Evidence map›Paper›PMID 22074553›Full record

ArticleBMC plant biology2011

Identification and analysis of phosphorylation status of proteins in dormant terminal buds of poplar.

Chang-Cai Liu, Chang-Fu Liu, Hong-Xia Wang, Zhi-Ying Shen, Chuan-Ping Yang, Zhi-Gang Wei

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

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  3. Phosphorylation is an on/off switch for 5-hydroxyconiferaldehyde O-methyltransferase activity in poplar monolignol biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 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

6 authors at 3 institutions in 1 country.

Chang-Cai LiuState Key Laboratory of Forest Genetics and Tree Breeding (Northeast Forestry University), 26 Hexing Road, Harbin 150040, China.
Chang-Fu Liu
Hong-Xia Wang
Zhi-Ying Shen
Chuan-Ping Yang
Zhi-Gang Wei
Northeast Forestry University · CNHarbin Medical University · CNInstitute of Basic Medical Sciences of the Chinese Academy of Medical Sciences

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAlthough there has been considerable progress made towards understanding the molecular mechanisms of bud dormancy, the roles of protein phosphorylation in the process of dormancy regulation in woody plants remain unclear.

resultsWe used mass spectrometry combined with TiO₂ phosphopeptide-enrichment strategies to investigate the phosphoproteome of dormant terminal buds (DTBs) in poplar (Populus simonii × P. nigra). There were 161 unique phosphorylated sites in 161 phosphopeptides from 151 proteins; 141 proteins have orthologs in Arabidopsis, and 10 proteins are unique to poplar. Only 34 sites in proteins in poplar did not match well with the equivalent phosphorylation sites of their orthologs in Arabidopsis, indicating that regulatory mechanisms are well conserved between poplar and Arabidopsis. Further functional classifications showed that most of these phosphoproteins were involved in binding and catalytic activity. Extraction of the phosphorylation motif using Motif-X indicated that proline-directed kinases are a major kinase group involved in protein phosphorylation in dormant poplar tissues.

conclusionsThis study provides evidence about the significance of protein phosphorylation during dormancy, and will be useful for similar studies on other woody plants.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsConserved SequenceMolecular Sequence DataPhosphorylationPlant ProteinsPlant ShootsPopulusProtein KinasesProteomeSignal TransductionArabidopsis ProteinsPlant ProteinsProtein KinasesProteome

Identifiers

PMID22074553
PMCPMC3234192
OpenAlexW1997318763

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.