Evidence map›Paper›PMID 35465159›Full record

ArticleComputational and structural biotechnology journal2022

Sensor dimer disruption as a new mode of action to block the IRE1-mediated unfolded protein response.

Kosala N Amarasinghe, Diana Pelizzari-Raymundo, Antonio Carlesso, Eric Chevet, Leif A Eriksson, Sayyed Jalil Mahdizadeh

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Computational and structural biotechnology journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

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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

6 authors at 3 institutions in 3 countries.

Kosala N AmarasingheDepartment of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Göteborg, Sweden.
Diana Pelizzari-RaymundoINSERM U1242, Université de Rennes, Rennes, France.
Antonio CarlessoDepartment of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Göteborg, Sweden.
Eric ChevetINSERM U1242, Université de Rennes, Rennes, France.
Leif A ErikssonDepartment of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Göteborg, Sweden.
Sayyed Jalil MahdizadehDepartment of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Göteborg, Sweden.
University of Gothenburg · SEInserm · FRUniversità della Svizzera italiana · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unfolded protein response (UPR) is activated to cope with an accumulation of improperly folded proteins in the Endoplasmic reticulum (ER). The Inositol requiring enzyme 1α (IRE1α) is the most evolutionary conserved transducer of the UPR. Activated IRE1 forms 'back-to-back'-dimers that enables the unconventional splicing of X-box Binding Protein 1 (XBP1) mRNA. The spliced XBP1 (

Indexed as

Dimer disruptorFDA approved drugsIRE1αMD simulationsPeptide dockingUPR

Identifiers

PMID35465159
PMCPMC9010685
OpenAlexW4220835537

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.