Evidence map›Paper›PMID 28377462›Full record

ArticleThe EMBO journal2017

An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.

Daniel Mateju, Titus M Franzmann, Avinash Patel, Andrii Kopach, Edgar E Boczek, Shovamayee Maharana, Hyun O Lee, Serena Carra, Anthony A Hyman, Simon Alberti

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 289 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
289citing papers in PubMed, 3 pooled it
18.7field-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

289 citing papers in PubMed, 3 syntheses or guidelines pooled it, 474 citations in OpenAlex.

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  15. amyloid-predict and LLPS-predict: Predicting phase separation propensities in the intrinsically disordered proteome.Proceedings of the National Academy of Sciences of the United States of America · 2026
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229 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 2 countries.

Daniel MatejuMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Titus M FranzmannMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Avinash PatelMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Andrii KopachMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Edgar E BoczekMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Shovamayee MaharanaMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Hyun O LeeMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Serena CarraDepartment of Biomedical, Metabolic and Neural Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Anthony A HymanMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Simon AlbertiMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany alberti@mpi-cbg.de.ORCID 0000-0003-4017-6505
Max Planck Institute of Molecular Cell Biology and Genetics · DEUniversity of Modena and Reggio Emilia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stress granules (SG) are membrane-less compartments involved in regulating mRNAs during stress. Aberrant forms of SGs have been implicated in age-related diseases, such as amyotrophic lateral sclerosis (ALS), but the molecular events triggering their formation are still unknown. Here, we find that misfolded proteins, such as ALS-linked variants of SOD1, specifically accumulate and aggregate within SGs in human cells. This decreases the dynamics of SGs, changes SG composition, and triggers an aberrant liquid-to-solid transition of

Indexed as

Cytoplasmic GranulesEpithelial CellsHeLa CellsHumansMolecular ChaperonesSuperoxide Dismutase-1Molecular ChaperonesSOD1 protein, humanSuperoxide Dismutase-1protein aggregationprotein misfoldingproteostasisSOD1stress granules

Identifiers

PMID28377462
PMCPMC5470046
OpenAlexW2604947514

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.