Evidence map›Paper›PMID 42008670›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

The temperature dependence of amyloid

Max Lindberg, Jing Hu, Dev Thacker, Emma Sparr, Sara Linse

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 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

5 authors.

Max LindbergDivision of Biochemistry and Structural Biology, Department of Chemistry, Lund University, Lund 221 00, Sweden.ORCID 0009-0008-1579-4970
Jing HuDivision of Physical Chemistry, Department of Chemistry, Lund University, Lund 221 00, Sweden.
Dev ThackerDivision of Biochemistry and Structural Biology, Department of Chemistry, Lund University, Lund 221 00, Sweden.ORCID 0000-0001-6171-9703
Emma SparrDivision of Physical Chemistry, Department of Chemistry, Lund University, Lund 221 00, Sweden.ORCID 0000-0001-8343-9657
Sara LinseDivision of Biochemistry and Structural Biology, Department of Chemistry, Lund University, Lund 221 00, Sweden.ORCID 0000-0001-9629-7109

Funding

EC | European Research Council (ERC) AdG 101097824Knut och Alice Wallenbergs Stiftelse (kawforskning) 2022-0059Vetenskapsrådet (VR) 2015-00143Vetenskapsrådet (VR) 2019-02397
6 · The paper itself

Abstract

The aggregation of amyloid proteins into fibrillar and oligomeric aggregates is linked to a number of neurodegenerative diseases. While the disease onset remains elusive in many cases, an understanding of the driving forces for the aggregation may help finding possible causes. While effects on amyloid formation kinetics are more commonly studied, gaining insights into these driving forces require a thermodynamic approach with equilibrium measurements. Here we investigate the temperature dependence of the solubility of the amyloid beta peptide, A

Indexed as

AmyloidAmyloid beta-PeptidesPeptide FragmentsCircular DichroismHumansHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsKineticsSolubilityTemperatureThermodynamicsAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-42)Peptide FragmentsAlzheimer’s diseaseAβself-assemblythermodynamicsβ-amyloid

Identifiers

PMID42008670
PMCPMC13123816

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.