ArticleBMC bioinformatics2017
Block-based characterization of protease specificity from substrate sequence profile.
Article in BMC bioinformatics, 2017. 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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Who cites it
2 citing papers in PubMed.
- The N-degron pathway governs autophagy to promote thermotolerance in Arabidopsis.Nature communications · 2025Article
- Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen.Nature communications · 2021Article
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Authors and funding
5 authors.
Funding
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Abstract
backgroundThe mechanism of action of proteases has been widely studied based on substrate specificity. Prior research has been focused on the amino acids at a single amino acid site, but rarely on combinations of amino acids around the cleavage bond.
resultsWe propose a novel block-based approach to reveal the potential combinations of amino acids which may regulate the action of proteases. Using the entropies of eight blocks centered at a cleavage bond, we created a distance matrix for 61 proteases to compare their specificities. After quantitative analysis, we discovered a number of prominent blocks, each of which consists of successive amino acids near a cleavage bond, intuitively characterizing the site cooperation of the substrate sequences.
conclusionThis approach will help in the discovery of specific substrate sequences which may bridge between proteases and cleavage substrate as more substrate information becomes available.
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