Evidence map›Paper›PMID 29067028›Full record

ReviewFrontiers in plant science2017

Sumoylation, Phosphorylation, and Acetylation Fine-Tune the Turnover of Plant Immunity Components Mediated by Ubiquitination.

Zhouqing He, Tingting Huang, Kevin Ao, Xiaofang Yan, Yan Huang

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in plant science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Solo or in Concert: SUMOylation in Pathogenic Fungi.The plant pathology journal · 2025
    Review
  3. Review
  4. A DEK domain-containing protein GhDEK2D mediatedPlant signaling & behavior · 2022
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. SUMOylation-Mediated Response to Mitochondrial Stress.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Review
  15. Review
  16. Battlefield Cytoskeleton: Turning the Tide on Plant Immunity.Molecular plant-microbe interactions : MPMI · 2019
    Review
  17. Review
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

5 authors at 2 institutions in 2 countries.

Zhouqing HeCollege of Life Sciences, Sichuan Agricultural University, Ya'an, China.
Tingting HuangCollege of Life Sciences, Sichuan Agricultural University, Ya'an, China.
Kevin AoMichael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada.
Xiaofang YanCollege of Life Sciences, Sichuan Agricultural University, Ya'an, China.
Yan HuangCollege of Life Sciences, Sichuan Agricultural University, Ya'an, China.
Sichuan Agricultural University · CNUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination-mediated protein degradation plays a crucial role in the turnover of immune proteins through rapid alteration of protein levels. Specifically, the over-accumulation of immune proteins and consequent activation of immune responses in uninfected cells is prevented through degradation. Protein post-translational modifications can influence and affect ubiquitination. There is accumulating evidence that suggests sumoylation, phosphorylation, and acetylation differentially affect the stability of immune-related proteins, so that control over the accumulation or degradation of proteins is fine-tuned. In this paper, we review the function and mechanism of sumoylation, phosphorylation, acetylation, and ubiquitination in plant disease resistance responses, focusing on how ubiquitination reacts with sumoylation, phosphorylation, and acetylation to regulate plant disease resistance signaling pathways. Future research directions are suggested in order to provide ideas for signaling pathway studies, and to advance the implementation of disease resistance proteins in economically important crops.

Indexed as

acetylationelongating enzyme E4phosphorylationplant immunitysumoylationubiquitinubiquitination

Identifiers

PMID29067028
PMCPMC5641357
OpenAlexW2761644553

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.