Literature summary for 2.5.1.10 extracted from

Muenzker, L.; Petrick, J.K.; Schleberger, C.; Clavel, D.; Cornaciu, I.; Wilcken, R.; Marquez, J.A.; Klebe, G.; Marzinzik, A.; Jahnke, W.
Fragment-based discovery of non-bisphosphonate binders of Trypanosoma brucei farnesyl pyrophosphate synthase (2020), ChemBioChem, 2020, 1-17 .

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Application

Application	Comment	Organism
drug development	the discovery of new binding sites and non-bisphosphonate binders is a critical step towards the investigation of farnesyl pyrophosphate synthase as a drug target for human African trypanosomiasis and opens up the possibility of a fragment-to-lead optimisation program	Trypanosoma brucei

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Trypanosoma brucei

Organism

Organism	UniProt	Comment	Textmining
Trypanosoma brucei	Q86C09	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Trypanosoma brucei

General Information

General Information	Comment	Organism
drug target	Trypanosoma brucei is the causative agent of human African trypanosomiasis. Nitrogen-containing bisphosphonates, a current treatment for bone diseases, have been shown to block the growth of the Trypanosoma brucei parasites by inhibiting farnesyl pyrophosphate synthase. However, due to their poor pharmacokinetic properties, they are not well suited for antiparasitic therapy. Tthe discovery of new binding sites and non-bisphosphonate binders is a critical step towards the investigation of farnesyl pyrophosphate synthase as a drug target for human African trypanosomiasis and opens up the possibility of a fragment-to-lead optimisation program	Trypanosoma brucei

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Release 2023.1 (January 2023)