ArticleThe Biochemical journal2004
Reduction of anti-leishmanial pentavalent antimonial drugs by a parasite-specific thiol-dependent reductase, TDR1.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.
What it found
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Who cites it
46 citing papers in PubMed, 1 synthesis or guideline pooled it, 140 citations in OpenAlex.
- Leishmania spp. genetic factors associated with cutaneous leishmaniasis antimony pentavalent drug resistance: a systematic review.Memorias do Instituto Oswaldo Cruz · 2024Pooled it
- Unresponsiveness to Glucantime treatment in Iranian cutaneous leishmaniasis due to drug-resistant Leishmania tropica parasites.PLoS medicine · 2006Trial
- Trivalent and Pentavalent Antimonials Impair Cardiac Mitochondrial Function in Mice.International journal of molecular sciences · 2025Article
- Unraveling the functional dynamics of Caenorhabditis elegans stress-responsive omega class GST-44.The FEBS journal · 2025Article
- Antimony resistance and gene expression inParasitology · 2024Review
- An Overview on Leishmaniasis in Romania: Diagnosis and Therapeutics.Tropical medicine and infectious disease · 2022Review
- Global distribution of treatment resistance gene markers for leishmaniasis.Journal of clinical laboratory analysis · 2022Review
- Availability, Toxicology and Medical Significance of Antimony.International journal of environmental research and public health · 2022Review
- Glutathione Is Involved in the Reduction of Methylarsenate to Generate Antibiotic Methylarsenite in Enterobacter sp. Strain CZ-1.Applied and environmental microbiology · 2022Article
- Antimony resistance mechanism in genetically different clinical isolates of Indian Kala-azar patients.Frontiers in cellular and infection microbiology · 2022Article
- Serine proteases profiles of Leishmania (Viannia) braziliensis clinical isolates with distinct susceptibilities to antimony.Scientific reports · 2021Article
- Determinants of Unresponsiveness to Treatment in Cutaneous Leishmaniasis: A Focus on Anthroponotic Form Due toFrontiers in microbiology · 2021Review
- Article
- Antimony susceptibility of Leishmania isolates collected over a 30-year period in Algeria.PLoS neglected tropical diseases · 2018Article
- Profiling gene expression of antimony response genes in Leishmania (Viannia) panamensis and infected macrophages and its relationship with drug susceptibility.Acta tropica · 2017Article
- Involvement of nucleoside diphosphate kinase b and elongation factor 2 in Leishmania braziliensis antimony resistance phenotype.Parasites & vectors · 2016Article
- The LABCG2 Transporter from the Protozoan Parasite Leishmania Is Involved in Antimony Resistance.Antimicrobial agents and chemotherapy · 2016Article
- Article
- Synthesis and characterization of bismuth(III) and antimony(V) porphyrins: high antileishmanial activity against antimony-resistant parasite.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- An alternate pathway of arsenate resistance in E. coli mediated by the glutathione S-transferase GstB.ACS chemical biology · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The reason why Leishmania parasites are susceptible to organic antimonial drugs, the standard chemotherapeutic agents for over 50 years, apparently lies in the fact that the mammalian stage of the parasite reduces the pentavalent form of the administered drug to a trivalent form that causes parasite death. We have identified and characterized a parasite-specific enzyme that can catalyse the reduction of pentavalent antimonials and may therefore be central to the anti-parasite activity of the drug. The unusual protein, a trimer of two-domain monomers in which each domain has some similarity to the Omega class glutathione S-transferases, is a thiol-dependent reductase (designated TDR1) that converts pentavalent antimonials into trivalent antimonials using glutathione as the reductant. The higher abundance of the enzyme in the mammalian stage of the parasite could explain why this parasite form is more susceptible to the drug.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.