Evidence map›Paper›PMID 30028312›Full record

ReviewNeural regeneration research2018

Subcellular localization of alpha-synuclein aggregates and their interaction with membranes.

Fabiana Miraglia, Alessio Ricci, Lucia Rota, Emanuela Colla

Open access · goldAbstract readReview
In one paragraph

Review in Neural regeneration research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Copper ion incorporation in α-synuclein amyloids.Protein science : a publication of the Protein Society · 2024
    Article
  11. Article
  12. Review
  13. Liquid-liquid phase separation and conformational strains ofFrontiers in molecular neuroscience · 2024
    Review
  14. Article
  15. Article
  16. ⍺-Synuclein Structural Diversity and the Cellular Environment in ⍺-Synuclein Transmission Models and Humans.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2023
    Review
  17. Review
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Fabiana MiragliaBio@SNS Laboratory, Scuola Normale Superiore, Pisa; Department of Pharmacy, University of Pisa, Pisa, Italy.
Alessio RicciBio@SNS Laboratory, Scuola Normale Superiore, Pisa, Italy.
Lucia RotaBio@SNS Laboratory, Scuola Normale Superiore, Pisa, Italy.
Emanuela CollaBio@SNS Laboratory, Scuola Normale Superiore, Pisa, Italy.
Scuola Normale Superiore · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For more than a decade numerous evidence has been reported on the mechanisms of toxicity of α-synuclein (αS) oligomers and aggregates in α-synucleinopathies. These species were thought to form freely in the cytoplasm but recent reports of αS multimer conformations when bound to synaptic vesicles in physiological conditions, have raised the question about where αS aggregation initiates. In this review we focus on recent literature regarding the impact on membrane binding and subcellular localization of αS toxic species to understand how regular cellular function of αS contributes to pathology. Notably αS has been reported to mainly associate with specific membranes in neurons such as those of synaptic vesicles, ER/Golgi and the mitochondria, while toxic species of αS have been shown to inhibit, among others, neurotransmission, protein trafficking and mitochondrial function. Strategies interfering with αS membrane binding have shown to improve αS-driven toxicity in worms and in mice. Thus, a selective membrane binding that would result in a specific subcellular localization could be the key to understand how aggregation and pathology evolves, pointing out to αS functions that are primarily affected before onset of irreversible damage.

Indexed as

aggregatesalpha-synucleinalpha-synucleinopathiesmembranes bindingneurodegenerationoligomersParkinson's diseasesubcellular localization

Identifiers

PMID30028312
PMCPMC6065224
OpenAlexW2883157135

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.