Evidence map›Paper›PMID 42888484›Full record

ReviewJournal of peptide science : an official publication of the European Peptide Society2026

Membrane Topology and Oligomerization of Peptaibols by Solid-State NMR Spectroscopy.

Burkhard Bechinger, Evgeniy S Salnikov

Abstract readReview
In one paragraph

Review in Journal of peptide science : an official publication of the European Peptide Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Burkhard BechingerUMR7177, Institut de Chimie, University of Strasbourg/CNRS, Strasbourg, France.ORCID https://orcid.org/0000-0001-5719-6073
Evgeniy S SalnikovUMR7177, Institut de Chimie, University of Strasbourg/CNRS, Strasbourg, France.ORCID https://orcid.org/0000-0001-5843-4125

Funding

Agence Nationale de la Recherche AMLAA 21-CE11-0038-02Agence Nationale de la Recherche AmphiPep 20-CE18-0021Agence Nationale de la Recherche ANR-10-IDEX-0002Agence Nationale de la Recherche Biosupramol 17-CE18-0033-3Agence Nationale de la Recherche Naturalarsenal 19-AMRB-0004-02Agence Nationale de la Recherche SAFEST 21-CE18-0043Centre National de la Recherche Scientifiquecofecub 88881.879071/2023-01Conseil régional du Grand EstIndo-French Centre for the Promotion of Advanced Research 62T10-1Université de Strasbourg
6 · The paper itself

Abstract

Here, we review solid-state NMR investigations of a variety of peptaibols in phospholipid bilayer environments. The peptides were prepared using different approaches such as microbial expression, solid-phase peptide synthesis or the chemical synthesis in solution and a modular fragment condensation approach. Importantly, the techniques allowed the preparation of peptaibols labelled with

Indexed as

Lipid BilayersPeptaibolsAlamethicinNuclear Magnetic Resonance, BiomolecularAlamethicinLipid BilayersPeptaibolschannel formationhydrophobic mismatchmembrane alignmentoligomer sizesolid‐state NMRsupported lipid bilayerstransmembrane anchor

Identifiers

PMID42888484
PMCPMC13675502

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.