ArticleActa crystallographica. Section F, Structural biology communications2017
Structure of a fungal form of aspartate-semialdehyde dehydrogenase from Aspergillus fumigatus.
Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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
3 citing papers in PubMed, 11 citations in OpenAlex.
- Subtractive Proteomics-Based Prioritization of Drug Targets in Enterococcus faecalis V583 and Structure-Based Identification of Plant-Derived Inhibitors Targeting Alanine Racemase: A High Priority Target.Molecular biotechnology · 2026Article
- Structural characterization of aspartate-semialdehyde dehydrogenase from Pseudomonas aeruginosa and Neisseria gonorrhoeae.Scientific reports · 2022Article
- Structure of aspartate β-semialdehyde dehydrogenase from Francisella tularensis.Acta crystallographica. Section F, Structural biology communications · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Aspartate-semialdehyde dehydrogenase (ASADH) functions at a critical junction in the aspartate biosynthetic pathway and represents a validated target for antimicrobial drug design. This enzyme catalyzes the NADPH-dependent reductive dephosphorylation of β-aspartyl phosphate to produce the key intermediate aspartate semialdehyde. The absence of this entire pathway in humans and other mammals will allow the selective targeting of pathogenic microorganisms for antimicrobial development. Here, the X-ray structure of a new form of ASADH from the pathogenic fungal species Aspergillus fumigatus has been determined. The overall structure of this enzyme is similar to those of its bacterial orthologs, but there are some critical differences both in biological assembly and in secondary-structural features that can potentially be exploited for the development of species-selective drugs with selective toxicity against infectious fungal organisms.
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