Evidence map›Paper›PMID 28373279›Full record

ArticleThe Journal of biological chemistry2017

A sensitive assay reveals structural requirements for α-synuclein fibril growth.

Dhruva D Dhavale, Christina Tsai, Devika P Bagchi, Laura A Engel, Jonathan Sarezky, Paul T Kotzbauer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  6. Seeding competent TDP-43 persists in human patient and mouse muscle.bioRxiv : the preprint server for biology · 2024
    Article
  7. Article
  8. Article
  9. Monitoring α-synuclein aggregation.Neurobiology of disease · 2023
    Review
  10. Review
  11. VCP suppresses proteopathic seeding in neurons.Molecular neurodegeneration · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. A53T Mutant Alpha-Synuclein Induces Tau-Dependent Postsynaptic Impairment Independently of Neurodegenerative Changes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  17. Article
  18. Article
  19. Glucose directs amyloid-beta into membrane-active oligomers.Physical chemistry chemical physics : PCCP · 2017
    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 at 1 institution in 1 country.

Dhruva D DhavaleFrom the Department of Neurology and Hope Center for Neurological Disorders, Washington University School of Medicine, St. Louis, Missouri 63110.ORCID 0000-0002-0096-1085
Christina TsaiFrom the Department of Neurology and Hope Center for Neurological Disorders, Washington University School of Medicine, St. Louis, Missouri 63110.
Devika P BagchiFrom the Department of Neurology and Hope Center for Neurological Disorders, Washington University School of Medicine, St. Louis, Missouri 63110.
Laura A EngelFrom the Department of Neurology and Hope Center for Neurological Disorders, Washington University School of Medicine, St. Louis, Missouri 63110.
Jonathan SarezkyFrom the Department of Neurology and Hope Center for Neurological Disorders, Washington University School of Medicine, St. Louis, Missouri 63110.
Paul T KotzbauerFrom the Department of Neurology and Hope Center for Neurological Disorders, Washington University School of Medicine, St. Louis, Missouri 63110 kotzbauerp@wustl.edu.
Hope Center for Neurological Disorders · US

Funding

Washington University Institute of Clinical and Translational SciencesUL1TR000448 · NCATS · WASHINGTON UNIVERSITY · PI EVANOFF, BRADLEY A · 2012 to 2016
$41.4M
Protein Aggregation and Neurotransmitter Deficits in Parkinson DiseaseR01NS097799 · NINDS · WASHINGTON UNIVERSITY · PI PAUL T KOTZBAUER · 2016 to 2026
$5.8M
Neurodegenerative consequences of PanK2 mutationsK08NS048924 · NINDS · WASHINGTON UNIVERSITY · PI KOTZBAUER, PAUL T · 2004 to 2008
$878k
ATOMIC FORCE MICROSCOPES10RR024733 · NCRR · WASHINGTON UNIVERSITY · PI GOLDBERG, MARK PAUL · 2008 to 2008
$275k
NCATS NIH HHS UL1 TR000448NCRR NIH HHS S10 RR024733NINDS NIH HHS K08 NS048924NINDS NIH HHS R01 NS097799
6 · The paper itself

Abstract

The accumulation of α-synuclein (α-syn) fibrils in neuronal inclusions is the defining pathological process in Parkinson's disease (PD). A pathogenic role for α-syn fibril accumulation is supported by the identification of dominantly inherited α-syn (

Indexed as

Mutation, MissenseParkinson DiseaseProtein Aggregation, Pathologicalalpha-SynucleinAmino Acid SubstitutionAmyloidHumansalpha-SynucleinAmyloidSNCA protein, humanalpha-synucleinbiarsenical tetracysteinefibrilFlAsHmutationsneurodegenerationoligomersParkinson's diseaseprotein aggregationprotein labeling

Identifiers

PMID28373279
PMCPMC5454090
OpenAlexW2604118844

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.