Evidence map›Paper›PMID 35741004›Full record

ReviewCells2022

Characterization of Protein-Membrane Interactions in Yeast Autophagy.

Kelsie A Leary, Michael J Ragusa

Abstract readReview
In one paragraph

Review in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

2 authors.

Kelsie A LearyDepartment of Chemistry, Dartmouth College, Hanover, NH 03755, USA.ORCID 0000-0001-8026-7327
Michael J RagusaDepartment of Chemistry, Dartmouth College, Hanover, NH 03755, USA.ORCID 0000-0002-0231-0876

Funding

Dissecting the Molecular Mechanisms of Selective AutophagyR35GM128663 · NIGMS · DARTMOUTH COLLEGE · PI Michael Joseph Ragusa · 2018 to 2026
$3.5M
NIGMS NIH HHS R35 GM128663
6 · The paper itself

Abstract

Cells rely on autophagy to degrade cytosolic material and maintain homeostasis. During autophagy, content to be degraded is encapsulated in double membrane vesicles, termed autophagosomes, which fuse with the yeast vacuole for degradation. This conserved cellular process requires the dynamic rearrangement of membranes. As such, the process of autophagy requires many soluble proteins that bind to membranes to restructure, tether, or facilitate lipid transfer between membranes. Here, we review the methods that have been used to investigate membrane binding by the core autophagy machinery and additional accessory proteins involved in autophagy in yeast. We also review the key experiments demonstrating how each autophagy protein was shown to interact with membranes.

Indexed as

AutophagySaccharomyces cerevisiaeAutophagosomesProteinsVacuolesProteinsautophagymembrane binding proteinsyeast

Identifiers

PMID35741004
PMCPMC9221364

What OpenQuestion holds

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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.