Evidence map›Paper›PMID 36755073›Full record

ReviewCell death and differentiation2023

Mechanisms controlling plant proteases and their substrates.

Álvaro Daniel Fernández-Fernández, Simon Stael, Frank Van Breusegem

Open access · greenAbstract readReview
In one paragraph

Review in Cell death and differentiation, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
6.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Processing and release of endogenous immunogenic peptide signals.The Plant journal : for cell and molecular biology · 2026
    Review
  3. A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 3 institutions in 3 countries.

Álvaro Daniel Fernández-FernándezDepartment of Plant Biotechnology and Bioinformatics, Ghent University, 9052, Ghent, Belgium.ORCID http://orcid.org/0000-0003-4770-9757
Simon StaelDepartment of Plant Biotechnology and Bioinformatics, Ghent University, 9052, Ghent, Belgium.
Frank Van BreusegemDepartment of Plant Biotechnology and Bioinformatics, Ghent University, 9052, Ghent, Belgium. frank.vanbreusegem@psb.vib-ugent.be.ORCID http://orcid.org/0000-0002-3147-0860
Ghent University · BESwedish University of Agricultural Sciences · SEUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plants, proteolysis is emerging as an important field of study due to a growing understanding of the critical involvement of proteases in plant cell death, disease and development. Because proteases irreversibly modify the structure and function of their target substrates, proteolytic activities are stringently regulated at multiple levels. Most proteases are produced as dormant isoforms and only activated in specific conditions such as altered ion fluxes or by post-translational modifications. Some of the regulatory mechanisms initiating and modulating proteolytic activities are restricted in time and space, thereby ensuring precision activity, and minimizing unwanted side effects. Currently, the activation mechanisms and the substrates of only a few plant proteases have been studied in detail. Most studies focus on the role of proteases in pathogen perception and subsequent modulation of the plant reactions, including the hypersensitive response (HR). Proteases are also required for the maturation of coexpressed peptide hormones that lead essential processes within the immune response and development. Here, we review the known mechanisms for the activation of plant proteases, including post-translational modifications, together with the effects of proteinaceous inhibitors.

Indexed as

EndopeptidasesPeptide HydrolasesPlantsProtein Processing, Post-TranslationalProteolysisEndopeptidasesPeptide Hydrolases

Identifiers

PMID36755073
PMCPMC10070405
OpenAlexW4319459064

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.