Evidence map›Paper›PMID 32203894›Full record

ReviewCurrent opinion in cell biology2020

Autophagosomes are formed at a distinct cellular structure.

David M Hollenstein, Claudine Kraft

Open access · hybridAbstract readReview
In one paragraph

Review in Current opinion in cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
10.0field-weighted citation impact, top 1% 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

76 citing papers in PubMed, 113 citations in OpenAlex.

  1. Role of Autophagy in Goose Astrovirus-Induced Renal Injury in Goslings.Animals : an open access journal from MDPI · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Autophagy: A Double-Edged Sword in the Aging ofInternational journal of molecular sciences · 2026
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Rethinking the Yeast Endomembrane System.Sub-cellular biochemistry · 2026
    Review
  12. The autophagy-specific exocyst subcomplex contributes to phagophore assembly site integrity by promoting phagophore expansion.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

16 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 2 countries.

David M HollensteinDepartment of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria.
Claudine KraftInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104 Freiburg, Germany; CIBSS-Centre for Integrative Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany. Electronic address: kraft@biochemie.uni-freiburg.de.
University of Freiburg · DEUniversity of Vienna · AT

Funding

Austrian Science Fund FWF W 1261HSRD VA HIR 10-001
6 · The paper itself

Abstract

Autophagy is characterized by the formation of double-membrane vesicles called autophagosomes, which deliver bulk cytoplasmic material to the lytic compartment of the cell for degradation. Autophagosome formation is initiated by assembly and recruitment of the core autophagy machinery to distinct cellular sites, referred to as phagophore assembly sites (PAS) in yeast or autophagosome formation sites in other organisms. A large number of autophagy proteins involved in the formation of autophagosomes has been identified; however, how the individual components of the PAS are assembled and how they function to generate autophagosomes remains a fundamental question. Here, we highlight recent studies that provide molecular insights into PAS organization and the role of the endoplasmic reticulum and the vacuole in autophagosome formation.

Indexed as

AutophagosomesAutophagyCellsModels, BiologicalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiae ProteinsATG1ATG12ATG13ATG16ATG17ATG18ATG2ATG29ATG31ATG5AutophagosomeAutophagosome formation siteAutophagyERIsolation membraneLipid transferLiquid dropletOrganelle contact sitePASPhagophorePhagophore assembly sitePhase separationPre-autophagosomal structureTetherVAC8Vacuole

Identifiers

PMID32203894
PMCPMC7588827
OpenAlexW3010716147

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.