Evidence map›Paper›PMID 18658220›Full record

ArticleBiophysical journal2008

Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers.

Christian Löw, Ulrich Weininger, Hwankyu Lee, Kristian Schweimer, Ines Neundorf, Annette G Beck-Sickinger, Richard W Pastor, Jochen Balbach

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 56 citations in OpenAlex.

  1. Bend it like BIN1: how a membrane-curving adaptor protein shapes cardiac physiology.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  2. Article
  3. Dynamics of membrane tubulation coupled with fission by a two-component module.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Proton-Coupled Electron Transfer from Tyrosine in the Interior of aJournal of the American Chemical Society · 2020
    Article
  9. Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Modeling Protein-Micelle Systems in Implicit Water.The journal of physical chemistry. B · 2015
    Article
  17. Article
  18. Article
  19. Article
  20. 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

8 authors at 4 institutions in 2 countries.

Christian LöwInstitut für Physik, Biophysik, Martin-Luther-Universität Halle-Wittenberg, D-06120 Halle (Saale), Germany.
Ulrich Weininger
Hwankyu Lee
Kristian Schweimer
Ines Neundorf
Annette G Beck-Sickinger
Richard W Pastor
Jochen Balbach
Martin Luther University Halle-Wittenberg · DELeipzig University · DEUniversity of Bayreuth · DENational Heart Lung and Blood Institute · US

Funding

Computer Simulations of Membranes and BiopolymersZIAHL000340 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI PASTOR, RICHARD WALTER · 2009 to 2025
$29.1M
Computer Simulations of Membranes and BiopolymersZ01HL000340 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI PASTOR, RICHARD WALTER · 2006 to 2008
$2.9M
6 · The paper itself

Abstract

Bin/Amphiphysin/Rvs-homology (BAR) domains generate and sense membrane curvature by binding the negatively charged membrane to their positively charged concave surfaces. N-BAR domains contain an N-terminal extension (helix-0) predicted to form an amphipathic helix upon membrane binding. We determined the NMR structure and nano-to-picosecond dynamics of helix-0 of the human Bin1/Amphiphysin II BAR domain in sodium dodecyl sulfate and dodecylphosphocholine micelles. Molecular dynamics simulations of this 34-amino acid peptide revealed electrostatic and hydrophobic interactions with the detergent molecules that induce helical structure formation from residues 8-10 toward the C-terminus. The orientation in the micelles was experimentally confirmed by backbone amide proton exchange. The simulation and the experiment indicated that the N-terminal region is disordered, and the peptide curves to adopted the micelle shape. Deletion of helix-0 reduced tubulation of liposomes by the BAR domain, whereas the helix-0 peptide itself was fusogenic. These findings support models for membrane curving by BAR domains in which helix-0 increases the binding affinity to the membrane and enhances curvature generation.

Indexed as

MicellesAdaptor Proteins, Signal TransducingAmidesDetergentsHumansHydrophobic and Hydrophilic InteractionsLipid BilayersMagnetic Resonance SpectroscopyMembranesModels, MolecularNuclear ProteinsProtein Structure, SecondaryProtein Structure, TertiaryProtonsStatic ElectricityTime FactorsAdaptor Proteins, Signal TransducingAmidesBIN1 protein, humanDetergentsLipid BilayersMicellesNuclear ProteinsProtonsTumor Suppressor Proteins

Identifiers

PMID18658220
PMCPMC2567947
OpenAlexW2070259193

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.