Evidence map›Paper›PMID 27604546›Full record

ArticleScientific reports2016

Biosynthesis and Regulation of Wheat Amylose and Amylopectin from Proteomic and Phosphoproteomic Characterization of Granule-binding Proteins.

Guan-Xing Chen, Jian-Wen Zhou, Yan-Lin Liu, Xiao-Bing Lu, Cai-Xia Han, Wen-Ying Zhang, Yan-Hao Xu, Yue-Ming Yan

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.5field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 66 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 1 country.

Guan-Xing ChenCollege of Life Science, Capital Normal University, 100048 Beijing, China.
Jian-Wen ZhouCollege of Life Science, Capital Normal University, 100048 Beijing, China.
Yan-Lin LiuCollege of Life Science, Capital Normal University, 100048 Beijing, China.
Xiao-Bing LuCollege of Life Science, Capital Normal University, 100048 Beijing, China.
Cai-Xia HanCollege of Life Science, Capital Normal University, 100048 Beijing, China.
Wen-Ying ZhangHubei Collaborative Innovation Center for Grain Industry, Yangtze University, 434025 Jingzhou, China.
Yan-Hao XuHubei Collaborative Innovation Center for Grain Industry, Yangtze University, 434025 Jingzhou, China.
Yue-Ming YanCollege of Life Science, Capital Normal University, 100048 Beijing, China.
Capital Normal University · CNYangtze University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Waxy starch has an important influence on the qualities of breads. Generally, grain weight and yield in waxy wheat (Triticum aestivum L.) are significantly lower than in bread wheat. In this study, we performed the first proteomic and phosphoproteomic analyses of starch granule-binding proteins by comparing the waxy wheat cultivar Shannong 119 and the bread wheat cultivar Nongda 5181. These results indicate that reduced amylose content does not affect amylopectin synthesis, but it causes significant reduction of total starch biosynthesis, grain size, weight and grain yield. Two-dimensional differential in-gel electrophoresis identified 40 differentially expressed protein (DEP) spots in waxy and non-waxy wheats, which belonged mainly to starch synthase (SS) I, SS IIa and granule-bound SS I. Most DEPs involved in amylopectin synthesis showed a similar expression pattern during grain development, suggesting relatively independent amylose and amylopectin synthesis pathways. Phosphoproteome analysis of starch granule-binding proteins, using TiO2 microcolumns and LC-MS/MS, showed that the total number of phosphoproteins and their phosphorylation levels in ND5181 were significantly higher than in SN119, but proteins controlling amylopectin synthesis had similar phosphorylation levels. Our results revealed the lack of amylose did not affect the expression and phosphorylation of the starch granule-binding proteins involved in amylopectin biosynthesis.

Indexed as

Amino Acid SequenceAmylopectinAmyloseEdible GrainGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGenes, PlantMetabolic Networks and PathwaysModels, MolecularPhosphorylationPlant ProteinsProteomicsSpecies SpecificityStarchStarch SynthaseAmylopectinAmylosegranule-bound starch synthase IPlant ProteinsStarchStarch Synthasestarch synthase II

Identifiers

PMID27604546
PMCPMC5015113
OpenAlexW2511999177

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LicenceCC BY
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Registered trials

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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.