Evidence map›Paper›PMID 38806297›Full record

ReviewTrends in neurosciences2024

Effect of host and strain factors on α-synuclein prion pathogenesis.

Amanda L Woerman, Jason C Bartz

Abstract readReview
In one paragraph

Review in Trends in neurosciences, 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
–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

10 citing papers in PubMed.

  1. Article
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  4. Review
  5. Article
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  9. Review
  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

2 authors.

Amanda L WoermanDepartment of Microbiology, Immunology, and Pathology, Prion Research Center, Colorado State University, Fort Collins, CO, USA. Electronic address: amanda.woerman@colostate.edu.
Jason C BartzDepartment of Microbiology, Immunology, and Pathology, Prion Research Center, Colorado State University, Fort Collins, CO, USA; Department of Medical Microbiology and Immunology, School of Medicine, Creighton University, Omaha, NE, USA. Electronic address: jbartz@creighton.edu.

Funding

Zoonotic potential of CWD and influence of environmental contamination on prion propagationP01AI077774 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI EDWARD Arthur HOOVER · 2008 to 2026
$36.1M
Effect of Agent and Host Factors on Alpha-Synuclein Strain PathogenesisR01NS121294 · NINDS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI Amanda L. Woerman · 2022 to 2026
$2.9M
Mechanisms of prion spread and establishment of infectionR01NS107246 · NINDS · CREIGHTON UNIVERSITY · PI BARTZ, JASON C, KINCAID, ANTHONY E. · 2018 to 2022
$2.4M
Contributions of prion strains and substrains to prion zoonotic potential and evolutionR01NS133050 · NINDS · CREIGHTON UNIVERSITY · PI Jason C Bartz · 2023 to 2026
$2.2M
Mechanisms of prion strain dynamicsR01NS103763 · NINDS · CREIGHTON UNIVERSITY · PI BARTZ, JASON C · 2018 to 2022
$1.9M
A Novel Gene Therapy Approach to Prevent Alpha-synuclein Misfolding in Multiple System AtrophyR21NS127002 · NINDS · COLORADO STATE UNIVERSITY · PI WOERMAN, AMANDA L. · 2023 to 2024
$422k
NIAID NIH HHS P01 AI077774NINDS NIH HHS R01 NS103763NINDS NIH HHS R01 NS107246NINDS NIH HHS R01 NS121294NINDS NIH HHS R01 NS133050NINDS NIH HHS R21 NS127002
6 · The paper itself

Abstract

Prion diseases are a group of neurodegenerative disorders caused by misfolding of proteins into pathogenic conformations that self-template to spread disease. Although this mechanism is largely associated with the prion protein (PrP) in classical prion diseases, a growing literature indicates that other proteins, including α-synuclein, rely on a similar disease mechanism. Notably, α-synuclein misfolds into distinct conformations, or strains, that cause discrete clinical disorders including multiple system atrophy (MSA) and Parkinson's disease (PD). Because the recognized similarities between PrP and α-synuclein are increasing, this review article draws from research on PrP to identify the host and strain factors that impact disease pathogenesis, predominantly in rodent models, and focuses on key considerations for future research on α-synuclein prions.

Indexed as

alpha-SynucleinPrion DiseasesAnimalsHumansPrionsalpha-SynucleinPrionsmultiple system atrophyneurodegenerative diseasesParkinson's diseaseprion titerstrain biologystrain interactions

Identifiers

PMID38806297
PMCPMC11236502

What OpenQuestion holds

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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.