Evidence map›Paper›PMID 30837482›Full record

ArticleScientific reports2019

Succinyl-proteome profiling of Pyricularia oryzae, a devastating phytopathogenic fungus that causes rice blast disease.

Jiaoyu Wang, Ling Li, Rongyao Chai, Zhen Zhang, Haiping Qiu, Xueqin Mao, Zhongna Hao, Yanli Wang, Guochang Sun

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

9 citing papers in PubMed, 20 citations in OpenAlex.

  1. Impact of Lysine Succinylation on the Biology of Fungi.Current issues in molecular biology · 2024
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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

9 authors at 1 institution in 1 country.

Jiaoyu WangState key laboratory breeding base for Zhejiang sustainable pest and disease control, Institute of plant protection and microbiology, Zhejiang academy of agricultural sciences, Hangzhou, 310021, China.
Ling LiState key laboratory breeding base for Zhejiang sustainable pest and disease control, Institute of plant protection and microbiology, Zhejiang academy of agricultural sciences, Hangzhou, 310021, China.
Rongyao ChaiState key laboratory breeding base for Zhejiang sustainable pest and disease control, Institute of plant protection and microbiology, Zhejiang academy of agricultural sciences, Hangzhou, 310021, China.
Zhen ZhangState key laboratory breeding base for Zhejiang sustainable pest and disease control, Institute of plant protection and microbiology, Zhejiang academy of agricultural sciences, Hangzhou, 310021, China.
Haiping QiuState key laboratory breeding base for Zhejiang sustainable pest and disease control, Institute of plant protection and microbiology, Zhejiang academy of agricultural sciences, Hangzhou, 310021, China.
Xueqin MaoState key laboratory breeding base for Zhejiang sustainable pest and disease control, Institute of plant protection and microbiology, Zhejiang academy of agricultural sciences, Hangzhou, 310021, China.
Zhongna HaoState key laboratory breeding base for Zhejiang sustainable pest and disease control, Institute of plant protection and microbiology, Zhejiang academy of agricultural sciences, Hangzhou, 310021, China.
Yanli WangState key laboratory breeding base for Zhejiang sustainable pest and disease control, Institute of plant protection and microbiology, Zhejiang academy of agricultural sciences, Hangzhou, 310021, China.
Guochang SunState key laboratory breeding base for Zhejiang sustainable pest and disease control, Institute of plant protection and microbiology, Zhejiang academy of agricultural sciences, Hangzhou, 310021, China. sungc01@sina.com.
ZheJiang Academy of Agricultural Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyricularia oryzae is the pathogen for rice blast disease, which is a devastating threat to rice production worldwide. Lysine succinylation, a newly identified post-translational modification, is associated with various cellular processes. Here, liquid chromatography tandem-mass spectrometry combined with a high-efficiency succinyl-lysine antibody was used to identify the succinylated peptides in P. oryzae. In total, 2109 lysine succinylation sites in 714 proteins were identified. Ten conserved succinylation sequence patterns were identified, among which, K*******K

Indexed as

Chromatography, High Pressure LiquidCitric Acid CycleFungal ProteinsLysineMagnaportheMetabolic Networks and PathwaysOryzaPeptidesPhylogenyPlant DiseasesProtein Processing, Post-TranslationalProteomeSuccinic AcidTandem Mass SpectrometryFungal ProteinsLysinePeptidesProteomeSuccinic Acid

Identifiers

PMID30837482
PMCPMC6401317
OpenAlexW2918212764

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.