Evidence map›Paper›PMID 26940507›Full record

ReviewBrain pathology (Zurich, Switzerland)2016

Protein Partners of α-Synuclein in Health and Disease.

Louise Berkhoudt Lassen, Lasse Reimer, Nelson Ferreira, Cristine Betzer, Poul Henning Jensen

Abstract readReview
In one paragraph

Review in Brain pathology (Zurich, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Copper ion incorporation in α-synuclein amyloids.Protein science : a publication of the Protein Society · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Interplay between tau and α-synuclein liquid-liquid phase separation.Protein science : a publication of the Protein Society · 2021
    Article
  12. Review
  13. Article
  14. Single-vesicle imaging reveals lipid-selective and stepwise membrane disruption by monomeric α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. The Molecular Basis of the Interaction of Cyclophilin A with α-Synuclein.Angewandte Chemie (International ed. in English) · 2020
    Article
  16. Review
  17. Article
  18. Review
  19. Recent advances on the molecular pathogenesis of prion diseases.Brain pathology (Zurich, Switzerland) · 2019
    Article
  20. Cell Responses to Extracellular α-Synuclein.Molecules (Basel, Switzerland) · 2019
    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

5 authors.

Louise Berkhoudt LassenDANDRITE-Danish Research Institute of Translational Neuroscience & Department of Biomedicine, University of Aarhus, Aarhus, Denmark.
Lasse ReimerDANDRITE-Danish Research Institute of Translational Neuroscience & Department of Biomedicine, University of Aarhus, Aarhus, Denmark.
Nelson FerreiraDANDRITE-Danish Research Institute of Translational Neuroscience & Department of Biomedicine, University of Aarhus, Aarhus, Denmark.
Cristine BetzerDANDRITE-Danish Research Institute of Translational Neuroscience & Department of Biomedicine, University of Aarhus, Aarhus, Denmark.
Poul Henning JensenDANDRITE-Danish Research Institute of Translational Neuroscience & Department of Biomedicine, University of Aarhus, Aarhus, Denmark.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-synuclein is normally situated in the nerve terminal but it accumulates and aggregates in axons and cell bodies in synucleinopathies such as Parkinson's disease. The conformational changes occurring during α-synucleins aggregation process affects its interactions with other proteins and its subcellular localization. This review focuses on interaction partners of α-synuclein within different compartments of the cell with a focus on those preferentially binding aggregated α-synuclein. The aggregation state of α-synuclein also affects its catabolism and we hypothesize impaired macroautophagy is involved neuronal excretion of α-synuclein species responsible for the prion-like spreading of α-synuclein pathology.

Indexed as

alpha-SynucleinAnimalsHumansNeurodegenerative Diseasesalpha-SynucleindementiaLewy BodyneurodegenerationParkinson's diseaseprotein interactionproteomicsα-synuclein

Identifiers

PMID26940507
PMCPMC8029326

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.