Evidence map›Paper›PMID 21718517›Full record

ArticleProteome science2011

Phosphoproteins regulated by heat stress in rice leaves.

Xinhai Chen, Wenfeng Zhang, Baoqian Zhang, Jiechao Zhou, Yongfei Wang, Qiaobin Yang, Yuqin Ke, Huaqin He

Open access · goldAbstract read
In one paragraph

Article in Proteome science, 2011. 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
1.9field-weighted citation impact, top 15% 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, 60 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.

Xinhai Chen *Key Laboratory of Ministry of Education for Genetic, Breeding and Multiple Utilization of Crops, Fuzhou 350002, China.
Wenfeng Zhang *Key Laboratory of Ministry of Education for Genetic, Breeding and Multiple Utilization of Crops, Fuzhou 350002, China.
Baoqian Zhang *College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Jiechao ZhouCollege of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Yongfei WangCollege of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Qiaobin YangCollege of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Yuqin KeCollege of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Huaqin HeKey Laboratory of Ministry of Education for Genetic, Breeding and Multiple Utilization of Crops, Fuzhou 350002, China.
Fujian Agriculture and Forestry University · CNMinistry of Education of the People's Republic of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHigh temperature is a critical abiotic stress that reduces crop yield and quality. Rice (Oryza sativa L.) plants remodel their proteomes in response to high temperature stress. Moreover, phosphorylation is the most common form of protein post-translational modification (PTM). However, the differential expression of phosphoproteins induced by heat in rice remains unexplored.

methodsPhosphoprotein in the leaves of rice under heat stress were displayed using two-dimensional electrophoresis (2-DE) and Pro-Q Diamond dye. Differentially expressed phosphoproteins were identified by MALDI-TOF-TOF-MS/MS and confirmed by Western blotting.

resultsTen heat-phosphoproteins were identified from twelve protein spots, including ribulose bisphos-phate carboxylase large chain, 2-Cys peroxiredoxin BAS1, putative mRNA binding protein, Os01g0791600 protein, OSJNBa0076N16.12 protein, putative H(+)-transporting ATP synthase, ATP synthase subunit beta and three putative uncharacterized proteins. The identification of ATP synthase subunit beta was further validated by Western-blotting. Four phosphorylation site predictors were also used to predict the phosphorylation sites and the specific kinases for these 10 phosphoproteins.

conclusionHeat stress induced the dephosphorylation of RuBisCo and the phosphorylation of ATP-β, which decreased the activities of RuBisCo and ATP synthase. The observed dephosphorylation of the mRNA binding protein and 2-Cys peroxiredoxin may be involved in the transduction of heat-stress signaling, but the functional importance of other phosphoproteins, such as H+-ATPase, remains unknown.

Identifiers

PMID21718517
PMCPMC3150237
OpenAlexW2091210050

What OpenQuestion holds

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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.