Mechanism of praziquantel action at a parasitic flatworm ion channel

Author:

Park Sang-Kyu1ORCID,Friedrich Lukas2ORCID,Yahya Nawal A.13ORCID,Rohr Claudia M.1ORCID,Chulkov Evgeny G.1ORCID,Maillard David4,Rippmann Friedrich2ORCID,Spangenberg Thomas5ORCID,Marchant Jonathan S.1ORCID

Affiliation:

1. Department of Cell Biology, Neurobiology and Anatomy, Medical College of Wisconsin, Milwaukee WI 53226, USA.

2. Computational Chemistry and Biology, Global Research & Development, Discovery Technologies, Merck Healthcare, Frankfurter Str. 250, 64293 Darmstadt, Germany.

3. Department of Pharmacology, University of Minnesota Medical School, 312 Church Street, Minneapolis, MN 55455, USA.

4. Central Process Development - Downstream Processing Services, Merck Performance Materials, Frankfurter Street 250, 64293 Darmstadt, Germany.

5. Global Health Institute of Merck, Ares Trading S.A., a subsidiary of Merck KGaA, Darmstadt, Germany, 1262 Eysins, Switzerland.

Abstract

Parasitic flatworm sensitivity to praziquantel is determined by amino acid variation in the binding pocket of a TRP channel.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

General Medicine

Reference41 articles.

1. Human schistosomiasis

2. The unacknowledged impact of chronic schistosomiasis

3. Schistosomiasis — Assessing Progress toward the 2020 and 2025 Global Goals

4. World Health Organization Ending the neglect to attain the Sustainable Development Goals—A road map for neglected tropical diseases 2021–2030. World Health Organ. Monogr. Ser. (2020).

5. Antiparasitics in Animal Health: Quo Vadis?

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