Evidence map›Paper›PMID 24747843›Full record

ArticlePloS one2014

Molecular characterization and expression profiling of the protein disulfide isomerase gene family in Brachypodium distachyon L.

Chong Zhu, Nana Luo, Miao He, Guanxing Chen, Jiantang Zhu, Guangjun Yin, Xiaohui Li, Yingkao Hu, Jiarui Li, Yueming Yan

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 41 citations in OpenAlex.

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  16. Nitrogen stress-induced alterations in the leaf proteome of two wheat varieties grown at different nitrogen levels.Physiology and molecular biology of plants : an international journal of functional plant biology · 2015
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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

10 authors at 2 institutions in 2 countries.

Chong ZhuCollege of Life Science, Capital Normal University, Beijing, China.
Nana LuoCollege of Life Science, Capital Normal University, Beijing, China.
Miao HeCollege of Life Science, Capital Normal University, Beijing, China.
Guanxing ChenCollege of Life Science, Capital Normal University, Beijing, China.
Jiantang ZhuCollege of Life Science, Capital Normal University, Beijing, China.
Guangjun YinCollege of Life Science, Capital Normal University, Beijing, China.
Xiaohui LiCollege of Life Science, Capital Normal University, Beijing, China.
Yingkao HuCollege of Life Science, Capital Normal University, Beijing, China.
Jiarui LiDepartment of Plant Pathology, Kansas State University, Manhattan, Kansas, United States of America.
Yueming YanCollege of Life Science, Capital Normal University, Beijing, China.
Capital Normal University · CNKansas State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein disulfide isomerases (PDI) are involved in catalyzing protein disulfide bonding and isomerization in the endoplasmic reticulum and functions as a chaperone to inhibit the aggregation of misfolded proteins. Brachypodium distachyon is a widely used model plant for temperate grass species such as wheat and barley. In this work, we report the first molecular characterization, phylogenies, and expression profiles of PDI and PDI-like (PDIL) genes in B. distachyon in different tissues under various abiotic stresses. Eleven PDI and PDIL genes in the B. distachyon genome by in silico identification were evenly distributed across all five chromosomes. The plant PDI family has three conserved motifs that are involved in catalyzing protein disulfide bonding and isomerization, but a different exon/intron structural organization showed a high degree of structural differentiation. Two pairs of genes (BdPDIL4-1 and BdPDIL4-2; BdPDIL7-1 and BdPDIL7-2) contained segmental duplications, indicating each pair originated from one progenitor. Promoter analysis showed that Brachypodium PDI family members contained important cis-acting regulatory elements involved in seed storage protein synthesis and diverse stress response. All Brachypodium PDI genes investigated were ubiquitously expressed in different organs, but differentiation in expression levels among different genes and organs was clear. BdPDIL1-1 and BdPDIL5-1 were expressed abundantly in developing grains, suggesting that they have important roles in synthesis and accumulation of seed storage proteins. Diverse treatments (drought, salt, ABA, and H2O2) induced up- and down-regulated expression of Brachypodium PDI genes in seedling leaves. Interestingly, BdPDIL1-1 displayed significantly up-regulated expression following all abiotic stress treatments, indicating that it could be involved in multiple stress responses. Our results provide new insights into the structural and functional characteristics of the plant PDI gene family.

Indexed as

Gene Expression ProfilingAmino Acid MotifsAmino Acid SequenceBrachypodiumEvolution, MolecularModels, MolecularMolecular Sequence DataOrgan SpecificityPhylogenyPromoter Regions, GeneticProtein Disulfide-IsomerasesSequence AlignmentStress, PhysiologicalProtein Disulfide-Isomerases

Identifiers

PMID24747843
PMCPMC3991636
OpenAlexW1995643716

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.