Evidence map›Paper›PMID 41804868›Full record

ArticleFEBS letters2026

Tau acetylation at K331 has limited impact on tau pathology in vivo.

Shoko Hashimoto, Yukio Matsuba, Mika Takahashi, Takaomi C Saido

Abstract read
In one paragraph

Article in FEBS letters, 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

4 authors.

Shoko HashimotoPioneering Research Division, Medical Innovation Research Center, Shiga University of Medical Science, Otsu, Shiga, Japan.ORCID https://orcid.org/0000-0002-5778-4884
Yukio MatsubaPioneering Research Division, Medical Innovation Research Center, Shiga University of Medical Science, Otsu, Shiga, Japan.
Mika TakahashiLaboratory for Proteolytic Neuroscience, RIKEN Center for Brain Science, Wako, Saitama, Japan.
Takaomi C SaidoLaboratory for Proteolytic Neuroscience, RIKEN Center for Brain Science, Wako, Saitama, Japan.ORCID https://orcid.org/0000-0003-1970-6903

Funding

Co-creation place formation support program JPMJPF2018Japan Society for the Promotion of Science JP22H05037Japan Society for the Promotion of Science JP23K06407
6 · The paper itself

Abstract

Post-translational modifications regulate tau aggregation and propagation, yet how amyloid pathology shapes the tau modification landscape remains unclear. Using liquid chromatography-tandem mass spectrometry, we compared tau modifications in MAPT knock-in (MAPT KI) mice and MAPT/App double knock-in mice with App

Indexed as

tau ProteinsAcetylationAnimalsBrainGene Knock-In TechniquesHumansLysineMacaca fascicularisMiceMice, TransgenicPhosphorylationProtein Processing, Post-TranslationalLysinetau ProteinsacetylationAlzheimer's diseaseknock‐in mouse modelspost‐translational modificationsTau

Identifiers

PMID41804868
PMCPMC13404147

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.