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Alteration of redox status by commonly used antimalarial drugs in the north-western region of Nigeria
A Muhammad, MA Ibrahim, HA Mohammed, OL Erukainure, I Malami, A Suleiman, A Mansir, A Godwin and HA Khalil Human & Experimental Toxicology 36(2) 176 (2017) https://doi.org/10.1177/0960327116641735
In VivoAntimalarial Activity ofAnnona muricataLeaf Extract in Mice Infected withPlasmodium berghei
Effects of 5,8-dimethylthieno[2,3-b]quinoline-2-carboxylic acid on the antioxidative defense and lipid membranes in Plasmodium berghei-infected erythrocytes
Néstor Aarón Mosqueda-Romo, Ana Laura Rodríguez-Morales, Fidel Orlando Buendía-González, et al. BioMed Research International 2014 1 (2014) https://doi.org/10.1155/2014/805495
Antiplasmodial properties of kaempferol-3-O-rhamnoside isolated from the leaves of Schima wallichii against chloroquine-resistant Plasmodium falciparum
New antimalarial indolone-N-oxides, generating radical species, destabilize the host cell membrane at early stages of Plasmodium falciparum growth: role of band 3 tyrosine phosphorylation
Pyrimethamine induces oxidative stress in Plasmodium yoelii 17XL-infected mice: A novel immunomodulatory mechanism of action for an old antimalarial drug?
Martha Legorreta-Herrera, Raquel Retana-Ugalde, José Luis Ventura-Gallegos and Verónica Narváez Experimental Parasitology 126(3) 381 (2010) https://doi.org/10.1016/j.exppara.2010.02.013
Targeting glutathione by dimethylfumarate protects against experimental malaria by enhancing erythrocyte cell membrane scrambling
Mehrdad Ghashghaeinia, Diwakar Bobbala, Thomas Wieder, Saisudha Koka, Jürgen Brück, Birgit Fehrenbacher, Martin Röcken, Martin Schaller, Florian Lang and Kamran Ghoreschi American Journal of Physiology-Cell Physiology 299(4) C791 (2010) https://doi.org/10.1152/ajpcell.00014.2010
Effect of dequalinium on the oxidative stress in Plasmodium berghei-infected erythrocytes
Modification of oxidative status in Plasmodium berghei-infected erythrocytes by E-2-chloro-8-methyl-3-[(4'-methoxy-1'-indanoyl)-2'-methyliden]-quinoline compared to chloroquine
N1‐acetyl‐N2‐formyl‐5‐methoxykynuramine modulates the cell cycle of malaria parasites
Alexandre Budu, Rafael Peres, Vânia Blasques Bueno, Luiz Henrique Catalani and Célia Regina da Silva Garcia Journal of Pineal Research 42(3) 261 (2007) https://doi.org/10.1111/j.1600-079X.2006.00414.x
Decreased glutathione-S-transferase activity: Diagnostic and protective role in vivax malaria
Thioredoxin Reductase Is Essential for the Survival ofPlasmodium falciparum Erythrocytic Stages
Zita Krnajski, Tim-Wolf Gilberger, Rolf D. Walter, Alan F. Cowman and Sylke Müller Journal of Biological Chemistry 277(29) 25970 (2002) https://doi.org/10.1074/jbc.M203539200
Nutritional and racial determinants of the increase in plasma homocysteine levels after methionine loading
Antiplasmodial Activity of Nitroaromatic and Quinoidal Compounds: Redox Potential vs Inhibition of Erythrocyte Glutathione Reductase
Philippe Grellier, Jonas Šarlauskas, Žilvinas Anusevičius, et al. Archives of Biochemistry and Biophysics 393(2) 199 (2001) https://doi.org/10.1006/abbi.2001.2487
The malaria parasite Plasmodium falciparum possesses a functional thioredoxin system
Potent antimalarial activity of clotrimazole in
in vitro
cultures of
Plasmodium falciparum
Teresa Tiffert, Hagai Ginsburg, Miriam Krugliak, Barry C. Elford and Virgilio L. Lew Proceedings of the National Academy of Sciences 97(1) 331 (2000) https://doi.org/10.1073/pnas.97.1.331
Management of HIV-infected pregnant patients in malaria-endemic areas: Therapeutic and safety considerations in concomitant use of antiretroviral and antimalarial agents
The Malaria Parasite Supplies Glutathione to its Host Cell — Investigation of Glutathione Transport and Metabolism in Human Erythrocytes Infected with Plasmodium Falciparum
Resistance of glucose-6-phosphate dehydrogenase deficiency to malaria: effects of fava bean hydroxypyrimidine glucosides onPlasmodium falciparumgrowth in culture and on the phagocytosis of infected cells
Plasmodium falciparum glutathione reductase exhibits sequence similarities with the human host enzyme in the core structure but differs at the ligand-binding sites
Sylke Müller, Katja Becker, Bärbel Bergmann, R.Heiner Schirmer and Rolf D. Walter Molecular and Biochemical Parasitology 74(1) 11 (1995) https://doi.org/10.1016/0166-6851(95)02476-X
Redox processes in malaria and other parasitic diseases