Evidence map›Paper›PMID 27742354›Full record

ArticleBiochimica et biophysica acta. Biomembranes2017

Polyunsaturated chains in asymmetric lipids disorder raft mixtures and preferentially associate with α-Synuclein.

Benjamin E Brummel, Anthony R Braun, Jonathan N Sachs

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 28% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Parkinson disease is a fatty acidopathy.Nature reviews. Neurology · 2025
    Review
  2. Beyond Fluidity: The Role of Lipid Unsaturation in Membrane Function.Cold Spring Harbor perspectives in biology · 2023
    Review
  3. Review
  4. Dysfunction of Synaptic Vesicle Endocytosis in Parkinson's Disease.Frontiers in integrative neuroscience · 2021
    Review
  5. Article
  6. Review
  7. Review
  8. 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

3 authors at 1 institution in 1 country.

Benjamin E BrummelDepartment of Biomedical Engineering, University of Minnesota, 7-124 Nils Hasselmo Hall, 312 Church St SE, Minneapolis, MN 55455, USA. Electronic address: brumm082@umn.edu.
Anthony R BraunDepartment of Biomedical Engineering, University of Minnesota, 7-124 Nils Hasselmo Hall, 312 Church St SE, Minneapolis, MN 55455, USA. Electronic address: brau0123@umn.edu.
Jonathan N SachsDepartment of Biomedical Engineering, University of Minnesota, 7-124 Nils Hasselmo Hall, 312 Church St SE, Minneapolis, MN 55455, USA. Electronic address: jnsachs@umn.edu.
University of Minnesota · US

Funding

Modeling synaptic vesicles: how does alpha-Synuclein inhibit fusion?R01NS084998 · NINDS · UNIVERSITY OF MINNESOTA · PI SACHS, JONATHAN N · 2013 to 2017
$1.9M
NIH HHS R01 NS084998-01NINDS NIH HHS R01 NS084998
6 · The paper itself

Abstract

Using molecular dynamics simulations, we have explored the effect of asymmetric lipids-specifically those that contain one polyunsaturated (PUFA) and one saturated fatty acid chain-on phase separation in heterogeneous membranes. These lipids are prevalent in neuronal membranes, particularly in synaptic membranes, where the Parkinson's Disease protein α-Synuclein (αS) is found. We have therefore explored the relationship between asymmetric, PUFA-containing lipids, and αS. The simulations show that asymmetric lipids partition to the liquid disordered (Ld) phase of canonical raft mixtures because of the highly disordered PUFA chain. In the case of a membrane built to mimic the lipid composition of a synaptic vesicle, the PUFA-containing asymmetric lipids completely disrupt phase separation. Because αS is positively charged, we show that it partitions with negatively charged lipids, regardless of the saturation state of the chains. Additionally, αS preferentially associates with the polyunsaturated fatty acid tails of both charged and neutral lipids. This is a consequence of those chains' ability to accommodate the void beneath the amphipathic helix. This article is part of a Special Issue entitled: Lipid order/lipid defects and lipid-control of protein activity edited by Dirk Schneider.

Indexed as

Molecular Dynamics Simulation1,2-Dipalmitoylphosphatidylcholinealpha-SynucleinBiomimetic MaterialsCholesterolHumansMembrane MicrodomainsMolecular ConformationPhase TransitionPhosphatidylcholinesProtein BindingStatic Electricity1,2-Dipalmitoylphosphatidylcholine1,2-linoleoylphosphatidylcholinealpha-SynucleinCholesterolPhosphatidylcholinesAmphipathic helicesLipid raftsMolecular dynamics simulationsPhase separationPolyunsaturated fatty acidsα-Synuclein

Identifiers

PMID27742354
PMCPMC5749632
OpenAlexW2530280857

What OpenQuestion holds

Textmetadata
LicenceTDM
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.