Evidence map›Paper›PMID 18705889›Full record

ReviewMolecular plant pathology2008

Papain-like cysteine proteases: key players at molecular battlefields employed by both plants and their invaders.

Takayuki Shindo, Renier A L Van der Hoorn

Open access · greenAbstract readReview
In one paragraph

Review in Molecular plant pathology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

49 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. A Novel Cysteine Protease fromPlants (Basel, Switzerland) · 2025
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  10. Genome-Wide Identification and Characterization of theInternational journal of molecular sciences · 2021
    Article
  11. Article
  12. Papain-Like Cysteine Protease Gene Family in Fig (Frontiers in plant science · 2021
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  14. 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

2 authors at 1 institution in 1 country.

Takayuki ShindoPlant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, 50829 Cologne, Germany.
Renier A L Van der Hoorn
Max Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Papain-like cysteine proteases (PLCPs) play crucial roles in plant-pathogen/pest interactions. During these parasitic interactions, PLCPs act on non-self substrates, provoking the selection of counteracting inhibitors and other means to evade proteolysis. We review examples of PLCPs acting on molecular battlefields in the extracellular space, plant cytoplasm and herbivore gut. Examples are maize Mir1 (Maize inbred resistance 1), tomato Rcr3 (Required for Cladosporium resistance-3), Pseudomonas AvrRpt2 and AurPphB, insect DvCAL1 (Diabrotica virgifera cathepsin L-like protease-1) and nematode MiCpl1 (Meloidogyne incognita cathepsin L-like protease 1). The data suggest that PLCPs cleave specific proteins and that their translocation, activation and inhibition of PLCPs are tightly regulated.

Indexed as

Host-Parasite InteractionsHost-Pathogen InteractionsAnimalsColeopteraCysteine EndopeptidasesPapainPlant DiseasesPlantsPseudomonas syringaeTylenchoideaCysteine EndopeptidasesPapain

Identifiers

PMID18705889
PMCPMC6640327
OpenAlexW2062182037

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.