ArticleScientific reports2019
An Internally Quenched Fluorescent Peptide Substrate for Protealysin.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Thermostable neutral metalloprotease from Geobacillus sp. EA1 does not share thermolysin's preference for substrates with leucine at the P1' position.FEBS letters · 2025Article
- A centenarian single nucleotide polymorphism in collagen gene COL25A1 promotes longevity in C. elegans.npj aging · 2025Article
- Protease S of entomopathogenic bacterium Photorhabdus laumondii: expression, purification and effect on greater wax moth Galleria mellonella.Molecular biology reports · 2024Article
- NMR structure of emfourin, a novel protein metalloprotease inhibitor: Insights into the mechanism of action.The Journal of biological chemistry · 2023Article
- Assay for Protealysin-like Protease Inhibitor Activity.Bio-protocol · 2022Article
- Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA.International journal of molecular sciences · 2022Article
- The role of polymeric chains as a protective environment for improving the stability and efficiency of fluorogenic peptide substrates.Scientific reports · 2022Article
- Evaluation of the effects of phosphorylation of synthetic peptide substrates on their cleavage by caspase-3 and -7.The Biochemical journal · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protealysin, a metalloprotease of Serratia proteamaculans, is the prototype of a subgroup of the M4 peptidase family. Protealysin-like proteases (PLPs) are widely spread in bacteria but also occur in fungi and certain archaea. The interest in PLPs is primarily due to their putative involvement in the bacterial pathogenesis in animals and plants. Studying PLPs requires an efficient quantitative assay for their activity; however, no such assay has been reported so far. Here, we used the autoprocessing site sequence of the protealysin precursor to construct an internally quenched fluorescent peptide substrate 2-aminobenzoyl-L-arginyl-L-seryl-L-valyl-L-isoleucyl-L-(ε-2,4-dinitrophenyl)lysine. Protealysin and thermolysin, the prototype of the M4 family, proved to hydrolyze only the Ser-Val bond of the substrate. The substrate exhibited a K
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.