Evidence map›Paper›PMID 38512670›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

Quantification of Methylation and Phosphorylation Stoichiometry.

Christopher A Ayoub, Khadijah I Moore, Jeff Kuret

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
2.4field-weighted citation impact, top 15% of its field
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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Article
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

3 authors at 1 institution in 1 country.

Christopher A AyoubMedical Scientist Training Program, Ohio State University College of Medicine, Columbus, OH, USA.
Khadijah I MooreInterdisciplinary Biophysics Graduate Program, Ohio State University College of Medicine, Columbus, OH, USA.
Jeff KuretDepartment of Biological Chemistry and Pharmacology, The Ohio State University College of Medicine, Columbus, OH, USA. kuret.3@osu.edu.
The Ohio State University · US

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
Decoding Selective Vulnerability: Effectors and Regulators of Tau Lesion Spread in Alzheimer's DiseaseF30AG072804 · NIA · OHIO STATE UNIVERSITY · PI AYOUB, CHRISTOPHER ANTHONY · 2022 to 2024
$134k
NIA NIH HHS F30 AG072804NIA NIH HHS R01 AG054018NIA NIH HHS U24 AG072458
6 · The paper itself

Abstract

Tauopathies including Alzheimer's disease (AD) are neurodegenerative disorders accompanied by the conversion of functional forms of the microtubule associated protein Tau into non-functional aggregates. A variety of post-translational modifications (PTMs) on Tau precede or accompany the conversion, placing them in position to modulate Tau function as well as its propensity to aggregate. Although Tau PTMs can be characterized by their sites of modification, their total stoichiometry when summed over all sites also is an important metric of their potential impact on function. Here we provide a protocol for rapidly producing recombinant Tau with enzyme-specific PTMs at high stoichiometry in vitro and demonstrate its utility in the context of hyperphosphorylation. Additionally, protocols for estimating phosphorylation and methylation stoichiometry on Tau proteins isolated from any source are presented. Together these methods support experimentation on Tau PTM function over a wide range of experimental conditions.

Indexed as

Alzheimer DiseaseTauopathiesHumansMethylationPhosphorylationProtein Processing, Post-Translationaltau Proteinstau ProteinsMass spectrometryMethylationPhosphorylationPost-Translational ModificationTau protein

Identifiers

PMID38512670
PMCPMC13180468
OpenAlexW4393051409

What OpenQuestion holds

Textmetadata
LicenceTDM
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.