Evidence map›Paper›PMID 32277540›Full record

ArticleProtein science : a publication of the Protein Society2020

Atg3 promotes Atg8 lipidation via altering lipid diffusion and rearrangement.

Shen Wang, Yun Li, Cong Ma

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Ubiquitin-like Proteins ofBiomolecules · 2023
    Review
  7. Atg8-PE protein-basedAutophagy · 2022
    Review
  8. Article
  9. Article
  10. Review
  11. Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy.Biochimica et biophysica acta. Molecular cell research · 2021
    Review
  12. Binding Features and Functions of ATG3.Frontiers in cell and developmental biology · 2021
    Review
  13. Review
  14. Atg3 promotes Atg8 lipidation via altering lipid diffusion and rearrangement.Protein science : a publication of the Protein Society · 2020
    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

3 authors at 2 institutions in 1 country.

Shen WangKey Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.ORCID 0000-0002-5013-1039
Yun LiSchool of Biological and Food Processing Engineering, Huanghuai University, Zhumadian, China.
Cong MaKey Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.
Huazhong University of Science and Technology · CNHuanghuai University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Atg3-catalyzed transferring of Atg8 to phosphatidylethanolamine (PE) in the phagophore membrane is essential for autophagy. Previous studies have demonstrated that this process requires Atg3 to interact with the phagophore membrane via its N-terminal amphipathic helix. In this study, by using combined biochemical and biophysical approaches, our data showed that in addition to binding to the membranes, Atg3 attenuates lipid diffusion and enriches lipid molecules with smaller headgroup. Our data suggest that Atg3 promotes Atg8 lipidation via altering lipid diffusion and rearrangement.

Indexed as

DiffusionAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsLipidsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesATG3 protein, S cerevisiaeATG8 protein, S cerevisiaeAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsLipidsSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating Enzymesamphipathic helixAtg3Atg8autophagylipid diffusion

Identifiers

PMID32277540
PMCPMC7255502
OpenAlexW3016034695

What OpenQuestion holds

Textmetadata
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.