Evidence map›Paper›PMID 42863048›Full record

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

A water-pinning hot spot drives templated tau aggregation.

Chung-Ta Han, Karen Tsay, Samuel Lobo, Saeed Najafi, Kieran Monahan, Erica Hong, M Scott Shell, Joan-Emma Shea, Songi Han

Abstract read
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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

9 authors.

Chung-Ta HanDepartment of Chemistry, Northwestern University, Evanston, IL 60208-3113.ORCID 0009-0006-0924-3617
Karen TsayDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106-9510.
Samuel LoboDepartment of Chemical Engineering, University of California, Santa Barbara, CA 93106-5080.ORCID 0000-0002-1162-8798
Saeed NajafiDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106-9510.
Kieran MonahanDepartment of Chemistry, Northwestern University, Evanston, IL 60208-3113.
Erica HongDepartment of Chemistry, Northwestern University, Evanston, IL 60208-3113.ORCID 0009-0004-9227-7847
M Scott ShellDepartment of Chemical Engineering, University of California, Santa Barbara, CA 93106-5080.ORCID 0000-0002-0439-1534
Joan-Emma SheaDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106-9510.ORCID 0000-0002-9801-9273
Songi HanDepartment of Chemistry, Northwestern University, Evanston, IL 60208-3113.ORCID 0000-0001-6489-6246

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tau assembles into fibrillar aggregates that are pathological hallmarks of a group of neurodegenerative diseases collectively called tauopathies. Templated aggregation of naïve tau to seeding-competent fibrils that proceed from cell to cell is a key driver of prion-like progression of tauopathies. This study tests the hypothesis that tau, an intrinsically disordered protein, achieves in-register stacking to form seed-competent fibrils by a pinning action of tau to each other and/or the seed surface via a single dominant hotspot to avoid mismatch in tau stacking to fibrils. Structured solvation water has been proposed to be a signature of such hot spots at both the tau fibril-end surface and soluble tau monomers. Although jR2R3-P301L tau exhibits a heterogeneous hydration landscape in its intrinsically disordered state, with enhanced water structuring near the P301L mutation site, it is unclear whether a localized hotspot exists at the fibril end surface and surface water facilitates the initial contacts in templated aggregation. Using rapid

Indexed as

Protein AggregatesProtein Aggregation, PathologicalTauopathiestau ProteinsWaterHumansMagnetic Resonance SpectroscopyMutationProtein Aggregatestau ProteinsWater

Identifiers

PMID42863048
PMCPMC13684300

What OpenQuestion holds

Textmetadata
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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.