Evidence map›Paper›PMID 35510806›Full record

ArticleThe New phytologist2022

Broad-range metalloprotease profiling in plants uncovers immunity provided by defence-related metalloenzyme.

Kyoko Morimoto, Daniel Krahn, Farnusch Kaschani, Digby Hopkinson-Woolley, Anna Gee, Pierre Buscaill, Shabaz Mohammed, Stephan A Sieber, Benjamin F Cravatt, Christopher J Schofield and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The New phytologist, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Genome-Wide Identification of thePlants (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Review
  4. Article
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

11 authors at 4 institutions in 3 countries.

Kyoko MorimotoThe Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford, OX1 3RB, UK.ORCID 0000-0002-8113-9201
Daniel KrahnThe Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford, OX1 3RB, UK.
Farnusch KaschaniThe Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, Cologne, 50829, Germany.ORCID 0000-0001-6572-3232
Digby Hopkinson-WoolleyThe Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford, OX1 3RB, UK.
Anna GeeThe Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford, OX1 3RB, UK.ORCID 0000-0002-2801-4768
Pierre BuscaillThe Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford, OX1 3RB, UK.ORCID 0000-0003-4756-1203
Shabaz MohammedDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.ORCID 0000-0003-2640-9560
Stephan A SieberDepartment of Chemistry, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.ORCID 0000-0002-9400-906X
Benjamin F CravattDepartment of Chemistry, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.ORCID 0000-0001-5330-3492
Christopher J SchofieldDepartment of Chemistry and the Ineos Oxford Institute for Antimcrobial Research, University of Oxford, Mansfield Road, Oxford, OX1 3TA, UK.ORCID 0000-0002-0290-6565
Renier A L van der HoornThe Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford, OX1 3RB, UK.ORCID 0000-0002-3692-7487
University of Oxford · GBMansfield University · USScripps Research Institute · USMax Planck Institute for Plant Breeding Research · DE

Funding

Biotechnology and Biological Sciences Research Council BB/R017913/1
6 · The paper itself

Abstract

Plants encode > 100 metalloproteases representing > 19 different protein families. Tools to study this large and diverse class of proteases have not yet been introduced into plant research. We describe the use of hydroxamate-based photoaffinity probes to explore plant proteomes for metalloproteases. We detected labelling of 23 metalloproteases in leaf extracts of the model plant Arabidopsis thaliana that belong to nine different metalloprotease families and localize to different subcellular compartments. The probes identified several chloroplastic FtsH proteases, vacuolar aspartyl aminopeptidase DAP1, peroxisomal metalloprotease PMX16, extracellular matrix metalloproteases and many cytosolic metalloproteases. We also identified nonproteolytic metallohydrolases involved in the release of auxin and in the urea cycle. Studies on tobacco plants (Nicotiana benthamiana) infected with the bacterial plant pathogen Pseudomonas syringae uncovered the induced labelling of PRp27, a secreted protein with implicated metalloprotease activity. PRp27 overexpression increases resistance, and PRp27 mutants lacking metal binding site are no longer labelled, but still show increased immunity. Collectively, these studies reveal the power of broad-range metalloprotease profiling in plants using hydroxamate-based probes.

Indexed as

ArabidopsisArabidopsis ProteinsMetalloproteinsMetalloproteasesNicotianaPlant DiseasesPseudomonas syringaeArabidopsis ProteinsMetalloproteasesMetalloproteinsArabidopsisimmunitymetalloproteasesphotoaffinity labellingPRp27

Identifiers

PMID35510806
PMCPMC9322406
OpenAlexW4229005222

What OpenQuestion 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 OpenQuestion graph.