ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Crystallization and preliminary X-ray crystallographic study of phosphoglucose isomerase from Plasmodium falciparum.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- In vitro antiplasmodial activity of cepharanthine.Malaria journal · 2014Article
- Biosynthesis of GDP-fucose and other sugar nucleotides in the blood stages of Plasmodium falciparum.The Journal of biological chemistry · 2013Article
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Authors and funding
8 authors at 4 institutions in 1 country.
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Abstract
Phosphoglucose isomerase (PGI) is a key enzyme in glycolysis and glycogenesis that catalyses the interconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P). For crystallographic studies, PGI from the human malaria parasite Plasmodium falciparum (PfPGI) was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data to 1.5 A resolution were collected from an orthorhombic crystal form belonging to space group P2(1)2(1)2(1) with unit-cell parameters a = 103.3, b = 104.1, c = 114.6 A. Structural analysis by molecular replacement is in progress.
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