Evidence map›Paper›PMID 27920026›Full record

ReviewCold Spring Harbor perspectives in medicine2017

The Transcellular Propagation and Intracellular Trafficking of α-Synuclein.

George K Tofaris, Michel Goedert, Maria Grazia Spillantini

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Initiation and progression of α-synuclein pathology in Parkinson's disease.Cellular and molecular life sciences : CMLS · 2022
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Structurally distinct α-synuclein fibrils induce robust parkinsonian pathology.Movement disorders : official journal of the Movement Disorder Society · 2020
    Article
  16. Review
  17. Alpha-synuclein oligomerization increases its effect on promoting NMDA receptor internalization.International journal of clinical and experimental pathology · 2019
    Article
  18. α-Synuclein: Multiple System Atrophy Prions.Cold Spring Harbor perspectives in medicine · 2018
    Review
  19. Cell Biology and Pathophysiology of α-Synuclein.Cold Spring Harbor perspectives in medicine · 2018
    Review
  20. Familial Parkinson's point mutation abolishes multiple system atrophy prion replication.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

3 authors at 3 institutions in 1 country.

George K TofarisNuffield Department of Clinical Neurosciences, University of Oxford, Oxford, UK.
Michel GoedertMRC Laboratory of Molecular Biology, Cambridge, UK.
Maria Grazia SpillantiniDepartment of Clinical Neurosciences, University of Cambridge, Cambridge, UK.
MRC Laboratory of Molecular Biology · GBUniversity of Cambridge · GBUniversity of Oxford · GB

Funding

Medical Research Council MC_U105184291Parkinson's UK G-0701Parkinson's UK G-1011Parkinson's UK G-1102Parkinson's UK J-0901Wellcome Trust
6 · The paper itself

Abstract

Parkinson's disease is the second most common neurodegenerative disorder, with only partial symptomatic therapy and no mechanism-based therapies. The accumulation and aggregation of α-synuclein is causatively linked to the sporadic form of the disease, which accounts for 95% of cases. The pathology is a result of a gain of toxic function of misfolded α-synuclein conformers, which can template the aggregation of soluble monomers and lead to cellular dysfunction, at least partly by interfering with membrane fusion events at synaptic terminals. Here, we discuss the transcellular propagation and intracellular trafficking of α-synuclein and posit that endosomal processing could be a point of convergence between these two routes. Understanding these events will clarify the therapeutic potential of enzymes that regulate protein trafficking and degradation in synucleinopathies.

Indexed as

alpha-SynucleinAnimalsDisease Models, AnimalHumansParkinson DiseaseProtein TransportSNARE Proteinsalpha-SynucleinSNARE Proteins

Identifiers

PMID27920026
PMCPMC5580513
OpenAlexW2559989756

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.