Evidence map›Paper›PMID 42175841›Full record

ArticleAngewandte Chemie (International ed. in English)2026

Water-Mediated Phosphoryl Wires Stabilize Pathological Tau Fibrils.

Lokeswara Rao Potnuru, Austin DuBose, Fiona Mon, Mesopotamia S Nowotarski, Michael Vigers, Boqin Zhang, Chung-Ta Han, John E Straub, Songi Han

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. A water-pinning hot spot drives templated tau aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. A water-pinning hotspot drives templated tau aggregation.bioRxiv : the preprint server for biology · 2026
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Lokeswara Rao PotnuruDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.ORCID 0000-0003-1321-9784
Austin DuBoseDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California, USA.
Fiona MonDepartment of Chemistry, Boston University, Boston, Massachusetts, USA.
Mesopotamia S NowotarskiDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California, USA.
Michael VigersDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California, USA.
Boqin ZhangDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California, USA.
Chung-Ta HanDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
John E StraubDepartment of Chemistry, Boston University, Boston, Massachusetts, USA.
Songi HanDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.ORCID 0000-0001-6489-6246

Funding

Probing the roles of membrane and cholesterol on Aβ biogenesis and prion protein interactionsR01GM107703 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI STRAUB, JOHN E., THIRUMALAI, DEVARAJAN · 2015 to 2022
$2.7M
Water as essential building blocks to direct protein structure and functionR35GM136411 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI Songi Han · 2020 to 2026
$2.4M
National Science Foundation CHE-2505621National Science Foundation DMR-1720256National Science Foundation FAIN-2423884NIGMS NIH HHS R01 GM107703NIGMS NIH HHS R35 GM136411NIH HHS R01GM107703NIH HHS R35GM136411
6 · The paper itself

Abstract

Hyperphosphorylation of tau is a hallmark of tauopathies, with specific phosphorylation sites elevated in pathological fibrils. However, the molecular role of this post-translational modification (PTM) in driving tau aggregation remains unclear. In-register fibril assembly places phosphoryl groups on adjacent monomers at ∼4.8 Å spacing, requiring an energetically favorable arrangement. Conventional intuition holds that closely packed phosphoryl groups should be electrostatically unfavorable. We test the opposing hypothesis: that phosphoryl groups within the fibril core associate into an extended "wire" that stabilizes the amyloid fibril. We examined two phosphorylation sites linked to neurodegeneration, serine 305 (S305

Indexed as

tau ProteinsWaterHumansMolecular Dynamics SimulationPhosphorylationtau ProteinsWater31P solid‐state NMRDNPmolecular dynamic simulationsmultiple‐quantum spin countingphosphorylationtauopathy

Identifiers

PMID42175841
PMCPMC13383178

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.