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Volumn 120, Issue 1, 2008, Pages 73-79

Leishmania donovani pteridine reductase 1: Biochemical properties and structure-modeling studies

Author keywords

Antileishmanial drug screening; Antileishmanial screening; Clinical isolate; DHFR TS, dihydrofolate reductase thymidylate synthase; DHPR, dihydropteridine reductase; Flow cytometry; GFP, green fluorescence protein; Leishmania donovani; MTX, methotrexate; pABA, para aminobenzoic acid; Pteridine reductase 1; PTR1, pteridine reductase 1; Recombinant protein; SAG, sodium antimony gluconate; Structural modeling

Indexed keywords

(4 FLUORO PHENYL) 6 METHYL 2 THIOXO 1,2,3,4 TETRAHYDRO PYRIMIDINE 5 CARBOXYLIC ACID ETHYL ESTER; CARBOXYLIC ACID; OXIDOREDUCTASE; OXIDOREDUCTASE INHIBITOR; PTERIDINE REDUCTASE 1; UNCLASSIFIED DRUG;

EID: 48849097750     PISSN: 00144894     EISSN: 10902449     Source Type: Journal    
DOI: 10.1016/j.exppara.2008.05.005     Document Type: Article
Times cited : (33)

References (34)
  • 2
    • 0027027467 scopus 로고
    • LUDI: rule-based automatic design of new substituents for enzyme inhibitor leads
    • Bohm H.J. LUDI: rule-based automatic design of new substituents for enzyme inhibitor leads. Journal Computer Aided Molecular Design 6 (1992) 593-606
    • (1992) Journal Computer Aided Molecular Design , vol.6 , pp. 593-606
    • Bohm, H.J.1
  • 4
    • 34247605954 scopus 로고    scopus 로고
    • DNA vaccination against the parasite enzyme gamma-glutamylcysteine synthetase confers protection against Leishmania donovani infection
    • Carter K.C., Henriquez F.L., Campbell S.A., Roberts C.W., Nok A., Mullen A.B., and McFarlane E. DNA vaccination against the parasite enzyme gamma-glutamylcysteine synthetase confers protection against Leishmania donovani infection. Vaccine 25 22 (2007) 4502-4509
    • (2007) Vaccine , vol.25 , Issue.22 , pp. 4502-4509
    • Carter, K.C.1    Henriquez, F.L.2    Campbell, S.A.3    Roberts, C.W.4    Nok, A.5    Mullen, A.B.6    McFarlane, E.7
  • 5
    • 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
  • 6
    • 18144394300 scopus 로고    scopus 로고
    • Development of a modified MTT assay for screening antimonial resistant field isolates of Indian visceral leishmaniasis
    • Dutta A., Bandyopadhyay S., Mandal C., and Chatterjee M. Development of a modified MTT assay for screening antimonial resistant field isolates of Indian visceral leishmaniasis. Parasitology International 54 (2005) 119-122
    • (2005) Parasitology International , vol.54 , pp. 119-122
    • Dutta, A.1    Bandyopadhyay, S.2    Mandal, C.3    Chatterjee, M.4
  • 7
    • 36749090119 scopus 로고    scopus 로고
    • Tetrabutylammonium hydrogensulphate catalysed efficient synthesis of glycosyl(aryl) dihydropyrimidones
    • Dwivedi N., Mishra R.C., and Tripathi R.P. Tetrabutylammonium hydrogensulphate catalysed efficient synthesis of glycosyl(aryl) dihydropyrimidones. Letters in Organic Chemistry 5 (2005) 450-457
    • (2005) Letters in Organic Chemistry , vol.5 , pp. 450-457
    • Dwivedi, N.1    Mishra, R.C.2    Tripathi, R.P.3
  • 8
    • 0029294584 scopus 로고
    • Molecular recognition of the inhibitor AG-1343 by HIV-1 protease: conformationally flexible docking by evolutionary programming
    • Gehlhaar D.K., Verkhivker G.M., Rejto P.A., Sherman C.J., Fogel D.B., Fogel L.J., and Freer S.T. Molecular recognition of the inhibitor AG-1343 by HIV-1 protease: conformationally flexible docking by evolutionary programming. Chemistry Biology 2 (1995) 317-324
    • (1995) Chemistry Biology , vol.2 , pp. 317-324
    • Gehlhaar, D.K.1    Verkhivker, G.M.2    Rejto, P.A.3    Sherman, C.J.4    Fogel, D.B.5    Fogel, L.J.6    Freer, S.T.7
  • 11
    • 0035067363 scopus 로고    scopus 로고
    • Leishmaniasis: current status of vaccine development
    • Handman E. Leishmaniasis: current status of vaccine development. Clinical Microbiology Reviews 14 (2001) 229-243
    • (2001) Clinical Microbiology Reviews , vol.14 , pp. 229-243
    • Handman, E.1
  • 12
    • 0031282556 scopus 로고    scopus 로고
    • Biochemical and genetic tests for inhibitors of Leishmania pteridine pathways
    • Hardy L.W., Matthews W., Nare B., and Beverly S.M. Biochemical and genetic tests for inhibitors of Leishmania pteridine pathways. Experimental Parasitology 87 (1997) 157-169
    • (1997) Experimental Parasitology , vol.87 , pp. 157-169
    • Hardy, L.W.1    Matthews, W.2    Nare, B.3    Beverly, S.M.4
  • 13
    • 0030255303 scopus 로고    scopus 로고
    • Scoring noncovalent protein-ligand interactions: a continuous differentiable function tuned to compute binding affinities
    • Jain A.N. Scoring noncovalent protein-ligand interactions: a continuous differentiable function tuned to compute binding affinities. Journal Computational Aided Molecular Design 20 (1996) 427-440
    • (1996) Journal Computational Aided Molecular Design , vol.20 , pp. 427-440
    • Jain, A.N.1
  • 17
    • 8844278445 scopus 로고    scopus 로고
    • Overexpression in Escherechia. Coli and purification of pteridine reducatase 1 (PTR1) from a clinical isolate of Leishmania donovani
    • Kumar P., Kothari H., and Singh N. Overexpression in Escherechia. Coli and purification of pteridine reducatase 1 (PTR1) from a clinical isolate of Leishmania donovani. Protein Expression and Purification 38 (2004) 228-236
    • (2004) Protein Expression and Purification , vol.38 , pp. 228-236
    • Kumar, P.1    Kothari, H.2    Singh, N.3
  • 18
    • 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., and Singh N. Degradation of pteridine reductase 1 (PTR1) enzyme during growth phase in the protozoan parasite Leishmania donovani. Experimental Parasitology 116 (2007) 182-189
    • (2007) Experimental Parasitology , vol.116 , pp. 182-189
    • Kumar, P.1    Sundar, S.2    Singh, N.3
  • 20
    • 0032005249 scopus 로고    scopus 로고
    • Residues involved in co-factor and substrate binding of the short-chain dehydrogenase/reductase PTR1 producing methotrexate resistance in Leishmania tarentolae
    • Leblanc E., Papadopulou B., Berenatchez C., and Oullete M. Residues involved in co-factor and substrate binding of the short-chain dehydrogenase/reductase PTR1 producing methotrexate resistance in Leishmania tarentolae. European Journal of Biochemistry 251 (1998) 768-774
    • (1998) European Journal of Biochemistry , vol.251 , pp. 768-774
    • Leblanc, E.1    Papadopulou, B.2    Berenatchez, C.3    Oullete, M.4
  • 22
    • 0033545622 scopus 로고    scopus 로고
    • A general and fast scoring function for protein-ligand interactions: a simplified potential approach
    • Muegge I., and Martin Y.C. A general and fast scoring function for protein-ligand interactions: a simplified potential approach. Journal Medicinal Chemistry 42 (1999) 791-804
    • (1999) Journal Medicinal Chemistry , vol.42 , pp. 791-804
    • Muegge, I.1    Martin, Y.C.2
  • 23
    • 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., Luba J., Hardy L.W., and Beverly S.M. The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major. The Journal of Biological Chemistry 272 (1997) 13883-13891
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 13883-13891
    • Nare, B.1    Luba, J.2    Hardy, L.W.3    Beverly, S.M.4
  • 24
    • 0021891891 scopus 로고
    • Biosynthesis and metabolism of tetrahydrobiopterin and molybdopterin
    • Nichol C.A., Smith G.K., and Duch D.S. Biosynthesis and metabolism of tetrahydrobiopterin and molybdopterin. Annual Review Biochemistry 54 (1985) 729-764
    • (1985) Annual Review Biochemistry , vol.54 , pp. 729-764
    • Nichol, C.A.1    Smith, G.K.2    Duch, D.S.3
  • 25
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modeling by satisfaction of spatial restraints. Journal of Molecular Biology 234 (1993) 779-815
    • (1993) Journal of Molecular Biology , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 26
    • 0021320759 scopus 로고
    • Identification of an infective stage of Leishmania promastigotes
    • Sacks D.L., and Perkins P.V. Identification of an infective stage of Leishmania promastigotes. Science 223 4643 (1984) 1417-1419
    • (1984) Science , vol.223 , Issue.4643 , pp. 1417-1419
    • Sacks, D.L.1    Perkins, P.V.2
  • 27
    • 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
    • Schüttelkopf A.W., Hardy L.W., Beverley S.M., and Hunter W.N. Structures of Leishmania major pteridine reductase complexes reveal the active site features important for ligand binding and to guide inhibitor design. Journal of Molecular Biology 352 (2005) 105-116
    • (2005) Journal of Molecular Biology , vol.352 , pp. 105-116
    • Schüttelkopf, A.W.1    Hardy, L.W.2    Beverley, S.M.3    Hunter, W.N.4
  • 28
    • 2442692807 scopus 로고    scopus 로고
    • Simple protocol for the synthesis of 3,4-dihydropyrimidine-2(1H)-ones
    • Shailza M., Manjula A., Vittal R.B., and Parvathi N. Simple protocol for the synthesis of 3,4-dihydropyrimidine-2(1H)-ones. Synthetic Communication 34 (2004) 1559-1564
    • (2004) Synthetic Communication , vol.34 , pp. 1559-1564
    • Shailza, M.1    Manjula, A.2    Vittal, R.B.3    Parvathi, N.4
  • 29
    • 0013026842 scopus 로고    scopus 로고
    • Is there true Sb(V) resistance in Indian kala-azar field isolates?
    • Singh N. Is there true Sb(V) resistance in Indian kala-azar field isolates?. Current Science 83 (2002) 101-102
    • (2002) Current Science , vol.83 , pp. 101-102
    • Singh, N.1
  • 30
    • 7644225314 scopus 로고    scopus 로고
    • Fluorescent Leishmania: application to antileishmanial drug testing
    • Singh N., and Dube A. Fluorescent Leishmania: application to antileishmanial drug testing. American Journal of Tropical Medicine and Hygiene 71 (2004) 400-402
    • (2004) American Journal of Tropical Medicine and Hygiene , vol.71 , pp. 400-402
    • Singh, N.1    Dube, A.2
  • 31
    • 8744244554 scopus 로고    scopus 로고
    • Tetrabutylammonium hydrogen sulfate catalysed eco-friendly and efficient synthesis of glycosyl 1,4-dihydropyridines
    • Tewari N., Dwivedi N., and Tripathi R.P. Tetrabutylammonium hydrogen sulfate catalysed eco-friendly and efficient synthesis of glycosyl 1,4-dihydropyridines. Tetrahedron Letters 45 (2004) 9011-9014
    • (2004) Tetrahedron Letters , vol.45 , pp. 9011-9014
    • Tewari, N.1    Dwivedi, N.2    Tripathi, R.P.3
  • 32
    • 0037212102 scopus 로고    scopus 로고
    • LigandFit: a novel method for the shape-directed rapid docking of ligands to protein active sites
    • Venkatachalam C.M., Jiang X., Oldfield T., and Waldman M. LigandFit: a novel method for the shape-directed rapid docking of ligands to protein active sites. Journal of Molecular Graphical Model 21 (2002) 289-307
    • (2002) Journal of Molecular Graphical Model , vol.21 , pp. 289-307
    • Venkatachalam, C.M.1    Jiang, X.2    Oldfield, T.3    Waldman, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.