Evidence map›Paper›PMID 41648378›Full record

ArticlebioRxiv : the preprint server for biology2026

Biomolecular Condensates Dictate the Folding Landscape of Proteins.

Nathaniel Hess, Jerelle A Joseph

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 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

5 · Who and what money

Authors and funding

2 authors.

Nathaniel HessDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544, USA.ORCID 0000-0001-8971-332X
Jerelle A JosephDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544, USA.ORCID 0000-0003-4525-180X

Funding

Inside Condensates: Bridging molecular structure and condensate material properties through simulationR35GM155259 · NIGMS · PRINCETON UNIVERSITY · PI Jerelle Aurelia Joseph · 2024 to 2026
$1.2M
NIGMS NIH HHS R35 GM155259
6 · The paper itself

Abstract

Protein structure is exquisitely sensitive to the surrounding chemical environment, and many proteins encounter complex environments within cells. Importantly, numerous proteins organize into biomolecular condensates-dense macromolecular assemblies with distinct physicochemical properties. This raises a fundamental question: how does condensation reshape protein structure and dynamics? Here, we investigate how protein folding landscapes are altered inside condensates, using the protein

Identifiers

PMID41648378
PMCPMC12871253

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.