{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,7]],"date-time":"2025-11-07T18:57:48Z","timestamp":1762541868952},"reference-count":33,"publisher":"Springer Science and Business Media LLC","issue":"9","license":[{"start":{"date-parts":[[2010,2,21]],"date-time":"2010-02-21T00:00:00Z","timestamp":1266710400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Mol Model"],"published-print":{"date-parts":[[2010,8]]},"DOI":"10.1007\/s00894-010-0649-0","type":"journal-article","created":{"date-parts":[[2010,2,20]],"date-time":"2010-02-20T02:04:16Z","timestamp":1266631456000},"page":"1539-1547","source":"Crossref","is-referenced-by-count":20,"title":["Probing the structure of Leishmania donovani chagasi DHFR-TS: comparative protein modeling and protein\u2013ligand interaction studies"],"prefix":"10.1007","volume":"16","author":[{"given":"Lakshmi","family":"Maganti","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Prabu","family":"Manoharan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nanda","family":"Ghoshal","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2010,2,21]]},"reference":[{"key":"649_CR1","first-page":"3","volume":"11","author":"AM Cunha","year":"1937","unstructured":"Cunha AM, Chagas E (1937) New species of protozoa of the genus Leishmania pathogenic to man Leishmania chagasi n. sp previous note. O Hospital 11:3\u20139","journal-title":"O Hospital"},{"key":"649_CR2","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/j.pt.2003.09.008","volume":"19","author":"SL Croft","year":"2003","unstructured":"Croft SL, Coombs GH (2003) Leishmaniasis\u2014current chemotherapy and recent advances in the search for novel drugs. Trends Parasitol 19:502\u2013508. doi: 10.1016\/j.pt.2003.09.008","journal-title":"Trends Parasitol"},{"key":"649_CR3","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1016\/S1473-3099(02)00347-X","volume":"2","author":"PJ Guerin","year":"2002","unstructured":"Guerin PJ, Olliaro P, Sundar S, Boelaert M, Croft Sl, Desjeux P, Wasunna MK, Bryceson ADM (2002) Visceral leishmaniasis: current status of control, diagnosis, and treatment, and a proposed research and development agenda. Lancet Infect Dis 2:494\u2013501. doi: 10.1016\/S1473-3099(02)00347-X","journal-title":"Lancet Infect Dis"},{"key":"649_CR4","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1136\/bmj.326.7385.377","volume":"326","author":"CR Davies","year":"2003","unstructured":"Davies CR, Kaye P, Croft SL, Sunder S (2003) Leishmaniasis: new approaches to disease control. BMJ 326:377\u2013382. doi: 10.1136\/bmj.326.7385.377","journal-title":"BMJ"},{"key":"649_CR5","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1007\/s004300100085","volume":"190","author":"P Desjeux","year":"2001","unstructured":"Desjeux P (2001) Worldwide increasing risk factors for leishmaniasis. Med Microbiol Immunol 190:77\u201379. doi: 10.1007\/s004300100085","journal-title":"Med Microbiol Immunol"},{"key":"649_CR6","unstructured":"World Health Organization (2000) The Leishmaniasis and Leishmania\/HIV co-infections. Fact Sheet Number 116. WHO, Geneva, Switzerland"},{"key":"649_CR7","doi-asserted-by":"crossref","first-page":"4300","DOI":"10.1021\/jm981130+","volume":"42","author":"FC Shafinaz","year":"1999","unstructured":"Shafinaz FC, Villamor VB, Guerrero RH, Leal I, Brun R, Croft SL, Goodman JM, Maes L, Ruiz-Perez LM, Pacanowska DG, Gilbert IH (1999) Design, synthesis, and evaluation of inhibitors of trypanosomal and leishmanial dihydrofolate reductase. J Med Chem 42:4300\u20134312. doi: 10.1021\/jm981130+","journal-title":"J Med Chem"},{"key":"649_CR8","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.2174\/1381612013397546","volume":"7","author":"R Decampo","year":"2001","unstructured":"Decampo R (2001) Recent developments in the chemotherapy of Cha-gas\u2019 disease. Curr Pharm Des 7:1157\u20131164. doi: 10.2174\/1381612013397546","journal-title":"Curr Pharm Des"},{"key":"649_CR9","first-page":"1780","volume":"60","author":"K McLuskey","year":"2004","unstructured":"McLuskey K, Gibellini F, Carvalho P, Avery MA, Huntera WN (2004) Inhibition of Leishmania major pteridine reductase by 2, 4, 6-triaminoquinazoline: structure of the NADPH ternary complex. Acta Cryst 60:1780\u20131785. doi: 10.1107\/S0907444904018955","journal-title":"Acta Cryst"},{"key":"649_CR10","doi-asserted-by":"crossref","first-page":"5802","DOI":"10.1073\/pnas.77.10.5802","volume":"77","author":"R Ferone","year":"1980","unstructured":"Ferone R, Roland S (1980) Dihydrofolate reductase: thymidylate synthase, a bifunctional polypeptide from Crithidia fasciculata. Proc Natl Acad Sci USA 77:5802\u20135806","journal-title":"Proc Natl Acad Sci USA"},{"key":"649_CR11","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0166-6851(84)90070-7","volume":"11","author":"CE Garrett","year":"1984","unstructured":"Garrett CE, Coderre JA, Meek TD, Garvey EP, Claman DM, Beverly SM, Santhi DV (1984) A Bifunctional thymidylate synthase-dihydrofolate reductase in protozoa. Mol Biochem Parasitol 11:257\u2013265. doi: 10.1016\/0166-6851(84)90070-7","journal-title":"Mol Biochem Parasitol"},{"key":"649_CR12","doi-asserted-by":"crossref","first-page":"1591","DOI":"10.1096\/fasebj.4.6.2180768","volume":"4","author":"KM Ivanetich","year":"1990","unstructured":"Ivanetich KM, Santhi DV (1990) Bifunctional thymidylate synthase-dihydrofolate reductase in protozoa. FASEB J 4:1591\u20131597. doi: 0892-6638\/90\/0004-1591\/$O1.50","journal-title":"FASEB J"},{"key":"649_CR13","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1002\/bies.10114","volume":"24","author":"A Bermingham","year":"2002","unstructured":"Bermingham A, Derrick JP (2002) The folic acid biosynthesis pathway in bacteria: evaluation of potential for antibacterial drug discovery. BioEssays 24:637\u2013648. doi: 10.1002\/bies.10114","journal-title":"BioEssays"},{"key":"649_CR14","doi-asserted-by":"crossref","DOI":"10.1128\/9781555817886","volume-title":"Antibiotics: actions, origins, resistance","author":"C Walsh","year":"2003","unstructured":"Walsh C (2003) Antibiotics: actions, origins, resistance. ASM, Washington. doi: 10.1110\/ps.041032204"},{"key":"649_CR15","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1179\/joc.2004.16.1.3","volume":"16","author":"RL Then","year":"2004","unstructured":"Then RL (2004) Antimicrobial dihydrofolate reductase inhibitors-achievements and future options: review. J Chemother 16:3\u201312","journal-title":"J Chemother"},{"key":"649_CR16","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1016\/j.bbrc.2005.05.169","volume":"333","author":"QC Zheng","year":"2005","unstructured":"Zheng QC, Li ZS, Sun M, Zhang Y, Sun CC (2005) Homology modeling and substrate binding study of nudix hydrolase Ndx1 from Thermos thermophilus HB8. Biochem Biophys Res Commun 333:881\u2013887","journal-title":"Biochem Biophys Res Commun"},{"key":"649_CR17","first-page":"971","volume":"28","author":"W Xu","year":"2007","unstructured":"Xu W, Cai P, Yan M, Xu L, Ouyang PK (2007) Molecular docking of xylitol and xylose isomerase from Thermus thermophilus and model analysis. Chem J Chin Univ 28:971\u2013973","journal-title":"Chem J Chin Univ"},{"key":"649_CR18","first-page":"254","volume":"26","author":"YP He","year":"2005","unstructured":"He YP, Hu HR, Xu LS (2005) Structure\u2013activity relationship studies on 6-naphthylmethyl substituted HEPT derivatives as nonnucleoside reverse transcriptase inhibitors based on molecular docking. Chem J Chin Univ 26:254\u2013258","journal-title":"Chem J Chin Univ"},{"key":"649_CR19","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/nsb0394-186","volume":"1","author":"DR Knighton","year":"1994","unstructured":"Knighton DR, Kan CC, Howland E, Janson CA, Hostomska Z, Welsh KM, Matthews DA (1994) Structure of and kinetic channelling in bifunctional dihydrofolate reductase-thymidylate synthase. Nat Struct Biol 1:186\u2013194. doi: 10.1038\/nsb0394-186","journal-title":"Nat Struct Biol"},{"key":"649_CR20","first-page":"704","volume":"65","author":"O Senkovich","year":"2009","unstructured":"Senkovich O, Schormann N, Chattopadhyay D (2009) Structures of dihydrofolate reductase-thymidylate synthase of Trypanosoma cruzi in the folate-free state and in complex with two antifolate drugs, trimetrexate and methotrexate. Acta Cryst 65:704\u2013716. doi: 10.1107\/S090744490901230X","journal-title":"Acta Cryst"},{"key":"649_CR21","unstructured":"InsightII (2007) Accelrys, San Diego"},{"key":"649_CR22","unstructured":"GOLD (2006) CCDC, Cambridge"},{"key":"649_CR23","unstructured":"http:\/\/www.pymol.org"},{"key":"649_CR24","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/0022-2836(70)90057-4","volume":"48","author":"SB Needleman","year":"1970","unstructured":"Needleman SB, Wunsch CD (1970) A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 48:443\u2013453. doi: 10.1016\/0022-2836(70)90057-4","journal-title":"J Mol Biol"},{"key":"649_CR25","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1007\/s008940050087","volume":"4","author":"L Jaroszewski","year":"1998","unstructured":"Jaroszewski L, Pawlowski K, Godzik A (1998) Multiple model approach: exploring the limits of comparative modeling. J Mol Model 4:294\u2013309. doi: 10.1007\/s008940050087","journal-title":"J Mol Model"},{"key":"649_CR26","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/356083a0","volume":"356","author":"R Luthy","year":"1992","unstructured":"Luthy R, Bowie JU, Eisenberg D (1992) Assessment of protein models with three-dimensional profiles. Nature 356:83\u201385. doi: 10.1038\/356083a0","journal-title":"Nature"},{"key":"649_CR27","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1002\/pro.5560020916","volume":"2","author":"C Colovos","year":"1993","unstructured":"Colovos C, Yeates TO (1993) Verification of protein structures: patterns of nonbonded atomic interactions. Protein Sci 2:1511\u20131519. doi: 10.1002\/pro.5560020916","journal-title":"Protein Sci"},{"key":"649_CR28","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1038\/381272a0","volume":"381","author":"RWW Hooft","year":"1996","unstructured":"Hooft RWW, Vriend G, Sander C, Abola EE (1996) Errors in protein structures. Nature 381:272\u2013272. doi: 10.1038\/381272a0","journal-title":"Nature"},{"key":"649_CR29","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1007\/BF02337562","volume":"7","author":"MJ Sippl","year":"1993","unstructured":"Sippl MJ (1993) Boltzmann\u2019s principle, knowledge-based mean fields and protein folding. J Comput Aided Mol Des 7:473\u2013501. doi: 10.1007\/BF02337562","journal-title":"J Comput Aided Mol Des"},{"key":"649_CR30","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","volume":"26","author":"RA Laskowski","year":"1993","unstructured":"Laskowski RA, Macarthur MW, Moss DS, Thornton JM (1993) PROCHECK a program to check the stereo chemical quality of protein structure. J Appl Cryst 26:283\u2013291. doi: 10.1107\/S0021889892009944","journal-title":"J Appl Cryst"},{"key":"649_CR31","doi-asserted-by":"crossref","first-page":"2714","DOI":"10.1002\/elps.1150181505","volume":"18","author":"N Guex","year":"1997","unstructured":"Guex N, Peitsch MC (1997) SWISS MODEL and the Swiss pdb viewer: an environment for comparative protein modeling. Electrophoresis 18:2714\u20132723. doi: 10.1093\/nar\/gkg520","journal-title":"Electrophoresis"},{"key":"649_CR32","unstructured":"Cerius2 (2006) Accelrys, San Diego"},{"key":"649_CR33","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1093\/protein\/8.2.127","volume":"8","author":"AC Wallace","year":"1995","unstructured":"Wallace AC, Laskowski RA, Thornton JM (1995) LIGPLOT: a program to generate schematic diagrams of protein\u2013ligand interactions. Protein Eng 8:127\u2013134. doi: 10.1093\/protein\/8.2.127","journal-title":"Protein Eng"}],"container-title":["Journal of Molecular Modeling"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00894-010-0649-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s00894-010-0649-0\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00894-010-0649-0","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,5,29]],"date-time":"2019-05-29T06:51:58Z","timestamp":1559112718000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s00894-010-0649-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,2,21]]},"references-count":33,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2010,8]]}},"alternative-id":["649"],"URL":"https:\/\/doi.org\/10.1007\/s00894-010-0649-0","relation":{},"ISSN":["1610-2940","0948-5023"],"issn-type":[{"value":"1610-2940","type":"print"},{"value":"0948-5023","type":"electronic"}],"subject":[],"published":{"date-parts":[[2010,2,21]]}}}