Evidence map›Paper›PMID 26972046›Full record

ReviewBiochimica et biophysica acta2016

Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein.

Ana West, Benjamin E Brummel, Anthony R Braun, Elizabeth Rhoades, Jonathan N Sachs

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. The disordered and structured regions ofbioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Decrease inInternational journal of molecular sciences · 2021
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Interplay between α-synuclein amyloid formation and membrane structure.Biochimica et biophysica acta. Proteins and proteomics · 2019
    Review
  17. Article
  18. Neurology · 2018
    Article
  19. Article
  20. Biophysics of membrane curvature remodeling at molecular and mesoscopic lengthscales.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    Article
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.

Ana WestDepartment of Biomedical Engineering, University of Minnesota, 312 Church St. SE, Minneapolis, MN 55455, USA.
Benjamin E BrummelDepartment of Biomedical Engineering, University of Minnesota, 312 Church St. SE, Minneapolis, MN 55455, USA.
Anthony R BraunDepartment of Neuroscience, University of Minnesota, 321 Church St. SE, Minneapolis, MN 55455, USA.
Elizabeth RhoadesDepartment of Chemistry, University of Pennsylvania, 231 S 34th St., Philadelphia, PA 19104, USA.
Jonathan N SachsDepartment of Biomedical Engineering, University of Minnesota, 312 Church St. SE, Minneapolis, MN 55455, USA. Electronic address: jnsachs@umn.edu.

Funding

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

Abstract

We review experimental and simulation approaches that have been used to determine curvature generation and remodeling of lipid bilayers by membrane-bending proteins. Particular emphasis is placed on the complementary approaches used to study α-Synuclein (αSyn), a major protein involved in Parkinson's disease (PD). Recent cellular and biophysical experiments have shown that the protein 1) deforms the native structure of mitochondrial and model membranes; and 2) inhibits vesicular fusion. Today's advanced experimental and computational technology has made it possible to quantify these protein-induced changes in membrane shape and material properties. Collectively, experiments, theory and multi-scale simulation techniques have established the key physical determinants of membrane remodeling and rigidity: protein binding energy, protein partition depth, protein density, and membrane tension. Despite the exciting and significant progress made in recent years in these areas, challenges remain in connecting biophysical insights to the cellular processes that lead to disease. This article is part of a Special Issue entitled: Membrane Proteins edited by J.C. Gumbart and Sergei Noskov.

Indexed as

Molecular Dynamics Simulationalpha-SynucleinBinding SitesComputer SimulationLipid BilayersMembrane FluidityMembrane ProteinsModels, ChemicalProtein BindingProtein ConformationProtein Interaction Mappingalpha-SynucleinLipid BilayersMembrane ProteinsBilayer rigidityCoarse-grained molecular dynamics (CGMD)Membrane curvatureParkinson's diseaseSynaptic vesiclesTubulationα-Synuclein

Identifiers

PMID26972046
PMCPMC5081225

What Socratic 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 Socratic graph.