Evidence map›Paper›PMID 35806307›Full record

ReviewInternational journal of molecular sciences2022

Degradation Mechanism of Autophagy-Related Proteins and Research Progress.

Yanhui Zhou, Hakim Manghwar, Weiming Hu, Fen Liu

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

34 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Autophagy in Melanoma: Molecular Mechanisms and Therapeutic Perspectives.International journal of molecular sciences · 2026
    Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Plants (Basel, Switzerland) · 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

4 authors at 2 institutions in 1 country.

Yanhui ZhouLushan Botanical Garden, Chinese Academy of Sciences, Jiujiang 332900, China.
Hakim ManghwarLushan Botanical Garden, Chinese Academy of Sciences, Jiujiang 332900, China.ORCID 0000-0002-0281-1590
Weiming HuLushan Botanical Garden, Chinese Academy of Sciences, Jiujiang 332900, China.ORCID 0000-0002-0151-886X
Fen LiuLushan Botanical Garden, Chinese Academy of Sciences, Jiujiang 332900, China.
Nanchang University · CNLushan Botanical Garden · CN

Funding

National Natural Science Foundation of China 32100297
6 · The paper itself

Abstract

In all eukaryotes, autophagy is the main pathway for nutrient recycling, which encapsulates parts of the cytoplasm and organelles in double-membrane vesicles, and then fuses with lysosomes/vacuoles to degrade them. Autophagy is a highly dynamic and relatively complex process influenced by multiple factors. Under normal growth conditions, it is maintained at basal levels. However, when plants are subjected to biotic and abiotic stresses, such as pathogens, drought, waterlogging, nutrient deficiencies, etc., autophagy is activated to help cells to survive under stress conditions. At present, the regulation of autophagy is mainly reflected in hormones, second messengers, post-transcriptional regulation, and protein post-translational modification. In recent years, the degradation mechanism of autophagy-related proteins has attracted much attention. In this review, we have summarized how autophagy-related proteins are degraded in yeast, animals, and plants, which will help us to have a more comprehensive and systematic understanding of the regulation mechanisms of autophagy. Moreover, research progress on the degradation of autophagy-related proteins in plants has been discussed.

Indexed as

LysosomesVacuolesAnimalsAutophagyAutophagy-Related ProteinsPlantsSaccharomyces cerevisiaeAutophagy-Related Proteinsautophagyautophagy-related proteindegradationproteasomeubiquitin

Identifiers

PMID35806307
PMCPMC9266641
OpenAlexW4283763187

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.