Evidence map›Paper›PMID 15266051›Full record

ArticlePlant physiology2004

Activity profiling of papain-like cysteine proteases in plants.

Renier A L van der Hoorn, Michiel A Leeuwenburgh, Matthew Bogyo, Matthieu H A J Joosten, Scott C Peck

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

62 citing papers in PubMed, 156 citations in OpenAlex.

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  11. The root pathogenFrontiers in plant science · 2023
    Article
  12. Article
  13. Knockout of a papain-like cysteine protease geneFrontiers in plant science · 2022
    Article
  14. Article
  15. Article
  16. Article
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  20. Article

2 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

5 authors at 3 institutions in 2 countries.

Renier A L van der HoornLaboratory of Phytopathology, Wageningen University, 6709 PD, Wageningen, The Netherlands. renier.vanderhoorn@wur.nl
Michiel A Leeuwenburgh
Matthew Bogyo
Matthieu H A J Joosten
Scott C Peck
John Innes Centre · GBLeiden University · NLSainsbury Laboratory · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcriptomic and proteomic technologies are generating a wealth of data that are frequently used by scientists to predict the function of proteins based on their expression or presence. However, activity of many proteins, such as transcription factors, kinases, and proteases, depends on posttranslational modifications that frequently are not detected by these technologies. Therefore, to monitor activity of proteases rather than their abundance, we introduce protease activity profiling in plants. This technology is based on the use of biotinylated, irreversible protease inhibitors that react with active proteases in a mechanism-based manner. Using a biotinylated derivative of the Cys protease inhibitor E-64, we display simultaneous activities of many papain-like Cys proteases in extracts from various tissues and from different plant species. Labeling is pH dependent, stimulated with reducing agents, and inhibited specifically by Cys protease inhibitors but not by inhibitors of other protease classes. Using one-step affinity capture of biotinylated proteases followed by sequencing mass spectrometry, we identified proteases that include xylem-specific XCP2, desiccation-induced RD21, and cathepsin B- and aleurain-like proteases. Together, these results demonstrate that this technology can identify differentially activated proteases and/or characterize the activity of a particular protease within complex mixtures.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBotanyCysteine EndopeptidasesMolecular Sequence DataPeptide FragmentsPlantsProtein Array AnalysisArabidopsis ProteinsCysteine EndopeptidasesPeptide Fragments

Identifiers

PMID15266051
PMCPMC519038
OpenAlexW2140883753

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.