Evidence map›Paper›PMID 22371507›Full record

ArticlePlant physiology2012

Subclassification and biochemical analysis of plant papain-like cysteine proteases displays subfamily-specific characteristics.

Kerstin H Richau, Farnusch Kaschani, Martijn Verdoes, Twinkal C Pansuriya, Sherry Niessen, Kurt Stüber, Tom Colby, Hermen S Overkleeft, Matthew Bogyo, Renier A L Van der Hoorn

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed, 1 pooled it
12.2field-weighted citation impact, top 1% 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

99 citing papers in PubMed, 1 synthesis or guideline pooled it, 204 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. SsPit2A/B Effectors fromPlants (Basel, Switzerland) · 2026
    Article
  6. Processing and release of endogenous immunogenic peptide signals.The Plant journal : for cell and molecular biology · 2026
    Review
  7. 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
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. A Novel Cysteine Protease fromPlants (Basel, Switzerland) · 2025
    Article
  18. Article
  19. Article
  20. Papain expression in theApplied and environmental microbiology · 2025
    Article

39 more citing papers are in PubMed but not listed here.

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

10 authors at 5 institutions in 3 countries.

Kerstin H RichauPlant Chemetics Laboratory, Chemical Genomics Centre of the Max Planck Society, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany.
Farnusch Kaschani
Martijn Verdoes
Twinkal C Pansuriya
Sherry Niessen
Kurt Stüber
Tom Colby
Hermen S Overkleeft
Matthew Bogyo
Renier A L Van der Hoorn
Chemical Genomics Centre · DEMax Planck Society · DELeiden University · NLMax Planck Institute for Plant Breeding Research · DEStanford University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Papain-like cysteine proteases (PLCPs) are a large class of proteolytic enzymes associated with development, immunity, and senescence. Although many properties have been described for individual proteases, the distribution of these characteristics has not been studied collectively. Here, we analyzed 723 plant PLCPs and classify them into nine subfamilies that are present throughout the plant kingdom. Analysis of these subfamilies revealed previously unreported distinct subfamily-specific functional and structural characteristics. For example, the NPIR and KDEL localization signals are distinctive for subfamilies, and the carboxyl-terminal granulin domain occurs in two PLCP subfamilies, in which some individual members probably evolved by deletion of the granulin domains. We also discovered a conserved double cysteine in the catalytic site of SAG12-like proteases and two subfamily-specific disulfides in RD19A-like proteases. Protease activity profiling of representatives of the PLCP subfamilies using novel fluorescent probes revealed striking polymorphic labeling profiles and remarkably distinct pH dependency. Competition assays with peptide-epoxide scanning libraries revealed common and unique inhibitory fingerprints. Finally, we expand the detection of PLCPs by identifying common and organ-specific protease activities and identify previously undetected proteases upon labeling with cell-penetrating probes in vivo. This study provides the plant protease research community with tools for further functional annotation of plant PLCPs.

Indexed as

Multigene FamilyAmino Acid MotifsAmino Acid SequenceArabidopsisConserved SequenceHydrogen-Ion ConcentrationIntercellular Signaling Peptides and ProteinsMolecular Sequence DataOrgan SpecificityPapainPeptide MappingPhylogenyPlantsProgranulinsProtease InhibitorsStaining and LabelingIntercellular Signaling Peptides and ProteinsPapainProgranulinsProtease Inhibitors

Identifiers

PMID22371507
PMCPMC3320171
OpenAlexW2117336992

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.