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The trematode liver fluke Fasciola hepatica causes the neglected tropical disease fascioliasis in humans and is associated with significant losses in agricultural industry due to reduced animal productivity. Triosephosphate isomerase (TPI) is a glycolytic enzyme that has been researched as a drug target for various parasites, including F. hepatica. The high-resolution crystal structure of F. hepatica TPI (FhTPI) has been solved at 1.51 Å resolution in its monoclinic form. The structure has been used to perform molecular-docking studies with the most successful fasciolocide triclabendazole (TCBZ), which has recently been suggested to target FhTPI. Two FhTPI residues, Lys50 and Asp51, are located at the dimer interface and are found in close proximity to the docked TCBZ. These residues are not conserved in mammalian hosts.
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http://dx.doi.org/10.1107/S2053230X25006454 | DOI Listing |
Exp Cell Res
September 2025
Department of Urology, the Affiliated Hospital of Zunyi Medical University, Zunyi 563000, Guizhou, China. Electronic address:
Prostate cancer (PCa) is a type of malignancy that originates in the prostate gland, often characterized by uncontrolled cell growth and potential metastasis. Long non-coding RNAs (lncRNAs) play crucial regulatory roles in the progression of prostate cancer, potentially facilitating tumor growth and metastasis via mechanisms that involve the enhancement of aerobic glycolysis. This study aimed to investigate the functional role of lncRNA HANR in prostate cancer progression.
View Article and Find Full Text PDFInt J Parasitol
September 2025
Department of Clinical Science, Faculty of Medicine, University of Bergen, Norway; National Centre for Tropical Infectious Diseases, Medical department, Haukeland University Hospital, Bergen, Norway. Electronic address:
Giardia duodenalis is a gastrointestinal parasite and one of the most frequently reported parasitic infections associated with contaminated water. This study investigated the diversity of domestic and imported Giardia assemblages in Norway, with a focus on the genetic characterization of domestic assemblage A isolates using multi-locus sequence typing (MLST) targeting six genome markers. We analysed 340 human, and 40 animal faecal samples collected between February 2022 and January 2024 from six medical microbiology laboratories and one veterinary diagnostic center across four Norwegian health regions.
View Article and Find Full Text PDFMol Genet Metab
August 2025
Department of Molecular and Human Genetics, Baylor Coll. of Medicine, Houston, TX, United States; Texas Children's Hospital, Houston, TX, United States; Baylor Genetics, Houston, TX, United States; Joint BCM-CUHK Center of Medical Genetics, Prince of Wales Hospital, ShaTin, Hong Kong, China. Electro
Triosephosphate isomerase (TPI) is a ubiquitously expressed enzyme encoded by the TPI1 gene. It catalyzes the interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate in the fifth step of glycolysis. TPI deficiency (TPI Df; MIM# 615512) is an autosomal recessive disorder due to biallelic pathogenic variants in TPI1.
View Article and Find Full Text PDFActa Crystallogr F Struct Biol Commun
September 2025
Henry Wellcome Building for Biocatalysis, Biosciences, Faculty of Health and Life Sciences, University of Exeter, Exeter EX4 4QD, United Kingdom.
The trematode liver fluke Fasciola hepatica causes the neglected tropical disease fascioliasis in humans and is associated with significant losses in agricultural industry due to reduced animal productivity. Triosephosphate isomerase (TPI) is a glycolytic enzyme that has been researched as a drug target for various parasites, including F. hepatica.
View Article and Find Full Text PDFSci Adv
August 2025
State Key Laboratory of Biocontrol, Guangdong Key Laboratory of Pharmaceutical Functional Genes, School of Life Sciences, Southern Marine Science and Engineering Guangdong Laboratory (Zhuhai), Sun Yat-sen University, Guangzhou 510275, China.
The mechanisms that organisms allocate resources to sustain biological phenotypes remain largely unknown. Here, we use mobilized colistin resistance (), which modifies lipopolysaccharide (LPS) to confer colistin resistance, as a model to explore how bacteria reallocate resources to support -mediated resistance. We show that bacteria redirect resources from glycolysis, the pyruvate cycle, and LPS biosynthesis toward glycerophospholipid metabolism to produce phosphatidylethanolamine, the substrate for to modify LPS, while reducing LPS content to limit colistin binding.
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