Evidence map›Paper›PMID 32051488›Full record

ArticleScientific reports2020

Proteome-wide identification and functional analysis of ubiquitinated proteins in peach leaves.

Yanbo Song, Xiaojing Shi, Yanli Zou, Juanru Guo, Nan Huo, Shuangjian Chen, Chengping Zhao, Hong Li, Guoliang Wu, Yong Peng

Erratum issuedOpen access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Yanbo SongHorticulture College, Shanxi Agricultural University, Taigu, Shanxi, 030801, PR China.
Xiaojing ShiLife Science College, Shanxi Agricultural University, Taigu, Shanxi, 030801, PR China.
Yanli ZouLife Science College, Shanxi Agricultural University, Taigu, Shanxi, 030801, PR China.
Juanru GuoLife Science College, Shanxi Agricultural University, Taigu, Shanxi, 030801, PR China.
Nan HuoLife Science College, Shanxi Agricultural University, Taigu, Shanxi, 030801, PR China.
Shuangjian ChenInstitute of Pomology, Shanxi Academy of Agricultural Sciences, Taigu, Shanxi, 030801, PR China.
Chengping ZhaoLife Science College, Shanxi Agricultural University, Taigu, Shanxi, 030801, PR China.
Hong LiLife Science College, Shanxi Agricultural University, Taigu, Shanxi, 030801, PR China.
Guoliang WuHorticulture College, Shanxi Agricultural University, Taigu, Shanxi, 030801, PR China. walnut-wu@126.com.
Yong PengShanghai Applied Protein Technology Co., Ltd, Shanghai, 201100, PR China.
Shanxi Agricultural University · CNShanxi Academy of Agricultural Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination is a critical post-translational modification machinery that governs a wide range of cellular functions by regulating protein homeostasis. Identification of ubiquitinated proteins and lysine residues can help researchers better understand the physiological roles of ubiquitin modification in different biological systems. In this study, we report the first comprehensive analysis of the peach ubiquitome by liquid chromatography-tandem mass spectrometry-based diglycine remnant affinity proteomics. Our systematic profiling revealed a total of 544 ubiquitination sites on a total of 352 protein substrates. Protein annotation and functional analysis suggested that ubiquitination is involved in modulating a variety of essential cellular and physiological processes in peach, including but not limited to carbon metabolism, histone assembly, translation and vesicular trafficking. Our results could facilitate future studies on how ubiquitination regulates the agricultural traits of different peach cultivars and other crop species.

Indexed as

Amino Acid SequencePlant LeavesPlant ProteinsProteomicsPrunus persicaUbiquitinated ProteinsUbiquitinationPlant ProteinsUbiquitinated Proteins

Identifiers

PMID32051488
PMCPMC7015887
OpenAlexW3006444643

What OpenQuestion holds

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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.