ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Purification, crystallization and preliminary X-ray analysis of the aspartate aminotransferase of 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 5 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
5 citing papers in PubMed, 11 citations in OpenAlex.
- Hydroxylamine and Carboxymethoxylamine Can InhibitAntimicrobial agents and chemotherapy · 2020Article
- Article
- Purification, crystallization and preliminary X-ray diffraction analysis of pyridoxal kinase from Plasmodium falciparum (PfPdxK).Acta crystallographica. Section F, Structural biology communications · 2014Article
- Vitamin B6-dependent enzymes in the human malaria parasite Plasmodium falciparum: a druggable target?BioMed research international · 2014Review
- Serum biochemical analysis to indicate pathogenic risk on mouse Mus musculus exposure to source of drinking water.Ecotoxicology (London, England) · 2011Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aspartate aminotransferases (EC 2.6.1.1) catalyse the conversion of aspartate and alpha-ketoglutarate to oxaloacetate and glutamate in a reversible manner. Thus, the aspartate aminotransferase of Plasmodium falciparum (PfAspAT) plays a central role in the transamination of amino acids. Recent findings suggest that PfAspAT may also play a pivotal role in energy metabolism and the de novo biosynthesis of pyrimidines. While therapeutics based upon the inhibition of other proteins in these pathways are already used in the treatment of malaria, the advent of multidrug-resistant strains has limited their efficacy. The presence of PfAspAT in these pathways may offer additional opportunities for the development of novel therapeutics. In order to gain a deeper understanding of the function and role of PfAspAT, it has been expressed and purified to homogeneity. The successful crystallization of PfAspAT, the collection of a 2.8 A diffraction data set and initial attempts to solve the structure using molecular replacement are reported.
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