Evidence map›Paper›PMID 41942094›Full record

ArticleBiochemistry2026

Model Peptides Enable Comparisons of Substrate Binding Modes of Hsp70 Molecular Chaperones.

Karishma Bhasne, Lea Dörries, Akshitha Maqtedar, Sydney T Mager, Eugenia M Clerico, Lila M Gierasch

Erratum issuedAbstract readComparative Study
In one paragraph

Article in Biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. 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

5 · Who and what money

Authors and funding

6 authors.

Karishma BhasneDepartments of Biochemistry & Molecular Biology and Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.
Lea DörriesDepartments of Biochemistry & Molecular Biology and Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.ORCID 0009-0008-6249-7768
Akshitha MaqtedarDepartments of Biochemistry & Molecular Biology and Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.ORCID 0009-0004-3811-1475
Sydney T MagerDepartments of Biochemistry & Molecular Biology and Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.ORCID 0009-0004-1690-452X
Eugenia M ClericoDepartments of Biochemistry & Molecular Biology and Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.ORCID 0000-0002-4433-8842
Lila M GieraschDepartments of Biochemistry & Molecular Biology and Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.ORCID 0000-0002-5706-115X

Funding

Protein folding in the cell: Challenges and coping mechanisms Administrative Supplement for Equipment PurchaseR35GM118161 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GIERASCH, LILA M · 2016 to 2025
$5.5M
NIGMS NIH HHS R35 GM118161
6 · The paper itself

Abstract

Hsp70 molecular chaperones play a wide array of essential roles in the cell by exploiting their ability to bind incompletely folded client proteins. Our past study of the

Indexed as

Escherichia coli ProteinsHSP70 Heat-Shock ProteinsPeptidesAmino Acid SequenceBinding SitesEscherichia coliHSC70 Heat-Shock ProteinsHumansModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein BindingSubstrate SpecificitydnaK protein, E coliEscherichia coli ProteinsHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSPA1A protein, humanPeptides

Identifiers

PMID41942094
PMCPMC13104019

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.