Evidence map›Paper›PMID 29853639›Full record

ArticleThe Journal of biological chemistry2018

Effects of phosphatidylcholine membrane fluidity on the conformation and aggregation of N-terminally acetylated α-synuclein.

Emma I O'Leary, Zhiping Jiang, Marie-Paule Strub, Jennifer C Lee

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
4.4field-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

71 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. Elevation of Stearoyl-Coenzyme A Desaturase and Monounsaturated Fatty Acids in Parkinson's Disease Serum.Movement disorders : official journal of the Movement Disorder Society · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Lipid-packing defects are sufficient to modulate membrane insertion and the bound state of α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Article
  13. Dysregulation of Monounsaturated Fatty Acids is Related to α-Synuclein in Multiple System Atrophy.Movement disorders : official journal of the Movement Disorder Society · 2025
    Article
  14. Article
  15. Article
  16. Amyloid formation of alternatively spliced variants of α-synuclein.Protein science : a publication of the Protein Society · 2025
    Article
  17. Article
  18. Insulin Resistance Is a Modifying Factor for Parkinson's Disease.Movement disorders : official journal of the Movement Disorder Society · 2025
    Article
  19. Review
  20. Review

11 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

4 authors at 1 institution in 2 countries.

Emma I O'LearyFrom the Laboratory of Protein Conformation and Dynamics and.
Zhiping JiangFrom the Laboratory of Protein Conformation and Dynamics and.
Marie-Paule Strubthe Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20892.
Jennifer C LeeFrom the Laboratory of Protein Conformation and Dynamics and leej4@mail.nih.gov.ORCID 0000-0003-0506-8349
National Institutes of Health · US

Funding

Protein Misfolding and AggregationZIAHL001055 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI LEE, JENNIFER · 2009 to 2025
$16.9M
6 · The paper itself

Abstract

Membrane association of α-synuclein (α-syn), a neuronal protein associated with Parkinson's disease (PD), is involved in α-syn function and pathology. Most previous studies on α-syn-membrane interactions have not used the physiologically relevant N-terminally acetylated (

Indexed as

Membrane FluidityAcetylationalpha-SynucleinAmino Acid SequenceAmyloidbeta-SynucleinCholesterolgamma-SynucleinHumansLipid BilayersMicellesNeoplasm ProteinsPhosphatidylcholinesProtein BindingProtein ConformationSequence Homologyalpha-SynucleinAmyloidbeta-SynucleinCholesterolgamma-SynucleinLipid BilayersMicellesNeoplasm ProteinsPhosphatidylcholinesSNCA protein, humanSNCB protein, humanSNCG protein, humanamyloidamyloid fibrilcircular dichroism (CD)gel-phaseliquid-ordered phaseParkinson diseasephosphatidylcholinepost-translational modification (PTM)protein–lipid interactionα-synuclein

Identifiers

PMID29853639
PMCPMC6052208
OpenAlexW2805481869

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.