ArticleMolecular and biochemical parasitology2019
The crystal structure of glucokinase from Leishmania braziliensis.
Article in Molecular and biochemical parasitology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed, 7 citations in OpenAlex.
- Immunoinformatics-Driven Identification of Conserved Multi-Epitope Vaccine Candidates from PDI Protein of Leishmania Donovani for Visceral Leishmaniasis.Cell biochemistry and biophysics · 2026Article
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4 authors at 2 institutions in 1 country.
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Abstract
Glucokinase from pathogenic protozoa of the genus Leishmania is a potential drug target for the chemotherapeutic treatment against leishmaniasis because this enzyme is located at a nodal point between two critically important metabolic pathways, glycolysis and the pentose phosphate pathway (PPP). L. braziliensis glucokinase (LbGlcK) was evaluated for its structural characterization and enzymatic performance. The enzyme catalyzes the phosphorylation of d-glucose with co-substrate ATP to yield the products G6P and ADP. LbGlcK had K
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