Evidence map›Paper›PMID 41154852›Full record

ReviewBiology2025

Catalyzing Protein Folding by Chaperones.

Zijue Huang, Scott Horowitz

Abstract readReview
In one paragraph

Review in Biology, 2025. 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

2 authors.

Zijue HuangDepartment of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA.ORCID 0000-0002-4870-6083
Scott HorowitzDepartment of Chemistry and Biochemistry, University of Denver, Denver, CO 80208, USA.ORCID 0000-0002-1148-0105

Funding

Nucleic Acids Roles in Protein Folding and AggregationR35GM142442 · NIGMS · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI Scott Andrew Horowitz · 2021 to 2026
$2.4M
NIGMS NIH HHS R35 GM142442NIH HHS 5R35GM142442-25
6 · The paper itself

Abstract

Protein folding is a fundamental process essential for cellular growth and health, yet it is also susceptible to errors that can result in misfolding and disease. This literature review explores the current knowledge of the roles of different factors on protein folding in the cell. We examine the cellular proteostasis network, with a focus on the catalytic actions of prolyl isomerases and molecular chaperones (including RNA G-quadruplexes), which collaborate to guide newly synthesized polypeptides toward their native structures and prevent aggregation. By integrating structural and biochemical insights, this review highlights the current understanding and ongoing questions regarding how chaperones can improve folding times of proteins to physiological pertinent rates.

Indexed as

chaperoneisomeraseprotein foldingquadruplexRNA

Identifiers

PMID41154852
PMCPMC12562196

What OpenQuestion holds

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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.