Evidence map›Paper›PMID 36310203›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

An Additive-Free Model for Tau Self-Assembly.

Youssra K Al-Hilaly, Karen E Marshall, Liisa Lutter, Luca Biasetti, Kurtis Mengham, Charles R Harrington, Wei-Feng Xue, Claude M Wischik, Louise C Serpell

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. 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
2.4field-weighted citation impact, top 11% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Review
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 at 5 institutions in 3 countries.

Youssra K Al-HilalyChemistry Department, College of Science, Mustansiriyah University, Baghdad, Iraq. youssra.alhilaly@uomustansiriyah.edu.iq.
Karen E MarshallSussex Neuroscience, School of Life Sciences, University of Sussex, Sussex, UK.
Liisa LutterSchool of Biosciences, University of Kent, Canterbury, UK.
Luca BiasettiSussex Neuroscience, School of Life Sciences, University of Sussex, Sussex, UK.
Kurtis MenghamSussex Neuroscience, School of Life Sciences, University of Sussex, Sussex, UK.
Charles R HarringtonInstitute of Medical Sciences, University of Aberdeen, Aberdeen, UK.
Wei-Feng XueSchool of Biosciences, University of Kent, Canterbury, UK.
Claude M WischikInstitute of Medical Sciences, University of Aberdeen, Aberdeen, UK.
Louise C SerpellSussex Neuroscience, School of Life Sciences, University of Sussex, Sussex, UK.
University of Sussex · GBUniversity of Kent · GBMustansiriyah University · IQTauRx (United Kingdom) · GBUniversity of Aberdeen · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tau is a natively unfolded protein that contributes to the stability of microtubules. Under pathological conditions such as Alzheimer's disease (AD), tau protein misfolds and self-assembles to form paired helical filaments (PHFs) and straight filaments (SFs). Full-length tau protein assembles poorly and its self-assembly is enhanced with polyanions such as heparin and RNA in vitro, but a role for heparin or other polyanions in vivo remains unclear. Recently, a truncated form of tau (297-391) has been shown to self-assemble in the absence of additives which provides an alternative in vitro PHF model system. Here we describe methods to prepare in vitro PHFs and SFs from tau (297-391) named dGAE. We also discuss the range of biophysical/biochemical techniques used to monitor tau filament assembly and structure.

Indexed as

Alzheimer Diseasetau ProteinsHeparinHumansNeurofibrillary TanglesPolyelectrolytesHeparinPolyelectrolytestau ProteinsAtomic force microscopyCircular dichroismCross-betaElectron microscopyPaired helical filamentSelf-assemblyTauThioflavin S fluorescenceTyrosine fluorescenceX-ray fibre diffraction

Identifiers

PMID36310203
OpenAlexW4307642811

What OpenQuestion holds

Textmetadata
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.