Evidence map›Paper›PMID 32203399›Full record

ReviewNature reviews. Neurology2020

Protein transmission in neurodegenerative disease.

Chao Peng, John Q Trojanowski, Virginia M-Y Lee

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Neurology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 352 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
352citing papers in PubMed, 1 pooled it
42.0field-weighted citation impact, top 1% 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

352 citing papers in PubMed, 1 synthesis or guideline pooled it, 590 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. SIRT1 in Neurodegenerative Diseases: Molecular Mechanisms, Disease Relevance, and Therapeutic Potential.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  7. Article
  8. Article
  9. International journal of molecular sciences · 2026
    Review
  10. The glymphatic system and Parkinson's disease: a narrative review.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

292 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Chao PengDepartment of Neurology, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA, USA.
John Q TrojanowskiThe Department of Pathology and Laboratory Medicine, Institute on Aging and Center for Neurodegenerative Disease Research, The Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA, USA.ORCID http://orcid.org/0000-0002-9239-8794
Virginia M-Y LeeThe Department of Pathology and Laboratory Medicine, Institute on Aging and Center for Neurodegenerative Disease Research, The Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA, USA. vmylee@upenn.edu.ORCID http://orcid.org/0000-0003-3536-6902
Institute on Aging · USUniversity of California, Los Angeles · US

Funding

Project IV "Tackling Heterogeneity of Cognitive Trajectory in LBD"U19AG062418 · NIA · UNIVERSITY OF PENNSYLVANIA · PI TROJANOWSKI, JOHN Q. · 2019 to 2023
$18.1M
NIA NIH HHS U19 AG062418
6 · The paper itself

Abstract

Most neurodegenerative diseases are characterized by the intracellular or extracellular aggregation of misfolded proteins such as amyloid-β and tau in Alzheimer disease, α-synuclein in Parkinson disease, and TAR DNA-binding protein 43 in amyotrophic lateral sclerosis. Accumulating evidence from both human studies and disease models indicates that intercellular transmission and the subsequent templated amplification of these misfolded proteins are involved in the onset and progression of various neurodegenerative diseases. The misfolded proteins that are transferred between cells are referred to as 'pathological seeds'. Recent studies have made exciting progress in identifying the characteristics of different pathological seeds, particularly those isolated from diseased brains. Advances have also been made in our understanding of the molecular mechanisms that regulate the transmission process, and the influence of the host cell on the conformation and properties of pathological seeds. The aim of this Review is to summarize our current knowledge of the cell-to-cell transmission of pathological proteins and to identify key questions for future investigation.

Indexed as

Protein Transportalpha-SynucleinAlzheimer DiseaseAmyloid beta-PeptidesAmyotrophic Lateral SclerosisAxonal TransportBrainCell CommunicationDNA-Binding ProteinsEndocytosisExosomesGenetic Predisposition to DiseaseHumansHuntingtin ProteinHuntington DiseaseMembrane Fusionalpha-SynucleinAmyloid beta-PeptidesDNA-Binding ProteinsHuntingtin ProteinTARDBP protein, humantau Proteins

Identifiers

PMID32203399
PMCPMC9242841
OpenAlexW3012646333

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.