Evidence map›Paper›PMID 19136719›Full record

ArticleMolecular & cellular proteomics : MCP2009

Diversity of serine hydrolase activities of unchallenged and botrytis-infected Arabidopsis thaliana.

Farnusch Kaschani, Christian Gu, Sherry Niessen, Heather Hoover, Benjamin F Cravatt, Renier A L van der Hoorn

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
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

45 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
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  6. The root pathogenFrontiers in plant science · 2023
    Article
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  13. Review
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  15. Article
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  18. Protease Activities Triggered byMolecular & cellular proteomics : MCP · 2018
    Article
  19. Article
  20. 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

6 authors at 3 institutions in 2 countries.

Farnusch KaschaniPlant Chemetics laboratory, Max Planck Institute for Plant Breeding Research, Carl-von-Linné Weg 10, 50829 Cologne, Germany.
Christian Gu
Sherry Niessen
Heather Hoover
Benjamin F Cravatt
Renier A L van der Hoorn
Scripps Research Institute · USMax Planck Institute for Plant Breeding Research · DEMax Planck Society · DE

Funding

Chemical Approaches for Activity-Based ProteomicsR37CA087660 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F · 2009 to 2018
$3.1M
NCI NIH HHS R37 CA087660
6 · The paper itself

Abstract

Activity-based protein profiling is a powerful method to display enzyme activities in proteomes and provides crucial information on enzyme activity rather than protein or transcript abundance. We applied activity-based protein profiling using fluorophosphonate-based probes to display the activities of Ser hydrolases in the model plant Arabidopsis thaliana. Multidimensional protein identification technology and in-gel analysis of fluorophosphonate-labeled leaf extracts revealed over 50 Ser hydrolases, including dozens of proteases, esterases, and lipases, representing over 10 different enzyme families. Except for some well characterized Ser hydrolases like subtilases TPP2 and ARA12, prolyl oligopeptidase acylamino acid-releasing enzyme, serine carboxypeptidase-like SNG1 and BRS1, carboxylesterase-like CXE12, methylesterases MES2 and MES3, and S-formylglutathione hydrolase, the majority of these serine hydrolases have not been described before. We studied transiently expressed SNG1 and investigated plants infected with the fungal pathogen Botrytis cinerea. Besides the down-regulation of several Arabidopsis Ser hydrolase activities during Botrytis infection, we detected the activities of Botrytis-derived cutinases and lipases, which are thought to contribute to pathogenicity.

Indexed as

AcyltransferasesAgrobacterium tumefaciensAmino Acid SequenceArabidopsisArabidopsis ProteinsBotrytisHost-Pathogen InteractionsMolecular Sequence DataNicotianaOrganophosphonatesPeptidesPlant LeavesSerine EndopeptidasesTissue ExtractsAcyltransferasesArabidopsis ProteinsOrganophosphonatesPeptidesSerine Endopeptidasessinapoylglucose malate sinapoyltransferaseTissue Extracts

Identifiers

PMID19136719
PMCPMC2689769
OpenAlexW2108744024

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.