Evidence map›Paper›PMID 38154792›Full record

ArticleBiochemistry2024

Reconstitution of the Alzheimer's Disease Tau Core Structure from Recombinant Tau

Calina Glynn, Joshua E Chun, Cameron C Donahue, Monica J S Nadler, Zhanyun Fan, Bradley T Hyman

Abstract read
In one paragraph

Article in Biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Structure-specific Mini-Prion Model for Alzheimer's Disease Tau Fibrils.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Inducers and modulators of protein aggregation in Alzheimer's disease - Critical tools for understanding the foundations of aggregate structures.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Post-Translational Modifications Control Phase Transitions of Tau.bioRxiv : the preprint server for biology · 2024
    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

6 authors.

Calina GlynnDepartment of Neurology, Massachusetts General Hospital, Boston, Massachusetts 02114, United States.ORCID 0000-0002-2197-2357
Joshua E ChunDepartment of Neurology, Massachusetts General Hospital, Boston, Massachusetts 02114, United States.
Cameron C DonahueDepartment of Neurology, Massachusetts General Hospital, Boston, Massachusetts 02114, United States.
Monica J S NadlerDepartment of Neurology, Massachusetts General Hospital, Boston, Massachusetts 02114, United States.
Zhanyun FanDepartment of Neurology, Massachusetts General Hospital, Boston, Massachusetts 02114, United States.
Bradley T HymanDepartment of Neurology, Massachusetts General Hospital, Boston, Massachusetts 02114, United States.ORCID 0000-0002-7959-9401

Funding

Are multiple tau species toxic in Alzheimer's Disease?RF1AG059789 · NIA · MASSACHUSETTS GENERAL HOSPITAL · PI HYMAN, BRADLEY T. · 2018 to 2018
$2.7M
Synergy between amyloid and tau in Alzheimer's DiseaseRF1AG058674 · NIA · MASSACHUSETTS GENERAL HOSPITAL · PI HYMAN, BRADLEY T. · 2018 to 2018
$2.6M
Program to enrich translation and multimodal research in Alzheimers disease and related dementiasT32AG066592 · NIA · MASSACHUSETTS GENERAL HOSPITAL · PI PRICE, JULIE C · 2021 to 2025
$1.6M
Complexity and Heterogeneity of Alzheimer diseaseR56AG061196 · NIA · MASSACHUSETTS GENERAL HOSPITAL · PI HYMAN, BRADLEY T. · 2019 to 2019
$654k
AGING AND RESPONSES OF AUDITORY NEURONSR01AG006241 · NIA · NORTHERN ILLINOIS UNIVERSITY · PI WILLOTT, JAMES F · 1986 to 1988
–
NIA NIH HHS P30 AG06241NIA NIH HHS R56 AG061196NIA NIH HHS RF1 AG058674NIA NIH HHS RF1 AG059789NIA NIH HHS T32 AG066592
6 · The paper itself

Abstract

The protein tau misfolds into disease-specific fibrillar structures in more than 20 neurodegenerative diseases collectively referred to as tauopathies. To understand and prevent disease-specific mechanisms of filament formation,

Indexed as

Alzheimer Diseasetau ProteinsCryoelectron MicroscopyHumansNeurofibrillary TanglesProtein Structure, Quaternarytau Proteins

Identifiers

PMID38154792
PMCPMC10795186

What OpenQuestion holds

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Read underepoch 390

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.