Evidence map›Paper›PMID 29371398›Full record

ReviewThe Journal of biological chemistry2018

A molecular perspective of mammalian autophagosome biogenesis.

Thomas J Mercer, Andrea Gubas, Sharon A Tooze

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 158 papers.

0numbers the graph read from it
0cells of the map it votes in
158citing 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

158 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. ER membrane receptors engage core autophagy machinery to initiate ER-phagy.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. Analysis of Migration and Adaptive Evolution in Tibetan Sheep Populations.Animals : an open access journal from MDPI · 2026
    Article
  10. Review
  11. Review
  12. Article
  13. The Roles of Autophagy in Oxidative Stress.Archives of Razi Institute · 2025
    Review
  14. Article
  15. The human autophagy-initiating complexes ULK1C and PI3KC3-C1.The Journal of biological chemistry · 2025
    Review
  16. Review
  17. Review
  18. Review
  19. Review
  20. Review

98 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

3 authors.

Thomas J MercerFrom the Molecular Cell Biology of Autophagy Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, United Kingdom.
Andrea GubasFrom the Molecular Cell Biology of Autophagy Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, United Kingdom.
Sharon A ToozeFrom the Molecular Cell Biology of Autophagy Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, United Kingdom sharon.tooze@crick.ac.uk.ORCID 0000-0002-2182-3116

Funding

Cancer Research UK 15153Cancer Research UK FC001187Medical Research Council FC001187Wellcome TrustWellcome Trust FC001187
6 · The paper itself

Abstract

Autophagy is a highly conserved process and is essential for the maintenance of cellular homeostasis. Autophagy occurs at a basal level in all cells, but it can be up-regulated during stress, starvation, or infection. Misregulation of autophagy has been linked to various disorders, including cancer, neurodegeneration, and immune diseases. Here, we discuss the essential proteins acting in the formation of an autophagosome, with a focus on the ULK and VPS34 kinase complexes, phosphatidylinositol 3-phosphate effector proteins, and the transmembrane autophagy-related protein ATG9. The function and regulation of these and other autophagy-related proteins acting during formation will be addressed, in particular during amino acid starvation.

Indexed as

AutophagyAnimalsAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsClass III Phosphatidylinositol 3-KinasesHumansImmune System DiseasesInfectionsNeoplasm ProteinsNeoplasmsNeurodegenerative DiseasesStarvationAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsClass III Phosphatidylinositol 3-KinasesNeoplasm ProteinsATG9ATG proteinsautophagyintracellular traffickingphosphatidylinositide 3-kinase (PI 3-kinase)post-translational modificationsignalingULK1VPS34WIPI2

Identifiers

PMID29371398
PMCPMC5900756

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.