ArticleThe Biochemical journal1985
The selectivity of action of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae).
Article in The Biochemical journal, 1985. 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.
- Test and Evaluation of ff99IDPs Force Field for Intrinsically Disordered Proteins.Journal of chemical information and modeling · 2015Article
- Predicting functional residues of the Solanum lycopersicum aspartic protease inhibitor (SLAPI) by combining sequence and structural analysis with molecular docking.Journal of molecular modeling · 2012Article
- Multi-scaled explorations of binding-induced folding of intrinsically disordered protein inhibitor IA3 to its target enzyme.PLoS computational biology · 2011Article
- Article
- A systematic series of synthetic chromophoric substrates for aspartic proteinases.The Biochemical journal · 1986Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The ability of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae) to affect the activities of a range of mammalian and microbial aspartic proteinases was examined. The inhibitor appeared to be completely selective in that only the aspartic proteinase A from yeast was inhibited to any significant extent. IA3 thus represents the first example of a totally specific, naturally occurring, aspartic-proteinase inhibitor.
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Registered trials
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