Evidence map›Paper›PMID 24040092›Full record

ArticlePloS one2013

Proteolytic pathways induced by herbicides that inhibit amino acid biosynthesis.

Amaia Zulet, Miriam Gil-Monreal, Joji Grace Villamor, Ana Zabalza, Renier A L van der Hoorn, Mercedes Royuela

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
7.9field-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

21 citing papers in PubMed, 68 citations in OpenAlex.

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  7. Fluctuation in amino acids content inSaudi journal of biological sciences · 2021
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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

6 authors at 2 institutions in 2 countries.

Amaia ZuletDepartamento de Ciencias del Medio Natural, Universidad Pública de Navarra, Pamplona, Spain.
Miriam Gil-Monreal
Joji Grace Villamor
Ana Zabalza
Renier A L van der Hoorn
Mercedes Royuela
Universidad Publica de Navarra · ESMax Planck Institute for Plant Breeding Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe herbicides glyphosate (Gly) and imazamox (Imx) inhibit the biosynthesis of aromatic and branched-chain amino acids, respectively. Although these herbicides inhibit different pathways, they have been reported to show several common physiological effects in their modes of action, such as increasing free amino acid contents and decreasing soluble protein contents. To investigate proteolytic activities upon treatment with Gly and Imx, pea plants grown in hydroponic culture were treated with Imx or Gly, and the proteolytic profile of the roots was evaluated through fluorogenic kinetic assays and activity-based protein profiling.

resultsSeveral common changes in proteolytic activity were detected following Gly and Imx treatment. Both herbicides induced the ubiquitin-26 S proteasome system and papain-like cysteine proteases. In contrast, the activities of vacuolar processing enzymes, cysteine proteases and metacaspase 9 were reduced following treatment with both herbicides. Moreover, the activities of several putative serine protease were similarly increased or decreased following treatment with both herbicides. In contrast, an increase in YVADase activity was observed under Imx treatment versus a decrease under Gly treatment.

conclusionThese results suggest that several proteolytic pathways are responsible for protein degradation upon herbicide treatment, although the specific role of each proteolytic activity remains to be determined.

Indexed as

Amino AcidsBlotting, WesternCysteine Proteinase InhibitorsGlycineGlyphosateHerbicidesHydroponicsImidazolesLeucineLeupeptinsOligopeptidesPisum sativumPlant ProteinsPlant RootsProteasome Endopeptidase ComplexProteolysisAmino Acidsbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCysteine Proteinase InhibitorsE 64epoxomicinGlycineGlyphosateHerbicidesimazamoxImidazolesLeucineLeupeptinsOligopeptidesPlant ProteinsProteasome Endopeptidase Complex

Identifiers

PMID24040092
PMCPMC3765261
OpenAlexW2091894396

What OpenQuestion holds

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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.