Evidence map›Paper›PMID 38489865›Full record

ReviewCurrent opinion in neurobiology2024

The structural line between prion and "prion-like": Insights from prion protein and tau.

Calina Glynn, Jose A Rodriguez, Bradley T Hyman

Open access · hybridAbstract readReview
In one paragraph

Review in Current opinion in neurobiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.9field-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

10 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Structure-specific Mini-Prion Model for Alzheimer's Disease Tau Fibrils.bioRxiv : the preprint server for biology · 2025
    Article
  7. Review
  8. Article
  9. Optical Taxonomic Signal and the Diagnosis of Alzheimer's Disease.IEEE open journal of engineering in medicine and biology · 2025
    Article
  10. 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

3 authors at 3 institutions in 1 country.

Calina GlynnDepartment of Neurology, Massachusetts General Hospital, Boston, MA, USA; Harvard Medical School, Cambridge, MA, USA.
Jose A RodriguezDepartment of Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, STROBE, NSF Science and Technology Center, University of California, Los Angeles, Los Angeles, CA, USA.
Bradley T HymanDepartment of Neurology, Massachusetts General Hospital, Boston, MA, USA; Harvard Medical School, Cambridge, MA, USA. Electronic address: bhyman@mgh.harvard.edu.
Harvard University · USMassachusetts General Hospital · USUniversity of California, Los Angeles · US

Funding

Research Education ComponentP30AG062421 · NIA · MASSACHUSETTS GENERAL HOSPITAL · PI STEVEN E ARNOLD · 2019 to 2026
$36.5M
Micro Electron Diffraction of Toxic and/or Infectious Macromolecular NanoassembliesR35GM128867 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Jose Alfonso Rodriguez · 2018 to 2026
$3.1M
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
Liquid liquid phase separation and tau biologyR21AG063347 · NIA · MASSACHUSETTS GENERAL HOSPITAL · PI HYMAN, BRADLEY T. · 2019 to 2020
$450k
NIA NIH HHS P30 AG062421NIA NIH HHS R21 AG063347NIA NIH HHS R56 AG061196NIA NIH HHS RF1 AG058674NIA NIH HHS RF1 AG059789NIA NIH HHS T32 AG066592NIGMS NIH HHS R35 GM128867
6 · The paper itself

Abstract

The concept of 'prion-like' behavior has emerged in the study of diseases involving protein misfolding where fibrillar structures, called amyloids, self-propagate and induce disease in a fashion similar to prions. From a biological standpoint, in order to be considered 'prion-like,' a protein must traverse cells and tissues and further propagate via a templated conformational change. Since 2017, cryo-electron microscopy structures from patient-derived 'prion-like' amyloids, in particular tau, have been presented and revealed structural similarities shared across amyloids. Since 2021, cryo-EM structures from prions of known infectivity have been added to the ex vivo amyloid structure family. In this review, we discuss current proposals for the 'prion-like' mechanisms of spread for tau and prion protein as well as discuss different influencers on structures of aggregates from tauopathies and prion diseases. Lastly, we discuss some of the current hypotheses for what may distinguish structures that are 'prion-like' from transmissible prion structures.

Indexed as

Prion Proteinstau ProteinsAmyloidAnimalsHumansPrion DiseasesPrionsTauopathiesAmyloidPrion ProteinsPrionstau Proteins

Identifiers

PMID38489865
PMCPMC11162956
OpenAlexW4392887999

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.