Evidence map›Paper›PMID 42692750›Full record

ArticleMethods in enzymology2026

Lysine methylation is an endogenous post-translational modifications of tau protein in human brain and a modulator of aggregation propensity.

Marisel Sanchez, Jeff Kuret

Abstract read
In one paragraph

Article in Methods in enzymology, 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

2 authors.

Marisel SanchezNeuroscience Graduate Program, The Ohio State University, Columbus, OH, United States.
Jeff KuretDepartment of Biological Chemistry & Pharmacology, The Ohio State University, Columbus, OH, United States. Electronic address: kuret.3@osu.edu.

Funding

Interdisciplinary Research Network on Biologically Active Tau Aggregate Polymorphs from Alzheimer's Disease and Related DementiasU24AG072458 · NIA · UNIVERSITY OF TEXAS MED BR GALVESTON · PI EISENBERG, DAVID, KAYED, RAKEZ · 2021 to 2025
$7.8M
Structure and Genesis of tau AggregatesR01AG054018 · NIA · OHIO STATE UNIVERSITY · PI Jeff Kuret · 2025 to 2026
$1.2M
NIA NIH HHS R01 AG054018NIA NIH HHS U24 AG072458
6 · The paper itself

Abstract

Tau protein undergoes a broad range of post-translational modifications in the brain, influencing its structure, solubility, and propensity to aggregate. This chapter presents an integrated methodological framework for characterizing tau methylation and evaluating its impact on tau biology. We describe procedures for isolating soluble and filamentous tau from post-mortem human brain tissue while preserving modifications for proteomic analysis. These approaches support precise mapping of methylation sites alongside other co-occurring modifications. To model methylation under controlled conditions, we outline protocols for recombinant tau expression, purification, and chemical reductive methylation, including radiolabeled assays for determining modification stoichiometry. We then detail biophysical assays used to assess how methylation alters tau conformation and aggregation propensity. This methodological framework supports experimentation seeking insight into mechanisms relevant to Alzheimer's disease and related tauopathies.

Indexed as

BrainLysineProtein Processing, Post-Translationaltau ProteinsAlzheimer DiseaseHumansMass SpectrometryMethylationProtein AggregatesProtein Aggregation, PathologicalProteomicsRecombinant ProteinsTauopathiesLysineMAPT protein, humanProtein AggregatesRecombinant Proteinstau ProteinsAlzheimer’s diseaseLysine methylationMass spectrometryPost-translational modificationProtein aggregationReductive methylationTauopathiesTau protein

Identifiers

PMID42692750
PMCPMC13542479

What OpenQuestion holds

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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.