<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Shivapurkar, Rupali</style></author><author><style face="normal" font="default" size="100%">Hingamire, Tejashri</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Akshay S.</style></author><author><style face="normal" font="default" size="100%">Rajamohanan,  P.  R.</style></author><author><style face="normal" font="default" size="100%">Reddy, D. Srinivasa</style></author><author><style face="normal" font="default" size="100%">Shanmugam, Dhanasekaran</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Evaluating antimalarial efficacy by tracking glycolysis in Plasmodium falciparum using NMR spectroscopy</style></title><secondary-title><style face="normal" font="default" size="100%">Scientific Reports</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%"> 8</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Glucose is an essential nutrient for Plasmodium falciparum and robust glycolytic activity is indicative of viable parasites. Using NMR spectroscopy, we show that P. falciparum infected erythrocytes consume similar to 20 times more glucose, and trophozoites metabolize similar to 6 times more glucose than ring stage parasites. The glycolytic activity, and hence parasite viability, can be measured within a period of 2 h to 5 h, using this method. This facilitates antimalarial bioactivity screening on ring and trophozoite stage parasites, exclusively. We demonstrate this using potent and mechanistically distinct antimalarial compounds such as chloroquine, atovaquone, cladosporin, DDD107498 and artemisinin. Our findings indicate that ring stage parasites are inherently more tolerant to antimalarial inhibitors, a feature which may facilitate emergence of drug resistance. Thus, there is a need to discover novel antimalarial compounds, which are potent and fast acting against ring stage parasites. The NMR method reported here can facilitate the identification of such molecules.</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">4.122</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sahu, Amit Kumar</style></author><author><style face="normal" font="default" size="100%">Said, Madhukar S.</style></author><author><style face="normal" font="default" size="100%">Hingamire, Tejashri</style></author><author><style face="normal" font="default" size="100%">Gaur, Megha</style></author><author><style face="normal" font="default" size="100%">Khan, Abujunaid</style></author><author><style face="normal" font="default" size="100%">Shanmugam, Dhanasekaran</style></author><author><style face="normal" font="default" size="100%">Barvkar, Vitthal T.</style></author><author><style face="normal" font="default" size="100%">Dharne, Mahesh S.</style></author><author><style face="normal" font="default" size="100%">Bharde, Atul A.</style></author><author><style face="normal" font="default" size="100%">Dastager, Syed G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Approach to nigericin derivatives and their therapeutic potential</style></title><secondary-title><style face="normal" font="default" size="100%">RSC Advances</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">10</style></volume><pages><style face="normal" font="default" size="100%">43085-43091</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;A new nigericin analogue that has been chemically modified was synthesized through a fluorination process from the parent nigericin, produced from a novel Streptomyces strain DASNCL-29. Fermentation strategies were designed for the optimised production of nigericin molecule and subjected for purification and structural analysis. The fermentation process resulted in the highest yield of nigericin (33% (w/w)). Initially, nigericin produced from the strain DASNCL-29 demonstrated polymorphism in its crystal structure, i.e., monoclinic and orthorhombic crystal lattices when crystallised with methanol and hexane, respectively. Furthermore, nigericin produced has been subjected to chemical modification by fluorination to enhance its efficacy. Two fluorinated analogues revealed that they possess a very potent antibacterial activity against Gram positive and Gram negative bacteria. To date, the nigericin molecule has not been reported for any reaction against Gram-negative bacteria, which are increasingly becoming resistant to antibiotics. For the first time, fluorinated analogues of nigericin have shown promising activity. In vitro cytotoxicity analysis of fluorinated analogues demonstrated tenfold lesser toxicity than the parent nigericin. This is the first type of study where the fluorinated analogues of nigericin showed very encouraging activity against Gram-negative organisms; moreover, they can be used as a candidate for treating many serious infections.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">70</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;3.119&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Patra, Alok Tanala</style></author><author><style face="normal" font="default" size="100%">Hingamire, Tejashri</style></author><author><style face="normal" font="default" size="100%">Belekar, Meenakshi A.</style></author><author><style face="normal" font="default" size="100%">Xiong, Aoli</style></author><author><style face="normal" font="default" size="100%">Subramanian, Gowtham</style></author><author><style face="normal" font="default" size="100%">Bozdech, Zbynek</style></author><author><style face="normal" font="default" size="100%">Preiser, Peter</style></author><author><style face="normal" font="default" size="100%">Shanmugam, Dhanasekaran</style></author><author><style face="normal" font="default" size="100%">Chandramohanadas, Rajesh</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Whole-cell phenotypic screening of medicines for malaria venture pathogen box identifies specific inhibitors of plasmodium falciparum late-stage development and egress</style></title><secondary-title><style face="normal" font="default" size="100%">Antimicrobial Agents and Chemotherapy</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">DNA fragmentation</style></keyword><keyword><style  face="normal" font="default" size="100%">egress</style></keyword><keyword><style  face="normal" font="default" size="100%">Medicines for Malaria Venture</style></keyword><keyword><style  face="normal" font="default" size="100%">MMV</style></keyword><keyword><style  face="normal" font="default" size="100%">Pathogen Box</style></keyword><keyword><style  face="normal" font="default" size="100%">phenotypic screening</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">schizonts</style></keyword><keyword><style  face="normal" font="default" size="100%">stage-specific inhibition</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">64</style></volume><pages><style face="normal" font="default" size="100%">e01802-19</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;We report a systematic, cellular phenotype-based antimalarial screening of the Medicines for Malaria Venture Pathogen Box collection, which facilitated the identification of specific blockers of late-stage intraerythrocytic development of Plasmodium falciparum. First, from standard growth inhibition assays, we identified 173 molecules with antimalarial activity (50% effective concentration [EC50] &amp;lt;= 10 mu M), which included 62 additional molecules over previously known antimalarial candidates from the Pathogen Box. We identified 90 molecules with EC50 of &amp;lt;= 1 mu M, which had significant effect on the ring-trophozoite transition, while 9 molecules inhibited the trophozoite-schizont transition and 21 molecules inhibited the schizontring transition (with &amp;gt;= 50% parasites failing to proceed to the next stage) at 1 mu M. We therefore rescreened all 173 molecules and validated hits in microscopy to prioritize 12 hits as selective blockers of the schizont-ring transition. Seven of these molecules inhibited the calcium ionophore-induced egress of Toxoplasma gondii, a related apicomplexan parasite, suggesting that the inhibitors may be acting via a conserved mechanism which could be further exploited for target identification studies. We demonstrate that two molecules, MMV020670 and MMV026356, identified as schizont inhibitors in our screens, induce the fragmentation of DNA in merozoites, thereby impairing their ability to egress and invade. Further mechanistic studies would facilitate the therapeutic exploitation of these molecules as broadly active inhibitors targeting late-stage development and egress of apicomplexan parasites relevant to human health.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;4.904&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kaushik, Meenakshi</style></author><author><style face="normal" font="default" size="100%">Hoti, Sugeerappa L.</style></author><author><style face="normal" font="default" size="100%">Saxena, Jitendra Kumar</style></author><author><style face="normal" font="default" size="100%">Hingamire, Tejashri</style></author><author><style face="normal" font="default" size="100%">Shanmugam, Dhanasekaran</style></author><author><style face="normal" font="default" size="100%">Joshi, Rajesh K.</style></author><author><style face="normal" font="default" size="100%">Metgud, Sharada C.</style></author><author><style face="normal" font="default" size="100%">Ungar, Banappa</style></author><author><style face="normal" font="default" size="100%">Singh, Ishwar</style></author><author><style face="normal" font="default" size="100%">Hegde, Harsha V.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Antimalarial activity of anacardium occidentale leaf extracts against plasmodium falciparum transketolase (PfTK)</style></title><secondary-title><style face="normal" font="default" size="100%">Acta Parasitologica</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Anacardium occidentale L</style></keyword><keyword><style  face="normal" font="default" size="100%">Antimalarial activity</style></keyword><keyword><style  face="normal" font="default" size="100%">malaria</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">Transketolase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">68</style></volume><pages><style face="normal" font="default" size="100%">832-841</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	BackgroundAs per estimates by WHO in 2021 almost half of the world's population was at risk of malaria and &amp;gt; 0.6 million deaths were attributed to malaria. Therefore, the present study was aimed to explore the antimalarial activity of extracts derived from the leaves of the plant Anacardium occidentale L., which has been used traditionally for the treatment of malaria. Different extracts of A.occidentale leaves were prepared and tested for their inhibitory activity against recombinant P. falciparum transketolase (rPfTK) enzyme, in vitro. Further, growth inhibitory activity against cultivated blood stage P. falciparum parasites (3D7 strain), was studied using SYBR Green fluorescence-based in vitro assays. Acute toxicity of the hydro alcoholic extracts of leaves of A. occidentale (HELA) at different concentrations was evaluated on mice and Zebra fish embryos. HELA showed 75.45 +/- 0.35% inhibitory activity against the recombinant PfTk and 99.31 +/- 0.08% growth inhibition against intra-erythrocytic stages of P. falciparum at the maximum concentration (50 mu g/ml) with IC50 of 4.17 +/- 0.22 mu g/ml. The toxicity test results showed that the heartbeat, somite formation, tail detachment and hatching of embryos were not affected when Zebra fish embryos were treated with 0.1 to 10 mu g/ml of the extract. However, at higher concentrations of the extract, at 48 h (1000 mu g/ml) and 96 h (100 mu g/ml and 1000 mu g/ml, respectively) there was no heartbeat in the fish embryos. In the acute oral toxicity tests performed on mice, the extract showed no toxicity up to 300 mg/kg body weight in mice.ConclusionThe hydro-alcoholic extract of leaves of A. occidentale L. showed potent antimalarial activity against blood stage P. falciparum. Based on the observed inhibitory activity on the transketolase enzyme of P. falciparum it is likely that this enzyme is the target for the development of bioactive molecules present in the plant extracts. The promising anti-malarial activity of purified compounds from leaves of A. occidentale needs to be further explored for development of new anti-malarial therapy.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	1.5&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Meena, Chhuttan L.</style></author><author><style face="normal" font="default" size="100%">Hingamire, Tejashri</style></author><author><style face="normal" font="default" size="100%">Gupta, Tanya</style></author><author><style face="normal" font="default" size="100%">Deshmukh, Bhagyashree</style></author><author><style face="normal" font="default" size="100%">Karmodiya, Krishanpal</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh</style></author><author><style face="normal" font="default" size="100%">Shanmugam, Dhanasekaran</style></author><author><style face="normal" font="default" size="100%">Sanjayan, Gangadhar J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Histidinal-based potent antimalarial agents</style></title><secondary-title><style face="normal" font="default" size="100%">ChemMedChem</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">artemisinin</style></keyword><keyword><style  face="normal" font="default" size="100%">chloroquine</style></keyword><keyword><style  face="normal" font="default" size="100%">digestive vacuole</style></keyword><keyword><style  face="normal" font="default" size="100%">docking</style></keyword><keyword><style  face="normal" font="default" size="100%">falcipains</style></keyword><keyword><style  face="normal" font="default" size="100%">falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">P</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">18</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Herein we report the synthesis and evaluation of peptide-histidinal conjugated drug scaffolds, which have the potential to target the hemoglobin-degrading proteases falcipain-2/3 from the human malaria parasite. Scaffolds with various substitutions were tested for antimalarial activity, and compounds 8 g, 8 h, and 15 exhibited EC50 values of similar to 0.018 mu M, similar to 0.069 mu M, and similar to 0.02 mu M, respectively. Structure-based docking studies on falcipain-2/3 proteases (PDB:2GHU and PDB:3BWK) revealed that compounds 8 g, 8 h, and 15 interact strongly with binding sites of falcipain-2/3 in a substrate-like manner. In silico ADME studies revealed that the molecules of interest showed no or minimal violations of drug-likeness parameters. Further, phenotypic assays revealed that compound 8 g and its biotinylated version inhibit hemoglobin degradation in the parasite food vacuole. The identification of falcipain-2/3 targeting potent inhibitors of the malaria parasite can serve as a starting point for the development of lead compounds as future antimalarial drug candidates.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">9</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	3.540&lt;/p&gt;
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