Evidence map›Paper›PMID 38864414›Full record

ReviewPlant biotechnology journal2024

Deciphering the mechanism of E3 ubiquitin ligases in plant responses to abiotic and biotic stresses and perspectives on PROTACs for crop resistance.

Yingying Su, Guillaume Legrand Ngolong Ngea, Kaili Wang, Yuchun Lu, Esa Abiso Godana, Michael Ackah, Qiya Yang, Hongyin Zhang

Abstract readReview
In one paragraph

Review in Plant biotechnology journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. How to frustrate a plant pathogen.The Plant journal : for cell and molecular biology · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The Role of E3 Ubiquitin Ligase GeneInternational journal of molecular sciences · 2025
    Review
  15. Article
  16. Genome-Wide Identification and Expression Analysis of the Alfalfa (International journal of molecular sciences · 2024
    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

8 authors.

Yingying Su *School of Food and Biological Engineering, Jiangsu University, Zhenjiang, China.
Guillaume Legrand Ngolong Ngea *School of Food and Biological Engineering, Jiangsu University, Zhenjiang, China.
Kaili WangSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, China.
Yuchun LuSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, China.
Esa Abiso GodanaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, China.
Michael AckahSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, China.ORCID 0000-0001-9019-8986
Qiya YangSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, China.
Hongyin ZhangSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang, China.ORCID 0000-0001-6906-4713

Funding

China Postdoctoral Science Foundation 2023M741440National Natural Science Foundation of China 32072276National Natural Science Foundation of China 32102030National Natural Science Foundation of China 32150410368
6 · The paper itself

Abstract

With global climate change, it is essential to find strategies to make crops more resistant to different stresses and guarantee food security worldwide. E3 ubiquitin ligases are critical regulatory elements that are gaining importance due to their role in selecting proteins for degradation in the ubiquitin-proteasome proteolysis pathway. The role of E3 Ub ligases has been demonstrated in numerous cellular processes in plants responding to biotic and abiotic stresses. E3 Ub ligases are considered a class of proteins that are difficult to control by conventional inhibitors, as they lack a standard active site with pocket, and their biological activity is mainly due to protein-protein interactions with transient conformational changes. Proteolysis-targeted chimeras (PROTACs) are a new class of heterobifunctional molecules that have emerged in recent years as relevant alternatives for incurable human diseases like cancer because they can target recalcitrant proteins for destruction. PROTACs interact with the ubiquitin-proteasome system, principally the E3 Ub ligase in the cell, and facilitate proteasome turnover of the proteins of interest. PROTAC strategies harness the essential functions of E3 Ub ligases for proteasomal degradation of proteins involved in dysfunction. This review examines critical advances in E3 Ub ligase research in plant responses to biotic and abiotic stresses. It highlights how PROTACs can be applied to target proteins involved in plant stress response to mitigate pathogenic agents and environmental adversities.

Indexed as

Crops, AgriculturalProteolysisStress, PhysiologicalUbiquitin-Protein LigasesPlant ProteinsProteasome Endopeptidase ComplexProteolysis Targeting ChimeraPlant ProteinsProteasome Endopeptidase ComplexProteolysis Targeting ChimeraUbiquitin-Protein Ligasesabiotic stressbiotic stresscropsE3 Ub ligasePROTACsubiquitin‐proteasomal system

Identifiers

PMID38864414
PMCPMC11536463

What OpenQuestion holds

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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.