Evidence map›Paper›PMID 27926846›Full record

ArticleBiophysical journal2016

Alamethicin Supramolecular Organization in Lipid Membranes from

Evgeniy S Salnikov, Jesus Raya, Marta De Zotti, Ekaterina Zaitseva, Cristina Peggion, Gema Ballano, Claudio Toniolo, Jan Raap, Burkhard Bechinger

Abstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Membrane Topology and Oligomerization of Peptaibols by Solid-State NMR Spectroscopy.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Antimicrobial Peptides: A Potent Alternative to Antibiotics.Antibiotics (Basel, Switzerland) · 2021
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Accelerated Molecular Dynamics Applied to the Peptaibol Folding Problem.International journal of molecular sciences · 2019
    Article
  11. Article
  12. Review
  13. Fast Magic-Angle-SpinningThe journal of physical chemistry. B · 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

9 authors.

Evgeniy S SalnikovInstitute of Chemistry, University of Strasbourg/CNRS, UMR7177, Strasbourg, France.
Jesus RayaInstitute of Chemistry, University of Strasbourg/CNRS, UMR7177, Strasbourg, France.
Marta De ZottiICB, Padova Unit, CNR, Department of Chemistry, University of Padova, Padova, Italy.
Ekaterina ZaitsevaDepartment of Membrane Physiology and Technology, Institute of Physiology, University of Freiburg, Freiburg, Germany.
Cristina PeggionICB, Padova Unit, CNR, Department of Chemistry, University of Padova, Padova, Italy.
Gema BallanoICB, Padova Unit, CNR, Department of Chemistry, University of Padova, Padova, Italy.
Claudio TonioloICB, Padova Unit, CNR, Department of Chemistry, University of Padova, Padova, Italy.
Jan RaapLeiden Institute of Chemistry, Gorlaeus Laboratories, University of Leiden, Leiden, the Netherlands.
Burkhard BechingerInstitute of Chemistry, University of Strasbourg/CNRS, UMR7177, Strasbourg, France. Electronic address: bechinge@unistra.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alamethicins (ALMs) are antimicrobial peptides of fungal origin. Their sequences are rich in hydrophobic amino acids and strongly interact with lipid membranes, where they cause a well-defined increase in conductivity. Therefore, the peptides are thought to form transmembrane helical bundles in which the more hydrophilic residues line a water-filled pore. Whereas the peptide has been well characterized in terms of secondary structure, membrane topology, and interactions, much fewer data are available regarding the quaternary arrangement of the helices within lipid bilayers. A new, to our knowledge, fluorine-labeled ALM derivative was prepared and characterized when reconstituted into phospholipid bilayers. As a part of these studies, C

Indexed as

AlamethicinAmino Acid SequenceAnti-Bacterial AgentsCell MembraneElectrophysiological PhenomenaMagnetic Resonance SpectroscopyPhosphatidylcholinesProtein Multimerization1-palmitoyl-2-oleoylphosphatidylcholineAlamethicinAnti-Bacterial AgentsPhosphatidylcholines

Identifiers

PMID27926846
PMCPMC5153535

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.