Evidence map›Paper›PMID 27273030›Full record

ArticleScientific reports2016

Structural Ensembles of Membrane-bound α-Synuclein Reveal the Molecular Determinants of Synaptic Vesicle Affinity.

Giuliana Fusco, Alfonso De Simone, Paolo Arosio, Michele Vendruscolo, Gianluigi Veglia, Christopher M Dobson

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 99 citations in OpenAlex.

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  19. α-Synuclein and biological membranes: the danger of loving too much.Chemical communications (Cambridge, England) · 2023
    Review
  20. Article

6 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Giuliana FuscoDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Alfonso De SimoneDepartment of Life Sciences, Imperial College London, South Kensington, London SW7 2AZ, UK.
Paolo ArosioDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Michele VendruscoloDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Gianluigi VegliaDepartment of Chemistry &Department of Biochemistry, Molecular Biology &Biophysics, University of Minnesota, 6-155 Jackson Hall 321 Church st. SE, Minneapolis, MN 55455, USA.
Christopher M DobsonDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
University of Cambridge · GBImperial College London · GBUniversity of Minnesota · US

Funding

Medical Research Council MR/N000676/1Parkinson's UK H-1103Wellcome Trust
6 · The paper itself

Abstract

A detailed characterisation of the molecular determinants of membrane binding by α-synuclein (αS), a 140-residue protein whose aggregation is associated with Parkinson's disease, is of fundamental significance to clarify the manner in which the balance between functional and dysfunctional processes are regulated for this protein. Despite its biological relevance, the structural nature of the membrane-bound state αS remains elusive, in part because of the intrinsically dynamic nature of the protein and also because of the difficulties in studying this state in a physiologically relevant environment. In the present study we have used solid-state NMR and restrained MD simulations to refine structure and topology of the N-terminal region of αS bound to the surface of synaptic-like membranes. This region has fundamental importance in the binding mechanism of αS as it acts as to anchor the protein to lipid bilayers. The results enabled the identification of the key elements for the biological properties of αS in its membrane-bound state.

Indexed as

alpha-SynucleinBinding SitesHumansLipid BilayersMagnetic Resonance SpectroscopyMembranesModels, MolecularMolecular ConformationMolecular Dynamics SimulationProtein BindingProtein Structure, SecondarySynaptic Vesiclesalpha-SynucleinLipid BilayersSNCA protein, human

Identifiers

PMID27273030
PMCPMC4897633
OpenAlexW2413508469

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Registered trials

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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.