Evidence map›Paper›PMID 28427325›Full record

ArticleBMC genomics2017

Global analysis of protein lysine succinylation profiles in common wheat.

Yumei Zhang, Guangyuan Wang, Limin Song, Ping Mu, Shu Wang, Wenxing Liang, Qi Lin

Open access · goldAbstract read
In one paragraph

Article in BMC genomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

36 citing papers in PubMed, 73 citations in OpenAlex.

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  5. Global Analysis of Lysine Lactylation of Germinated Seeds in Wheat.International journal of molecular sciences · 2023
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  12. Global Profiling of 2-hydroxyisobutyrylome in Common Wheat.Genomics, proteomics & bioinformatics · 2022
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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

7 authors at 2 institutions in 1 country.

Yumei ZhangCollege of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao, Shandong, 266109, China.
Guangyuan WangCollege of Life Sciences, Shandong Province Key Laboratory of Applied Mycology, Qingdao Agricultural University, Qingdao, 266109, China.
Limin SongCollege of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao, Shandong, 266109, China.
Ping MuCollege of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao, Shandong, 266109, China.
Shu WangCollege of Agronomy, Shenyang Agricultural University, Shenyang, Liaoning, 110866, China.
Wenxing LiangCollege of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao, Shandong, 266109, China. wliang1@qau.edu.cn.
Qi LinCollege of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao, Shandong, 266109, China. nxxlinqi@163.com.
Qingdao Agricultural University · CNShenyang Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundProtein lysine succinylation is an important post-translational modification and plays a critical regulatory role in almost every aspects of cell metabolism in both eukaryotes and prokaryotes. Common wheat is one of the major global cereal crops. However, to date, little is known about the functions of lysine succinylation in this plant. Here, we performed a global analysis of lysine succinylation in wheat and examined its overlap with lysine acetylation.

resultsIn total, 330 lysine succinylated modification sites were identified in 173 proteins. Bioinformatics analysis showed that the modified proteins are distributed in multiple subcellular compartments and are involved in a wide variety of biological processes such as photosynthesis and the Calvin-Benson cycle, suggesting an important role for lysine succinylation in these processes. Five putative succinylation motifs were identified. A protein interaction network analysis revealed that diverse interactions are modulated by protein succinylation. Moreover, 21 succinyl-lysine sites were found to be acetylated at the same position, and 33 proteins were modified by both acetylation and succinylation, suggesting an extensive overlap between succinylation and acetylation in common wheat. Comparative analysis indicated that lysine succinylation is conserved between common wheat and Brachypodium distachyon.

conclusionsThese results suggest that lysine succinylation is involved in diverse biological processes, especially in photosynthesis and carbon fixation. This systematic analysis represents the first global analysis of lysine succinylation in common wheat and provides an important resource for exploring the physiological role of lysine succinylation in this cereal crop and likely in all plants.

Indexed as

Protein Processing, Post-TranslationalProteomicsAcetylationCarbon CycleLysineMolecular Sequence AnnotationPhotosynthesisPlant ProteinsProtein Structure, SecondaryProtein TransportSuccinic AcidTriticumLysinePlant ProteinsSuccinic AcidLysine succinylationPhotosynthesisPost-translational modificationSuccinylomeTriticum aestivum L.

Identifiers

PMID28427325
PMCPMC5397794
OpenAlexW2605917783

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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.