Evidence map›Paper›PMID 20087596›Full record

ArticlePlant cell reports2010

Arabidopsis sensitivity to protein synthesis inhibitors depends on 26S proteasome activity.

Jasmina Kurepa, Consolée Karangwa, Liliana Sfichi Duke, Jan A Smalle

Abstract read
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In one paragraph

Article in Plant cell reports, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Jasmina KurepaPlant Physiology, Biochemistry, Molecular Biology Program, Department of Plant and Soil Sciences, College of Agriculture, University of Kentucky, 1401 University Drive, Lexington, KY 40546-0236, USA.
Consolée Karangwa
Liliana Sfichi Duke
Jan A Smalle
University of Kentucky · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 26S proteasome (26SP), the central protease of the ubiquitin-dependent proteolysis pathway, controls the regulated proteolysis of functional proteins and the removal of misfolded and damaged proteins. In Arabidopsis, cellular and stress response phenotypes of a number of mutants with partially impaired 26SP function have been reported. Here, we describe the responses of proteasome mutants to protein synthesis inhibitors. We show that the rpt2a-3, rpn10-1 and rpn12a-1 mutants are hypersensitive to the antibiotic hygromycin B, and tolerant to the translation inhibitor cycloheximide (CHX) and herbicide L-phosphinothricin (PPT). In addition to the novel mechanism for herbicide tolerance, our data suggests that the combination of hygromycin B, CHX and PPT growth-response assays could be used as a facile diagnostic tool to detect altered 26SP function in plant mutants and transgenic lines.

Indexed as

AminobutyratesArabidopsisCycloheximideGerminationHerbicidesHygromycin BMutationProteasome Endopeptidase ComplexProtein Synthesis InhibitorsAminobutyratesATP dependent 26S proteaseCycloheximideHerbicidesHygromycin BphosphinothricinProteasome Endopeptidase ComplexProtein Synthesis Inhibitors

Identifiers

PMID20087596
OpenAlexW2089554779

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.