{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T16:28:22Z","timestamp":1787761702282,"version":"build-2784847793"},"reference-count":35,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"2","content-domain":{"domain":["lww.com","ovid.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2017,4]]},"abstract":"<jats:sec>\n                    <jats:title>Introduction:<\/jats:title>\n                    <jats:p>\n                      The treatment of Indian tropical disease such as kala-azar is likely to be troublesome to the clinicians as AmpB- and miltefosine-resistant\n                      <jats:italic toggle=\"yes\">Leishmania donovani<\/jats:italic>\n                      has been reported. The rationale behind designed a novel inhibitors of model of\n                      <jats:italic toggle=\"yes\">L. donovani<\/jats:italic>\n                      enolase and performing a binding study with its inhibitors to gain details of the interaction between protein residues and ligand molecules.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods and Materials:<\/jats:title>\n                    <jats:p>\n                      The\n                      <jats:italic toggle=\"yes\">L. donovani<\/jats:italic>\n                      enolase model consists of two typical domains. The N-terminal one contains three-stranded antiparallel \u03b2-sheets, followed by six \u03b1-helices. The C-terminal domain composes of eleven-stranded mixed \u03b1\/\u03b2-barrel with connectivity. The first \u03b1-helix within the C-terminal domain, H7, and the second \u03b2-strand, S7, of the barrel domain was arranged in an antiparallel fashion compared to all other \u03b1-helices and \u03b2-strands. The root-mean-square deviation between predicted model and template is 0.4 \u00c5. The overall conformation of\n                      <jats:italic toggle=\"yes\">L. donovani<\/jats:italic>\n                      enolase model is similar to those of\n                      <jats:italic toggle=\"yes\">Trypanosoma cruzi<\/jats:italic>\n                      enolase and\n                      <jats:italic toggle=\"yes\">Streptococcus pneumoniae<\/jats:italic>\n                      enolase crystal structures.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Result:<\/jats:title>\n                    <jats:p>The key amino acid residues within the docking complex model involved in the interaction between model enolase structure and ligand molecule are Lys70, Asn165, Ala168, Asp17, and Asn213.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion:<\/jats:title>\n                    <jats:p>Our theoretical prediction may lead to the establishment of prophylactic and therapeutic approaches for the treatment of kala-azar. This biomedical informatics analysis will help us to combat future kala-azar.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.4103\/jpbs.jpbs_241_16","type":"journal-article","created":{"date-parts":[[2023,2,9]],"date-time":"2023-02-09T00:05:58Z","timestamp":1675901158000},"page":"99-105","update-policy":"https:\/\/doi.org\/10.1097\/lww.0000000000001000","source":"Crossref","is-referenced-by-count":2,"title":["Homology Modeling of Leishmania donovani Enolase and its Molecular Interaction with Novel Inhibitors"],"prefix":"10.4103","volume":"9","author":[{"given":"Jay Prakash","family":"Mahato","sequence":"first","affiliation":[{"name":"Department of Biotechnology, Sri Satya Sai University of Technology and Medical Sciences, Bhopal, Madhya Pradesh, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sindhuprava","family":"Rana","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Sri Satya Sai University of Technology and Medical Sciences, Bhopal, Madhya Pradesh, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maneesh","family":"Kumar","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, College of Commerce, Arts and Science (Magadh University, Bodh Gaya), Patna, Bihar, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Surendra","family":"Sarsaiya","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, College of Commerce, Arts and Science (Magadh University, Bodh Gaya), Patna, Bihar, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"276","reference":[{"key":"R1-20250525","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1128\/CMR.19.1.111-126.2006","article-title":"Drug resistance in leishmaniasis","volume":"19","author":"Croft","year":"2006","journal-title":"Clin Microbiol Rev"},{"key":"R2-20250525","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1186\/1471-2172-12-44","article-title":"In silico predicted epitopes from the COOH-terminal extension of cysteine proteinase B inducing distinct immune responses during leishmania (leishmania) amazonensis experimental murine infection","volume":"12","author":"Pereira","year":"2011","journal-title":"BMC Immunol"},{"key":"R3-20250525","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1016\/j.exppara.2011.07.001","article-title":"Immunogenicity of Leishmania donovani iron superoxide dismutase B1 and peroxidoxin 4 in BALB\/c mice: The contribution of Toll-like receptor agonists as adjuvant","volume":"129","author":"Daifalla","year":"2011","journal-title":"Exp Parasitol"},{"key":"R4-20250525","doi-asserted-by":"crossref","first-page":"32","DOI":"10.4172\/jpb.1000059","article-title":"Homology modeling and functional analysis of LPG2 protein of Leishmania strains","volume":"2","author":"Sahoo","year":"2009","journal-title":"J Proteomics Bioinformatics"},{"key":"R5-20250525","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/0738-081X(96)00057-0","article-title":"Leishmaniasis. 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