Evidence map›Paper›PMID 31699981›Full record

ArticleNature communications2019

ESCRT-III-driven piecemeal micro-ER-phagy remodels the ER during recovery from ER stress.

Marisa Loi, Andrea Raimondi, Diego Morone, Maurizio Molinari

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed, 1 pooled it
7.3field-weighted citation impact, top 2% 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

100 citing papers in PubMed, 1 synthesis or guideline pooled it, 145 citations in OpenAlex.

  1. Guideline
  2. Emerging mechanisms of ATG8-independent non-canonical autophagy.Journal of physiology and biochemistry · 2026
    Review
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  20. Exploiting autophagy and related pathways: pioneering new horizons in cataract therapy.Apoptosis : an international journal on programmed cell death · 2025
    Review

40 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

4 authors at 3 institutions in 2 countries.

Marisa LoiFaculty of Biomedical Sciences, Institute for Research in Biomedicine, Università della Svizzera italiana (USI), Bellinzona, Switzerland.
Andrea RaimondiExperimental Imaging Center, San Raffaele Scientific Institute, 20132, Milan, Italy.
Diego MoroneFaculty of Biomedical Sciences, Institute for Research in Biomedicine, Università della Svizzera italiana (USI), Bellinzona, Switzerland.
Maurizio MolinariFaculty of Biomedical Sciences, Institute for Research in Biomedicine, Università della Svizzera italiana (USI), Bellinzona, Switzerland. maurizio.molinari@irb.usi.ch.ORCID http://orcid.org/0000-0002-7636-5829
École Polytechnique Fédérale de Lausanne · CHSan Raffaele University of Rome · ITUniversità della Svizzera italiana · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) produces about 40% of the nucleated cell's proteome. ER size and content in molecular chaperones increase upon physiologic and pathologic stresses on activation of unfolded protein responses (UPR). On stress resolution, the mammalian ER is remodeled to pre-stress, physiologic size and function on activation of the LC3-binding activity of the translocon component SEC62. This elicits recov-ER-phagy, i.e., the delivery of the excess ER generated during the phase of stress to endolysosomes (EL) for clearance. Here, ultrastructural and genetic analyses reveal that recov-ER-phagy entails the LC3 lipidation machinery and proceeds via piecemeal micro-ER-phagy, where RAB7/LAMP1-positive EL directly engulf excess ER in processes that rely on the Endosomal Sorting Complex Required for Transport (ESCRT)-III component CHMP4B and the accessory AAA

Indexed as

Endoplasmic Reticulum StressUnfolded Protein ResponseAnimalsATPases Associated with Diverse Cellular ActivitiesAutophagosomesAutophagyEndoplasmic ReticulumEndosomal Sorting Complexes Required for TransportEndosomesFibroblastsGene Knockout TechniquesHEK293 CellsHumansLysosomesMembrane Transport ProteinsMiceATPases Associated with Diverse Cellular ActivitiesCHMP4B protein, humanCHMP4B protein, mouseEndosomal Sorting Complexes Required for TransportMAP1LC3A protein, humanMembrane Transport ProteinsMicrotubule-Associated ProteinsSEC62 protein, humanSNARE ProteinsVacuolar Proton-Translocating ATPasesVPS4A protein, humanVps4a protein, mouse

Identifiers

PMID31699981
PMCPMC6838186
OpenAlexW2986888980

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.