Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Inhibition Mechanism of Antimalarial Drugs Targeting the Cytochrome bc1 Complex.

Journal of chemical information and modeling - 22 Mar 2021

Jacobsen Luise, Husen Peter, Solov'yov Ilia A

Abstract excerpt

Plasmodium falciparum (P. falciparum) is the main parasite known to cause malaria in humans. The antimalarial drug atovaquone is known to inhibit the Qo-site of the cytochrome bc1 complex of P. falciparum, which ultimately blocks ATP synthesis, leading to cell death. Through the years, mutations of the P. falciparum cytochrome bc1 complex, causing resistance to atovaquone, have emerged. The present investigation...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antimalarials
Share to Computational Drug Discovery Methods

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytochromes

Share to Drug Resistance

Share to Malaria, Falciparum

Share to Malaria Research and Control

Share to Mutation

Share to Plasmodium falciparum

Source

Identifiers

PMID: 33617262
DOI: 10.1021/acs.jcim.0c01148

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inhibition Mechanism of Antimalarial Drugs Targeting the Cytochrome bc1 Complex.PMID 33617262Read ↗

Understanding the mechanism of atovaquone drug resistance in Plasmodium falciparum cytochrome b mutation Y268S using computational methods.Semantic proximity Read ↗

Decoding the Molecular Effects of Atovaquone Linked Resistant Mutations on Plasmodium falciparum Cytb-ISP Complex in the Phospholipid Bilayer Membrane.Semantic proximity Read ↗

Uncovering the molecular mode of action of the antimalarial drug atovaquone using a bacterial system.Semantic proximity Read ↗

Structure-based therapeutic development against the Apicomplexan parasitesSemantic proximity Read ↗

Cytochrome b mutations that modify the ubiquinol-binding pocket of the cytochrome bc1 complex and confer anti-malarial drug resistance in Saccharomyces cerevisiae.Semantic proximity Read ↗

Molecular and biochemical pharmacology of mitochondrial enzymes in the malaria parasite Plasmodium falciparumSemantic proximity Read ↗

Cytochrome b Mutation Y268S Conferring Atovaquone Resistance Phenotype in Malaria Parasite Results in Reduced Parasite bc1 Catalytic Turnover and Protein ExpressionSemantic proximity Read ↗

Therapeutics development against the Apicomplexa parasites Plasmodium falciparum and Toxoplasma gondiiSemantic proximity Read ↗

Direct evidence for the atovaquone action on the Plasmodium cytochrome bc1 complex.Semantic proximity Read ↗

Mutation underlying resistance of Plasmodium berghei to atovaquone in the quinone binding domain 2 (Qo(2)) of the cytochrome b gene.Semantic proximity Read ↗

Mitochondrial Drug Targets in Apicomplexan ParasitesSemantic proximity Read ↗

The interaction of atovaquone with the P. carinii cytochrome bc1 complex.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.