Evidence map›Paper›PMID 39658213›Full record

ReviewJournal of experimental botany2025

RD21-like proteases: key effector hubs in plant-pathogen interactions.

Jie Huang, Renier A L van der Hoorn

Abstract readReview
In one paragraph

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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. SsPit2A/B Effectors fromPlants (Basel, Switzerland) · 2026
    Article
  5. 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
  6. Review
  7. Pathogen-inspired engineering of plant protease enhances late blight resistance.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
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

2 authors.

Jie HuangThe Plant Chemetics Laboratory, Department of Biology, University of Oxford, Oxford OX1 3RB, UK.ORCID 0000-0002-6657-8740
Renier A L van der HoornThe Plant Chemetics Laboratory, Department of Biology, University of Oxford, Oxford OX1 3RB, UK.ORCID 0000-0002-3692-7487

Funding

BBSRC BB/Y000560/1
6 · The paper itself

Abstract

Over the past decades, numerous studies have demonstrated that proteases serve as a crucial regulatory mechanism in controlling plant immunity. In this review, we specifically focus on the role of one subfamily of RD21-like papain-like cysteine proteases that carry a C-terminal granulin domain. These proteases share high homology but have been described under very different names in different plant species. We provide a comprehensive overview of the background, endogenous regulation, and subcellular localization of RD21-like proteases in plants. Notably, RD21-like proteases act in immunity against various pathogens and they are targeted by many unrelated pathogen-secreted effectors that inactivate, mislocalize, or degrade RD21-like proteases. We highlight open questions and strategies to use this knowledge to develop innovative approaches for crop protection.

Indexed as

Cysteine ProteasesHost-Pathogen InteractionsPeptide HydrolasesPlant DiseasesPlant ImmunityPlant ProteinsPlantsCysteine ProteasesPeptide HydrolasesPlant ProteinseffectorInhibitorpapain-like cysteine proteasesplant immunityplant proteaseRD21

Identifiers

PMID39658213
PMCPMC12485362

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.