{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T13:56:11Z","timestamp":1793109371957,"version":"4.5.0"},"reference-count":72,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T00:00:00Z","timestamp":1635724800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T00:00:00Z","timestamp":1635724800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T00:00:00Z","timestamp":1635724800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T00:00:00Z","timestamp":1635724800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T00:00:00Z","timestamp":1635724800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T00:00:00Z","timestamp":1635724800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T00:00:00Z","timestamp":1635724800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001321","name":"National Research Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001321","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004695","name":"University of KwaZulu-Natal","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004695","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic & Medicinal Chemistry"],"published-print":{"date-parts":[[2021,11]]},"DOI":"10.1016\/j.bmc.2021.116458","type":"journal-article","created":{"date-parts":[[2021,10,11]],"date-time":"2021-10-11T23:47:20Z","timestamp":1633996040000},"page":"116458","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":46,"special_numbering":"C","title":["Lactate dehydrogenase and malate dehydrogenase: Potential antiparasitic targets for drug development studies"],"prefix":"10.1016","volume":"50","author":[{"given":"Francis","family":"Kayamba","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mbuso","family":"Faya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ofentse Jacob","family":"Pooe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Babita","family":"Kushwaha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Narva Deshwar","family":"Kushwaha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincent A.","family":"Obakachi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincent O.","family":"Nyamori","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajshekhar","family":"Karpoormath","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bmc.2021.116458_b0005","doi-asserted-by":"crossref","first-page":"179","DOI":"10.3390\/microorganisms7060179","article-title":"Malaria: The past and the present","volume":"7","author":"Talapko","year":"2019","journal-title":"Microorganisms"},{"key":"10.1016\/j.bmc.2021.116458_b0010","unstructured":"WHO. Malaria Rapid Diagnostic Test Performance: Results of WHO Product Testing of Malaria RDTs: Round 8 (2016\u20132018); 2018."},{"key":"10.1016\/j.bmc.2021.116458_b0015","first-page":"1","article-title":"The global burden of disease of zoonotic parasitic diseases: top 5 contenders for priority consideration","volume":"4","author":"Pisarski","year":"2019","journal-title":"Trop Med Infect Dis"},{"key":"10.1016\/j.bmc.2021.116458_b0020","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1016\/S2095-3119(19)62845-5","article-title":"Lactate dehydrogenase: an important molecule involved in acetamizuril action against Eimeria tenella","volume":"19","author":"Liu","year":"2020","journal-title":"J Integr Agric"},{"key":"10.1016\/j.bmc.2021.116458_b0025","doi-asserted-by":"crossref","first-page":"e0173745","DOI":"10.1371\/journal.pone.0173745","article-title":"Lactate dehydrogenase in Toxoplasma gondii controls virulence, bradyzoite differentiation, and chronic infection","volume":"12","author":"Abdelbaset","year":"2017","journal-title":"PLoS ONE"},{"key":"10.1016\/j.bmc.2021.116458_b0030","doi-asserted-by":"crossref","first-page":"e1007953","DOI":"10.1371\/journal.ppat.1007953","article-title":"Novel lactate dehydrogenase inhibitors with in vivo efficacy against Cryptosporidium parvum","volume":"15","author":"Li","year":"2019","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.bmc.2021.116458_b0035","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molbiopara.2018.08.005","article-title":"Antibodies against Schistosoma japonicum lactate dehydrogenase B enhance enzyme active","volume":"226","author":"Li","year":"2018","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.bmc.2021.116458_b0040","doi-asserted-by":"crossref","first-page":"5","DOI":"10.3390\/scipharm85010005","article-title":"Natural products as new treatment options for trichomoniasis: a molecular docking investigation","volume":"85","author":"Setzer","year":"2017","journal-title":"Sci Pharm"},{"key":"10.1016\/j.bmc.2021.116458_b0045","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.chemphys.2014.02.018","article-title":"The enzymatic reaction catalyzed by lactate dehydrogenase exhibits one dominant reaction path Jean","volume":"442","author":"Masterson","year":"2015","journal-title":"Chem Phys"},{"key":"10.1016\/j.bmc.2021.116458_b0050","doi-asserted-by":"crossref","first-page":"6124","DOI":"10.1002\/cam4.1820","article-title":"Lactate dehydrogenase A: a key player in carcinogenesis and potential target in cancer therapy","volume":"7","author":"Han","year":"2018","journal-title":"Wiley Cancer Med"},{"key":"10.1016\/j.bmc.2021.116458_b0055","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-019-38854-7","article-title":"Novel peptide inhibitors for lactate dehydrogenase A (LDHA): a survey to inhibit LDHA activity via disruption of protein-protein interaction","volume":"9","author":"Jafary","year":"2019","journal-title":"Sci Rep"},{"key":"10.1016\/j.bmc.2021.116458_b0060","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1016\/j.biochi.2009.09.005","article-title":"Structure and function of Plasmodium falciparum malate dehydrogenase: role of critical amino acids in co-substrate binding pocket q","volume":"91","author":"Pradhan","year":"2009","journal-title":"Biochimie"},{"key":"10.1016\/j.bmc.2021.116458_b0065","doi-asserted-by":"crossref","first-page":"3488","DOI":"10.1111\/j.1432-1033.2004.04281.x","article-title":"An \u03b1-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum: Cloning and biochemical characterization of the enzyme","volume":"271","author":"Tripathi","year":"2004","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.bmc.2021.116458_b0070","doi-asserted-by":"crossref","first-page":"2088","DOI":"10.7150\/jca.19373","article-title":"Characterization of the role of the malate dehydrogenases to lung tumor cell survival","volume":"8","author":"Zhang","year":"2017","journal-title":"J Cancer"},{"key":"10.1016\/j.bmc.2021.116458_b0075","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.1111\/febs.15185","article-title":"How enzyme promiscuity and horizontal gene transfer contribute to metabolic innovation","volume":"287","author":"Glasner","year":"2020","journal-title":"FEBS J"},{"key":"10.1016\/j.bmc.2021.116458_b0080","doi-asserted-by":"crossref","first-page":"e12794","DOI":"10.1111\/cmi.12794","article-title":"Functional analysis of Toxoplasma lactate dehydrogenases suggests critical roles of lactate fermentation for parasite growth in vivo","volume":"20","author":"Xia","year":"2018","journal-title":"Cell Microbiol"},{"key":"10.1016\/j.bmc.2021.116458_b0085","doi-asserted-by":"crossref","DOI":"10.1186\/1475-2875-8-211","article-title":"PfHRP2 and PfLDH antigen detection for monitoring the efficacy of artemisinin-based combination therapy (ACT) in the treatment of uncomplicated falciparum malaria","volume":"8","author":"Houz\u00e9","year":"2009","journal-title":"Malar J"},{"key":"10.1016\/j.bmc.2021.116458_b0090","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1136\/bmj.g3846","article-title":"Rapid diagnostic tests for malaria","volume":"348","author":"Bisoffi","year":"2014","journal-title":"BMJ"},{"key":"10.1016\/j.bmc.2021.116458_b0095","doi-asserted-by":"crossref","DOI":"10.1186\/1475-2875-12-349","article-title":"Usefulness of Plasmodium falciparum-specific rapid diagnostic tests for assessment of parasite clearance and detection of recurrent infections after artemisinin-based combination therapy","volume":"12","author":"Aydin-Schmidt","year":"2013","journal-title":"Malar J"},{"key":"10.1016\/j.bmc.2021.116458_b0100","doi-asserted-by":"crossref","first-page":"1046","DOI":"10.3390\/pharmaceutics12111046","article-title":"Current advances in the development of diagnostic tests based on aptamers in parasitology: a systematic review","volume":"12","author":"Ospina-Villa","year":"2020","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.bmc.2021.116458_b0105","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1128\/JCM.00181-14","article-title":"Combining parasite lactate dehydrogenase-based and histidine-rich protein 2-based rapid tests to improve specificity for diagnosis of malaria due to plasmodium knowlesi and other plasmodium species in Sabah, Malaysia","volume":"52","author":"Grigg","year":"2014","journal-title":"J Clin Microbiol"},{"key":"10.1016\/j.bmc.2021.116458_b0110","doi-asserted-by":"crossref","DOI":"10.1186\/s13071-019-3549-x","article-title":"Clearance dynamics of lactate dehydrogenase and aldolase following antimalarial treatment for Plasmodium falciparum infection","volume":"12","author":"Plucinski","year":"2019","journal-title":"Parasites Vectors"},{"key":"10.1016\/j.bmc.2021.116458_b0115","unstructured":"To A, Bordoni B. Physiology, Krebs Cycle. StatPearls Publishing; 2021. https:\/\/www.ncbi.nlm.nih.gov\/books\/NBK556032\/#_NBK556032_pubdet_."},{"key":"10.1016\/j.bmc.2021.116458_b0120","doi-asserted-by":"crossref","first-page":"3841","DOI":"10.1021\/jm070336k","article-title":"Design, synthesis, and biological evaluation of Plasmodium falciparum lactate dehydrogenase inhibitors","volume":"50","author":"Choi","year":"2007","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2021.116458_b0125","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.02582-16","article-title":"Praziquantel for Schistosomiasis: single- drug metabolism revisited, mode of action, and resistance","volume":"61","author":"Vale","year":"2017","journal-title":"Antimicrob Agents Chemother"},{"key":"10.1016\/j.bmc.2021.116458_b0130","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1021\/jm3014844","article-title":"Fragment growing and linking lead to novel nanomolar lactate dehydrogenase inhibitors","volume":"56","author":"Kohlmann","year":"2012","journal-title":"J Med Chem"},{"key":"10.1016\/j.bmc.2021.116458_b0135","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1002\/pro.2904","article-title":"Gradual neofunctionalization in the convergent evolution of trichomonad lactate and malate dehydrogenases","volume":"25","author":"Steindel","year":"2016","journal-title":"Protein Soc"},{"key":"10.1016\/j.bmc.2021.116458_b0140","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/S0166-6851(01)00360-7","article-title":"The kinetic properties and sensitivities to inhibitors of lactate dehydrogenases (LDH1 and LDH2) from Toxoplasma gondii: comparisons with pLDH from Plasmodium falciparum","volume":"118","author":"Dando","year":"2001","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.bmc.2021.116458_b0145","doi-asserted-by":"crossref","first-page":"1578","DOI":"10.1017\/S0031182019000933","article-title":"Partial inhibition of the main energetic pathways and its metabolic consequences after in vivo treatment with benzimidazole derivatives in experimental neurocysticercosis","volume":"146","author":"Pican\u00e7o","year":"2019","journal-title":"Parasitology"},{"key":"10.1016\/j.bmc.2021.116458_b0150","first-page":"1","article-title":"Cryptosporidium Lactate dehydrogenase is associated with the parasitophorous vacuole membrane and is a potential target for developing therapeutics","author":"Zhang","year":"2015","journal-title":"PLos Pathog"},{"key":"10.1016\/j.bmc.2021.116458_b0155","unstructured":"WHO. Artemisinin resistance and artemisinin-based combination therapy efficacy. Who. 2018;(August):1-10. https:\/\/www.who.int\/malaria\/publications\/atoz\/artemisinin-resistance-august2018\/en\/."},{"key":"10.1016\/j.bmc.2021.116458_b0160","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2018.02587","article-title":"Drug Resistance in Toxoplasma gondii","volume":"9","author":"Montazeri","year":"2018","journal-title":"Front Microbiol"},{"key":"10.1016\/j.bmc.2021.116458_b0165","unstructured":"WHO. World Malaria Report 2020- WHO: 20 Years of Global Progress and Challenges; 2020. https:\/\/www.mmv.org\/newsroom\/publications\/world-malaria-report-2020?gclid=Cj0KCQiAv6yCBhCLARIsABqJTjYQ5UgQmOuMIr3YNko1HARzcENfzQ8RTa2YLaZ9RvrRwQHX0l75s2kaAsksEALw_wcB."},{"key":"10.1016\/j.bmc.2021.116458_b0170","doi-asserted-by":"crossref","first-page":"113330","DOI":"10.1016\/j.ejmech.2021.113330","article-title":"Design and synthesis of quinoline- pyrimidine inspired hybrids as potential plasmodial inhibitors","volume":"217","author":"Kayamba","year":"2021","journal-title":"Eur J Med Chem"},{"key":"10.1016\/j.bmc.2021.116458_b0175","doi-asserted-by":"crossref","first-page":"1608","DOI":"10.1016\/S0140-6736(18)30324-6","article-title":"Malaria","volume":"391","author":"Ashley","year":"2018","journal-title":"Lancet"},{"key":"10.1016\/j.bmc.2021.116458_b0180","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-018-36197-3","article-title":"Evaluating antimalarial efficacy by tracking glycolysis in Plasmodium falciparum using NMR spectroscopy","volume":"8","author":"Shivapurkar","year":"2018","journal-title":"Sci Rep"},{"key":"10.1016\/j.bmc.2021.116458_b0185","doi-asserted-by":"crossref","first-page":"17883","DOI":"10.1080\/07391102.2018.1471417","article-title":"Multiple e-pharmacophore modelling pooled with high-throughput virtual screening, docking and molecular dynamics simulations to discover potential inhibitors of Plasmodium falciparum lactate dehydrogenase (PfLDH)","volume":"37","author":"Saxena","year":"2019","journal-title":"J Biomol Struct Dyn"},{"key":"10.1016\/j.bmc.2021.116458_b0190","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1631\/jzus.B1500219","article-title":"Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase","volume":"17","author":"Takahashi-\u00ed\u00f1iguez","year":"2016","journal-title":"J Zhejiang Univ-Sci B (Biomed Biotechnol)"},{"key":"10.1016\/j.bmc.2021.116458_b0195","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1093\/femsre\/fuz010","article-title":"Revisiting gametocyte biology in malaria parasites","volume":"43","author":"Ngotho","year":"2019","journal-title":"FEMS Microbiol Rev"},{"key":"10.1016\/j.bmc.2021.116458_b0200","doi-asserted-by":"crossref","first-page":"e21237","DOI":"10.1371\/journal.pone.0021237","article-title":"Antimalarial activity of potential inhibitors of Plasmodium falciparum lactate dehydrogenase enzyme selected by docking studies","volume":"6","author":"Penna-Coutinho","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1016\/j.bmc.2021.116458_b0205","doi-asserted-by":"crossref","first-page":"6434","DOI":"10.1021\/acs.biochem.8b00913","article-title":"Functional and structural resilience of the active site loop in the evolution of plasmodium lactate dehydrogenase","volume":"57","author":"Wirth","year":"2018","journal-title":"PMC Biochem"},{"key":"10.1016\/j.bmc.2021.116458_b0210","first-page":"1","article-title":"Exploiting unique structural and functional properties of malarial glycolytic enzymes for antimalarial drug development","volume":"2014","author":"Alam","year":"2014","journal-title":"Malar Res Treat"},{"key":"10.1016\/j.bmc.2021.116458_b0215","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1080\/07391102.2011.10507383","article-title":"Docking studies on the binding of Quinoline derivatives and Hematin to Plasmodium Falciparum Lactate Dehydrogenase","volume":"29","author":"Cortopassi","year":"2011","journal-title":"J Biomol Struct Dyn"},{"key":"10.1016\/j.bmc.2021.116458_b0220","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/S1473-3099(06)70521-7","article-title":"Schistosomiasis and water resources development: systematic review, meta-analysis, and estimates of people at risk","author":"Steinmann","year":"2006","journal-title":"Lancet Infect Dis"},{"key":"10.1016\/j.bmc.2021.116458_b0225","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0140-6736(18)30098-9","article-title":"Underestimation of the global burden of schistosomiasis","volume":"391","author":"King","year":"2018","journal-title":"Lancet"},{"key":"10.1016\/j.bmc.2021.116458_b0230","doi-asserted-by":"crossref","first-page":"105897","DOI":"10.1016\/j.actatropica.2021.105897","article-title":"Population-based, spatiotemporal modeling of social risk factors and mortality from schistosomiasis","volume":"218","author":"Silva da Paz","year":"2021","journal-title":"Acta Trop"},{"key":"10.1016\/j.bmc.2021.116458_b0235","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fgene.2014.00176","article-title":"Revisiting glucose uptake and metabolism in schistosomes: new molecular insights for improved schistosomiasis therapies","volume":"5","author":"You","year":"2014","journal-title":"Front Genet"},{"key":"10.1016\/j.bmc.2021.116458_b0240","doi-asserted-by":"crossref","first-page":"585","DOI":"10.3201\/eid0606.000606","article-title":"Evidence against rapid emergence of praziquantel resistance in Schistosoma haematobium, Kenya","volume":"6","author":"King","year":"2000","journal-title":"Emerg Infect Dis"},{"key":"10.1016\/j.bmc.2021.116458_b0245","first-page":"1","article-title":"Antiparasitic activity in Trichomonas vaginalis","author":"Sena-lopes","year":"2019","journal-title":"Biotechnol Res Innov"},{"key":"10.1016\/j.bmc.2021.116458_b0250","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.3390\/ijms20071565","article-title":"Gene Expression in developmental stages of Schistosoma japonicum provides further insight into the importance of the schistosome insulin-like peptide","volume":"20","author":"Du","year":"2019","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.bmc.2021.116458_b0255","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1590\/S0074-02761998000700035","article-title":"Lactate dehydrogenase: sequence and analysis of its expression during the life cycle of Schistosoma mansoni","volume":"93","author":"Franco","year":"1998","journal-title":"Mem Inst Oswaldo Cruz"},{"key":"10.1016\/j.bmc.2021.116458_b0260","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/0014-4894(55)90021-7","article-title":"The immunological specificity of lactic dehydrogenase of Schistosoma mansoni'","volume":"4","author":"Henion","year":"1955","journal-title":"Exp Parasitol"},{"key":"10.1016\/j.bmc.2021.116458_b0265","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1080\/20477724.2018.1514137","article-title":"A review on inactivation methods of Toxoplasma gondii in foods","volume":"112","author":"Mirza Alizadeh","year":"2018","journal-title":"Pathog Glob Health"},{"key":"10.1016\/j.bmc.2021.116458_b0270","first-page":"1","article-title":"Prevalence and predictors of Toxoplasma gondii infection in pregnant women from","volume":"4","author":"Al-adhroey","year":"2019","journal-title":"BMC Infect Dis"},{"key":"10.1016\/j.bmc.2021.116458_b0275","doi-asserted-by":"crossref","DOI":"10.1186\/s13071-020-3954-1","article-title":"The global serological prevalence of Toxoplasma gondii in felids during the last five decades (1967\u20132017): a systematic review and meta - analysis","volume":"13","author":"Montazeri","year":"2020","journal-title":"Parasit Vectors"},{"key":"10.1016\/j.bmc.2021.116458_b0280","article-title":"A lactate fermentation mutant of toxoplasma stimulates protective immunity against acute and chronic toxoplasmosis","volume":"9","author":"Xia","year":"1814","journal-title":"Front Immunol"},{"key":"10.1016\/j.bmc.2021.116458_b0285","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1111\/mmi.12999","article-title":"Expression of the glycolytic enzymes enolase and lactate dehydrogenase during the early phase of Toxoplasma differentiation is regulated by an intron retention mechanism","volume":"96","author":"Lunghi","year":"2015","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.bmc.2021.116458_b0290","series-title":"Biochemistry and metabolism of Toxoplasma gondii: carbohydrates, lipids and nucleotides","author":"Coppens","year":"2014"},{"key":"10.1016\/j.bmc.2021.116458_b0295","first-page":"879","article-title":"Structure of Toxoplasma gondii LDH1: Active-Site Differences from Human Lactate Dehydrogenases and the Structural Basis for Efficient APAD + Use","volume":"43","author":"Kavanagh","year":"2004","journal-title":"Am Chem Soc"},{"key":"10.1016\/j.bmc.2021.116458_b0300","doi-asserted-by":"crossref","DOI":"10.1186\/s13071-020-04445-z","article-title":"The life-cycle of Toxoplasma gondii reviewed using animations","volume":"13","author":"Attias","year":"2020","journal-title":"Parasit Vectors"},{"key":"10.1016\/j.bmc.2021.116458_b0305","doi-asserted-by":"crossref","first-page":"52300","DOI":"10.1074\/jbc.M409175200","article-title":"The expression of lactate dehydrogenase is important for the cell cycle of toxoplasma gondii*","volume":"279","author":"Al-Anouti","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.bmc.2021.116458_b0310","doi-asserted-by":"crossref","first-page":"2355","DOI":"10.1007\/s00018-018-2808-x","article-title":"A latent ability to persist: differentiation in Toxoplasma gondii","volume":"75","author":"Jeffers","year":"2019","journal-title":"Cellullar Mol Life Sci"},{"key":"10.1016\/j.bmc.2021.116458_b0315","unstructured":"CDC. Trichomoniasis - CDC Fact Sheet. Cent Diesease Control. Published online 2020. https:\/\/www.cdc.gov\/std\/trichomonas\/stdfact-trichomoniasis.htm."},{"key":"10.1016\/j.bmc.2021.116458_b0320","first-page":"1","article-title":"Infection with Trichomonas vaginalis increases the risk of psychiatric disorders in women: a nationwide population - based cohort study","author":"Lin","year":"2019","journal-title":"Parasit Vectors"},{"key":"10.1016\/j.bmc.2021.116458_b0325","doi-asserted-by":"crossref","first-page":"e1006831","DOI":"10.1371\/journal.ppat.1006831","article-title":"Does the common sexually transmitted parasite Trichomonas vaginalis have sex?","volume":"14","author":"Bradic","year":"2018","journal-title":"Plos Pathog"},{"key":"10.1016\/j.bmc.2021.116458_b0330","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2019.00430","article-title":"Demonstration and characterization of cyst-like structures in the life cycle of Trichomonas vaginalis","volume":"9","author":"Beri","year":"2020","journal-title":"Front Cell Infect Microbiol"},{"key":"10.1016\/j.bmc.2021.116458_b0335","doi-asserted-by":"crossref","first-page":"5033","DOI":"10.1128\/AAC.49.12.5033-5036.2005","article-title":"Alternative pathway of metronidazole activation in trichomonas vaginalis hydrogenosomes","volume":"49","author":"Hrdy","year":"2005","journal-title":"Antimicrob Agents Chemother"},{"key":"10.1016\/j.bmc.2021.116458_b0340","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1128\/EC.05225-11","article-title":"A machine learning approach to identify hydrogenosomal proteins in trichomonas vaginalis","volume":"11","author":"Burstein","year":"2012","journal-title":"Eukaryot Cell"},{"key":"10.1016\/j.bmc.2021.116458_b0345","first-page":"1","article-title":"Recent advances in the Trichomonas vaginalis field","volume":"5","author":"Leitsch","year":"2016","journal-title":"FloooResearch"},{"key":"10.1016\/j.bmc.2021.116458_b0350","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1016\/j.ijbiomac.2014.12.019","article-title":"Biochemical and structural characterization of Cryptosporidium parvum Lactate dehydrogenase","volume":"74","author":"Cook","year":"2015","journal-title":"Int J Biol Macromol"},{"key":"10.1016\/j.bmc.2021.116458_b0355","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1093\/molbev\/msh042","article-title":"Evolution of Cryptosporidium parvum lactate dehydrogenase from malate dehydrogenase by a very recent event of gene duplication","volume":"21","author":"Madern","year":"2004","journal-title":"Soc Mol Biol Evol"},{"key":"10.1016\/j.bmc.2021.116458_b0360","first-page":"2488","article-title":"Structurally linked dynamics in lactate dehydrogenases of evolutionarily distinct species structurally linked dynamics in lactate dehydrogenases of evolutionarily distinct species","volume":"56","author":"Varga","year":"2017","journal-title":"Am Chem Soc Biochem"}],"container-title":["Bioorganic & Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089621004661?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089621004661?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T01:15:55Z","timestamp":1760836555000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0968089621004661"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,11]]},"references-count":72,"alternative-id":["S0968089621004661"],"URL":"https:\/\/doi.org\/10.1016\/j.bmc.2021.116458","relation":{},"ISSN":["0968-0896"],"issn-type":[{"value":"0968-0896","type":"print"}],"subject":[],"published":{"date-parts":[[2021,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Lactate dehydrogenase and malate dehydrogenase: Potential antiparasitic targets for drug development studies","name":"articletitle","label":"Article Title"},{"value":"Bioorganic & Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bmc.2021.116458","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"116458"}}