Evidence map›Paper›PMID 27515067›Full record

ArticleScientific reports2016

First Comprehensive Proteome Analyses of Lysine Acetylation and Succinylation in Seedling Leaves of Brachypodium distachyon L.

Shoumin Zhen, Xiong Deng, Jian Wang, Gengrui Zhu, Hui Cao, Linlin Yuan, Yueming 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 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

37 citing papers in PubMed, 97 citations in OpenAlex.

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  14. Cataloging Posttranslational Modifications in Plant Histones.Advances in experimental medicine and biology · 2021
    Article
  15. Article
  16. Article
  17. Secretome-Wide Analysis of Lysine Acetylation inFrontiers in microbiology · 2020
    Article
  18. Article
  19. Article
  20. Article
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

7 authors at 1 institution in 1 country.

Shoumin ZhenCollege of Life Science, Capital Normal University, Beijing, 100048, China.
Xiong DengCollege of Life Science, Capital Normal University, Beijing, 100048, China.
Jian WangCollege of Life Science, Capital Normal University, Beijing, 100048, China.
Gengrui ZhuCollege of Life Science, Capital Normal University, Beijing, 100048, China.
Hui CaoCollege of Life Science, Capital Normal University, Beijing, 100048, China.
Linlin YuanCollege of Life Science, Capital Normal University, Beijing, 100048, China.
Yueming YanCollege of Life Science, Capital Normal University, Beijing, 100048, China.
Capital Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein acetylation and succinylation are the most crucial protein post-translational modifications (PTMs) involved in the regulation of plant growth and development. In this study, we present the first lysine-acetylation and lysine-succinylation proteome analysis of seedling leaves in Brachypodium distachyon L (Bd). Using high accuracy nano LC-MS/MS combined with affinity purification, we identified a total of 636 lysine-acetylated sites in 353 proteins and 605 lysine-succinylated sites in 262 proteins. These proteins participated in many biology processes, with various molecular functions. In particular, 119 proteins and 115 sites were found to be both acetylated and succinylated, simultaneously. Among the 353 acetylated proteins, 148 had acetylation orthologs in Oryza sativa L., Arabidopsis thaliana, Synechocystis sp. PCC 6803, and Glycine max L. Among the 262 succinylated proteins, 170 of them were found to have homologous proteins in Oryza sativa L., Escherichia coli, Sacchayromyces cerevisiae, or Homo sapiens. Motif-X analysis of the acetylated and succinylated sites identified two new acetylated motifs (K---K and K-I-K) and twelve significantly enriched succinylated motifs for the first time, which could serve as possible binding loci for future studies in plants. Our comprehensive dataset provides a promising starting point for further functional analysis of acetylation and succinylation in Bd and other plant species.

Indexed as

AcetylationBrachypodiumLysinePlant LeavesPlant ProteinsProtein Processing, Post-TranslationalSeedlingsSuccinic AcidLysinePlant ProteinsSuccinic Acid

Identifiers

PMID27515067
PMCPMC4981852
OpenAlexW2508262787

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.