Evidence map›Paper›PMID 42176846›Full record

ReviewCell stress & chaperones2026

Wiring of cellular proteostasis by J-domain proteins.

Matthias P Mayer

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Cell stress & chaperones, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

1 author.

Matthias P MayerCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany. Electronic address: m.mayer@zmbh.uni-heidelberg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Originally J-domain proteins (JDPs) were viewed as accessory co-chaperones of 70 kDa heat shock proteins (Hsp70s), the actual chaperones, stimulating ATPase activity of Hsp70s when a protein substrate is bound. This view apparently underestimates the role of JDPs, as most of the decisions within the Hsp70 network seems to be taken at the level of JDPs. The JDPs are the brain, so to speak, and the Hsp70s are the muscles of this chaperone network.

Indexed as

HSP70 Heat-Shock ProteinsMolecular ChaperonesProteostasisAnimalsHumansProtein DomainsProtein FoldingHSP70 Heat-Shock ProteinsMolecular ChaperonesAmyloid fibrilsChaperonesHsp70Neurodegenerative diseasesProtein folding

Identifiers

PMID42176846
PMCPMC13254874

What Socratic 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 Socratic graph.