Evidence map›Paper›PMID 24599158›Full record

ArticlePloS one2014

Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity.

Julia Gath, Luc Bousset, Birgit Habenstein, Ronald Melki, Anja Böckmann, Beat H Meier

Open access · goldAbstract readComparative Study
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
5.5field-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

69 citing papers in PubMed, 133 citations in OpenAlex.

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  17. Liquid-liquid phase separation and conformational strains ofFrontiers in molecular neuroscience · 2024
    Review
  18. Direct Observation of Seeded Conformational Conversion of hIAPPJournal of chemical information and modeling · 2023
    Article
  19. Article
  20. Solid-State NMR Structure of Amyloid-β Fibrils.Methods in molecular biology (Clifton, N.J.) · 2023
    Article

9 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.

Julia GathPhysical Chemistry, ETH Zürich, Zurich, Switzerland.
Luc BoussetLaboratoire d'Enzymologie et Biochimie Structurales, UPR 3082 CNRS, Gif-sur-Yvette, France.
Birgit HabensteinInstitut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, Lyon, France.
Ronald MelkiLaboratoire d'Enzymologie et Biochimie Structurales, UPR 3082 CNRS, Gif-sur-Yvette, France.
Anja BöckmannInstitut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, Lyon, France.
Beat H MeierPhysical Chemistry, ETH Zürich, Zurich, Switzerland.
Centre National de la Recherche Scientifique · FRETH Zurich · CHUniversité Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We structurally compare, using solid-state NMR, two different polymorphs of α-synuclein which, as established recently, display contrasting biochemical properties, toxicity, and tropism for cells. We show that both forms, which can each be produced as a pure polymorph, are greatly different in secondary structure. While β-sheets are the dominating secondary structure elements for both polymorphs, they are markedly divergent in terms of number of elements, as well as their distribution. We demonstrate that all identified β-sheets feature an in-register parallel stacking for both polymorphs. The two forms show a different molecular arrangement in the unit cell and distinct dynamic features, while sharing a highly flexible C-terminal domain. The use of reproducible, well-identified conditions for sample preparation and the recording of identical NMR experiments allows for a direct comparison of the results.

Indexed as

Magnetic Resonance Spectroscopyalpha-SynucleinAmino Acid SequenceHumansMolecular Sequence DataPliabilityProtein IsoformsProtein Structure, Secondaryalpha-SynucleinProtein Isoforms

Identifiers

PMID24599158
PMCPMC3944079
OpenAlexW1997167527

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.