Evidence map›Paper›PMID 20385545›Full record

ArticleJournal of experimental botany2010

Brachypodium distachyon grain: identification and subcellular localization of storage proteins.

C Larré, S Penninck, B Bouchet, V Lollier, O Tranquet, S Denery-Papini, F Guillon, H Rogniaux

Open access · bronzeAbstract read
In one paragraph

Article in Journal of experimental botany, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
12.4field-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

30 citing papers in PubMed, 55 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

8 authors at 2 institutions in 2 countries.

C LarréUR1268 Biopolymères Interactions Assemblages, INRA, F-44300 Nantes, France. larre@nantes.inra.fr
S Penninck
B Bouchet
V Lollier
O Tranquet
S Denery-Papini
F Guillon
H Rogniaux
Biopolymères Interactions Assemblages · FRInstitut National de la Recherche Agronomique · MA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Seed storage proteins are of great importance in nutrition and in industrial transformation because of their functional properties. Brachypodium distachyon has been proposed as a new model plant to study temperate cereals. The protein composition of Brachypodium grain was investigated by separating the proteins on the basis of their solubility combined with a proteomic approach. Salt-soluble proteins as well as salt-insoluble proteins separated by two-dimensional gel electrophoresis revealed 284 and 120 spots, respectively. Proteins from the major spots were sequenced by mass spectrometry and identified by searching against a Brachypodium putative protein database. Our analysis detected globulins and prolamins but no albumins. Globulins were represented mainly by the 11S type and their solubility properties corresponded to the glutelin found in rice. An in silico search for storage proteins returned more translated genes than expressed products identified by mass spectrometry, particularly in the case of prolamin type proteins, reflecting a strong expression of globulins at the expense of prolamins. Microscopic examination of endosperm cells revealed scarce small-size starch granules surrounded by protein bodies containing 11S globulins. The presence of protein bodies containing glutelins makes B. distachyon closer to rice or oat than to wheat endosperm.

Indexed as

Electrophoresis, Gel, Two-DimensionalGlobulinsMass SpectrometryMicroscopy, Electron, TransmissionPlant ProteinsPoaceaeProlaminsSeedsGlobulinsPlant ProteinsProlamins

Identifiers

PMID20385545
PMCPMC2852671
OpenAlexW2100765995

What OpenQuestion holds

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LicenceCC BY-NC
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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.