.1    Jaroslawski, S.2    Wyllie, S.3    Fairlamb, A.H.4
  • 10
    • 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., and Beverley S.M. PTR1: a reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major. Proc. Natl. Acad. Sci. USA 91 (1994) 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
  • 11
    • 0030946111 scopus 로고    scopus 로고
    • The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major
    • Nare B., Hardy L.W., and Beverley S.M. The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major. J. Biol. Chem. 272 (1997) 13883-13891
    • (1997) J. Biol. Chem. , vol.272 , pp. 13883-13891
    • Nare, B.1    Hardy, L.W.2    Beverley, S.M.3
  • 12
    • 0030599418 scopus 로고    scopus 로고
    • Leishmania donovani possess a NADPH-dependent alkylglycerol cleavage enzyme
    • Ma D.Q., Beverley S.M., and Turco S.J. Leishmania donovani possess a NADPH-dependent alkylglycerol cleavage enzyme. Biochem. Biophys. Res. Commun. 227 (1996) 885-889
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 885-889
    • Ma, D.Q.1    Beverley, S.M.2    Turco, S.J.3
  • 14
    • 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., and Beverley S.M. Regulation of differentiation to the infective stage of the protozoan parasite Leishmania major by tetrahydrobiopterin. Science 292 (2001) 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
  • 17
    • 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. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0035815312 scopus 로고    scopus 로고
    • Pteridine salvage throughout the Leishmania infectious cycle: Implications for antifolate chemotherapy
    • Cunningham M.L., and Beverley S.M. Pteridine salvage throughout the Leishmania infectious cycle: Implications for antifolate chemotherapy. Mol. Biochem. Parasitol. 113 (2001) 199-213
    • (2001) Mol. Biochem. Parasitol. , vol.113 , pp. 199-213
    • Cunningham, M.L.1    Beverley, S.M.2
  • 19
    • 0018868814 scopus 로고
    • Analysis of reduced forms of biopterin in biological tissues and fluids
    • Fukushima T., and Nixon J.C. Analysis of reduced forms of biopterin in biological tissues and fluids. Anal. Biochem. 102 (1980) 176-188
    • (1980) Anal. Biochem. , vol.102 , pp. 176-188
    • Fukushima, T.1    Nixon, J.C.2
  • 20
    • 0002556548 scopus 로고
    • Chemistry of naturally occurring pterins
    • Blakeley R.L., and Benkovic S.J. (Eds), John Wiley, New York
    • Pfleiderer W. Chemistry of naturally occurring pterins. In: Blakeley R.L., and Benkovic S.J. (Eds). Chemistry and Biochemistry of Pterins (1985), John Wiley, New York 43-114
    • (1985) Chemistry and Biochemistry of Pterins , pp. 43-114
    • Pfleiderer, W.1
  • 21
    • 0003076967 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data, Joint CCP4 + ESF - EAMCB
    • Leslie A.G.W. Recent changes to the MOSFLM package for processing film and image plate data, Joint CCP4 + ESF - EAMCB. Newslett. Protein Crystallogr. 26 (1992) 1-10
    • (1992) Newslett. Protein Crystallogr. , vol.26 , pp. 1-10
    • Leslie, A.G.W.1
  • 23
    • 0028103275 scopus 로고
    • 4, The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project no
    • Collaborative Computational Project no. 4, The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D 50 (1994) 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 24
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin A., and Teplyakov A. An approach to multi-copy search in molecular replacement. Acta Crystallogr. D 56 (2000) 1622-1624
    • (2000) Acta Crystallogr. D , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 25
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 26
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: a tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf A.W., and van Aalten D.M. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D 60 (2004) 1355-1363
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    van Aalten, D.M.2
  • 27
    • 13244281317 scopus 로고    scopus 로고
    • COOT: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. COOT: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 28
    • 0014454095 scopus 로고
    • Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
    • Morrison J.F. Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors. Biochem. Biophys. Acta 185 (1969) 269-286
    • (1969) Biochem. Biophys. Acta , vol.185 , pp. 269-286
    • Morrison, J.F.1
  • 29
    • 0018699952 scopus 로고
    • The kinetics of reversible tight-binding inhibition
    • Williams J.W., and Morrison J.F. The kinetics of reversible tight-binding inhibition. Methods Enzymol. 63 (1979) 437-467
    • (1979) Methods Enzymol. , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2
  • 30
    • 0034657809 scopus 로고    scopus 로고
    • High-throughput screening of enzyme inhibitors: automatic determination of tight-binding inhibition constants
    • Kuzmic P., Sideris S., Cregar L.M., Elrod K.C., Rice K.D., and Janc J.W. High-throughput screening of enzyme inhibitors: automatic determination of tight-binding inhibition constants. Anal. Biochem. 281 (2000) 62-67
    • (2000) Anal. Biochem. , vol.281 , pp. 62-67
    • Kuzmic, P.1    Sideris, S.2    Cregar, L.M.3    Elrod, K.C.4    Rice, K.D.5    Janc, J.W.6
  • 31
    • 0034327782 scopus 로고    scopus 로고
    • High-throughput enzyme kinetics: Simultaneous determination of tight-binding inhibition constants and enzyme concentration
    • Kuzmic P., Elrod K.C., Cregar L.M., Sideris S., Rai R., and Janc J.W. High-throughput enzyme kinetics: Simultaneous determination of tight-binding inhibition constants and enzyme concentration. Anal. Biochem. 286 (2000) 45-50
    • (2000) Anal. Biochem. , vol.286 , pp. 45-50
    • Kuzmic, P.1    Elrod, K.C.2    Cregar, L.M.3    Sideris, S.4    Rai, R.5    Janc, J.W.6
  • 33
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of nonlinear parameters
    • Marquardt D.W. An algorithm for least-squares estimation of nonlinear parameters. J. Soc. Ind. Appl. Math. 11 (1963) 431-441
    • (1963) J. Soc. Ind. Appl. Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 34
    • 1642505558 scopus 로고    scopus 로고
    • Practical robust fit of enzyme inhibition data
    • Kuzmic P. Practical robust fit of enzyme inhibition data. Methods Enzymol. 383 (2004) 366-381
    • (2004) Methods Enzymol. , vol.383 , pp. 366-381
    • Kuzmic, P.1
  • 36
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang J.-H., Chung T.D.Y., and Oldenburg K.R. A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J. Biomol. Screen. 4 (1999) 67-73
    • (1999) J. Biomol. Screen. , vol.4 , pp. 67-73
    • Zhang, J.-H.1    Chung, T.D.Y.2    Oldenburg, K.R.3
  • 37
    • 0018176784 scopus 로고
    • Stoichiometric studies on the oxidation of tetrahydropterin with ferri-cytochrome c
    • Hasegawa H., Nakanishi N., and Akino M. Stoichiometric studies on the oxidation of tetrahydropterin with ferri-cytochrome c. J. Biochem. (Tokyo) 84 (1978) 499-506
    • (1978) J. Biochem. (Tokyo) , vol.84 , pp. 499-506
    • Hasegawa, H.1    Nakanishi, N.2    Akino, M.3
  • 39
    • 0033179199 scopus 로고    scopus 로고
    • Mutant PTR1 proteins from Leishmania tarentolae: Comparative kinetic properties and active-site labeling
    • Chang C.-F., Bray T., and Whiteley J.M. Mutant PTR1 proteins from Leishmania tarentolae: Comparative kinetic properties and active-site labeling. Arch. Biochem. Biophys. 368 (1999) 161-171
    • (1999) Arch. Biochem. Biophys. , vol.368 , pp. 161-171
    • Chang, C.-F.1    Bray, T.2    Whiteley, J.M.3
  • 42
    • 0031574462 scopus 로고    scopus 로고
    • A pteridine reductase gene ptr1 contiguous to a P-glycoprotein confers resistance to antifolates in Trypanosoma cruzi
    • Robello C., Navarro P., Castanys S., and Gamarro F. A pteridine reductase gene ptr1 contiguous to a P-glycoprotein confers resistance to antifolates in Trypanosoma cruzi. Mol. Biochem. Parasitol. 90 (1997) 525-535
    • (1997) Mol. Biochem. Parasitol. , vol.90 , pp. 525-535
    • Robello, C.1    Navarro, P.2    Castanys, S.3    Gamarro, F.4
  • 43
    • 0028308713 scopus 로고
    • Isolation and characterization of a mutant dihydrofolate reductase-thymidylate synthase from methotrexate-resistant Leishmania cells
    • Arrebola R., Olmo A., Reche P., Garvey E.P., Santi D.V., Ruiz-Perez L.M., and Gonzalez-Pacanowska D. Isolation and characterization of a mutant dihydrofolate reductase-thymidylate synthase from methotrexate-resistant Leishmania cells. J. Biol. Chem. 269 (1994) 10590-10596
    • (1994) J. Biol. Chem. , vol.269 , pp. 10590-10596
    • Arrebola, R.1    Olmo, A.2    Reche, P.3    Garvey, E.P.4    Santi, D.V.5    Ruiz-Perez, L.M.6    Gonzalez-Pacanowska, D.7
  • 44
    • 0030998431 scopus 로고    scopus 로고
    • Construction of a homodimeric dihydrofolate reductase-thymidylate synthase bifunctional enzyme
    • Trujillo M., Duncan R., and Santi D.V. Construction of a homodimeric dihydrofolate reductase-thymidylate synthase bifunctional enzyme. Prot. Eng. 10 (1997) 567-573
    • (1997) Prot. Eng. , vol.10 , pp. 567-573
    • Trujillo, M.1    Duncan, R.2    Santi, D.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.