ArticleInternational journal of molecular sciences2024
Assessing the Efficacy of Protease Inactivation for the Preservation of Bioactive Amphibian Skin Peptides.
Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
The trial behind it
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
2 citing papers in PubMed.
- ExD identification of C-terminal Ile/Leu in natural peptides using d-ions.Analytical and bioanalytical chemistry · 2026Article
- The Road to the Full Sequencing of Natural Frogs' Peptides Relying Solely on Mass Spectrometry.Mass spectrometry (Tokyo, Japan) · 2025Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The skin of amphibians is a rich source of peptides with a wide range of biological activities. They are stored in secretory granules in an inactive form. Upon stimulation, they are secreted together with proteases into the skin. Once activated, they rapidly exert their biological effects, including fighting microorganisms and predators, while their excess is immediately destroyed by the released proteases. To keep bioactive peptides in their initial form, it is necessary to inhibit these enzymes. Several inhibitors for this purpose have previously been mentioned; however, there has not been any reliable comparison of their efficiency so far. Here, we studied the efficiency of methanol and hydrochloric and formic acids, as well as phenylmethylsulfonyl fluoride, in the inhibition of nine frog peptides with the known sequence, belonging to five families in the secretion of
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Registered trials
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