ReviewJournal of experimental botany2025
Four guidelines to identify bona fide protease-substrate pairs.
Review in Journal of experimental botany, 2025. 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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- Linker Design in Antibody-Drug Conjugates: Balancing Stability and Drug Release.Pharmaceutics · 2026Review
- Plant proteases: guardians of proteome integrity and regulators of protein function.Journal of experimental botany · 2025Article
- Marine macroalgae-associated fungi from Yacila and Los Cangrejos beaches (Northern Peru) and previously selected marine bacteria evaluated as plant growth promoters in maize under saline stress.Frontiers in fungal biology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Plant proteases are an important class of enzymes, with proposed involvement in various aspects of the plant life cycle. However, pinpointing authentic protease-substrate interactions remains challenging, which hinders a comprehensive understanding of the biological function of proteases. Moreover, a structured set of guidelines to validate protease substrates is lacking. In this review, we outline a minimum of four key guidelines that, when followed, can confirm the specificity of protease-substrate interaction for proteases that perform limited proteolysis and with specific cleavage sites: (i) the observation of substrate cleavage; (ii) the reduction in substrate cleavage due to protease inhibitors or (iii) genetic mutation of the protease; and (iv) a final proof of the specificity of the substrate cleavage site. It is important to emphasize that these guidelines are not universally applicable to all proteases. By creating a set of guidelines, summarizing current findings and proposing future research directions, this review aims to highlight innovative techniques that will improve the specificity and accuracy of protease research and facilitate a deeper understanding of the role of proteases in plant biology.
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What OpenQuestion holds
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.