Structures of Plasmodium falciparum Chloroquine Resistance Transporter (PfCRT) Isoforms and Their Interactions with Chloroquine
Author:
Affiliation:
1. Departments of Chemistry and Biochemistry and Cellular and Molecular Biology, Georgetown University, 37th and O Streets NW, Washington, District of Columbia 20057, United States
Funder
National Institute of Allergy and Infectious Diseases
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.2c00669
Reference64 articles.
1. Mutations in the P. falciparum Digestive Vacuole Transmembrane Protein PfCRT and Evidence for Their Role in Chloroquine Resistance
2. The Antimalarial Drug Resistance Protein Plasmodium falciparum Chloroquine Resistance Transporter Binds Chloroquine
3. Chloroquine Transport via the Malaria Parasite’s Chloroquine Resistance Transporter
4. Chloroquine Transport in Plasmodium falciparum. 2. Analysis of PfCRT-Mediated Drug Transport Using Proteoliposomes and a Fluorescent Chloroquine Probe
5. Alternative Mutations at Position 76 of the Vacuolar Transmembrane Protein PfCRT Are Associated with Chloroquine Resistance and Unique Stereospecific Quinine and Quinidine Responses inPlasmodium falciparum
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1. Additional PfCRT mutations driven by selective pressure for improved fitness can result in the loss of piperaquine resistance and altered Plasmodium falciparum physiology;mBio;2024-01-16
2. pH-dependence of the Plasmodium falciparum chloroquine resistance transporter is linked to the transport cycle;Nature Communications;2023-07-15
3. PfCRT mutations conferring piperaquine resistance in falciparum malaria shape the kinetics of quinoline drug binding and transport;PLOS Pathogens;2023-06-07
4. APlasmodium falciparumgenetic cross reveals the contributions ofpfcrtandplasmepsin II/IIIto piperaquine drug resistance;2023-06-07
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