Evidence map›Paper›PMID 22838494›Full record

ArticleBMC research notes2012

Seed storage proteins of the globulin family are cleaved post-translationally in wheat embryos.

Adam G Koziol, Evelin Loit, Melissa McNulty, Amanda J MacFarlane, Fraser W Scott, Illimar Altosaar

Open access · goldAbstract read
In one paragraph

Article in BMC research notes, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-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

3 citing papers in PubMed, 13 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

6 authors at 4 institutions in 3 countries.

Adam G KoziolDepartment of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Canada.
Evelin Loit
Melissa McNulty
Amanda J MacFarlane
Fraser W Scott
Illimar Altosaar
University of Ottawa · CAEstonian University of Life Sciences · EEOttawa Hospital · CAOttawa Hospital Research Institute

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

backgroundThe 7S globulins are plant seed storage proteins that have been associated with the development of a number of human diseases, including peanut allergy. Immune reactivity to the wheat seed storage protein globulin-3 (Glo-3) has been associated with the development of the autoimmune disease type 1 diabetes in diabetes-prone rats and mice, as well as in a subset of human patients.

findingsThe present study characterized native wheat Glo-3 in salt-soluble wheat seed protein extracts. Glo-3-like peptides were observed primarily in the wheat embryo. Glo-3-like proteins varied significantly in their molecular masses and isoelectric points, as determined by two dimensional electrophoresis and immunoblotting with anti-Glo-3A antibodies. Five major polypeptide spots were identified by mass spectrometry and N-terminal sequencing as belonging to the Glo-3 family.

conclusionsThese results in combination with our previous findings have allowed for the development of a hypothetical model of the post-translational events contributing to the wheat 7S globulin profile in mature wheat kernels.

Indexed as

Protein Processing, Post-TranslationalBlotting, WesternElectrophoresis, Gel, Two-DimensionalEndospermGlobulinsIsoelectric PointModels, BiologicalMolecular WeightPlant ProteinsSequence Analysis, ProteinTandem Mass SpectrometryTriticumGlobulinsPlant Proteinsstorage protein, Triticum aestivum

Identifiers

PMID22838494
PMCPMC3434096
OpenAlexW2076402162

What OpenQuestion holds

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LicenceCC BY
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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.