Evidence map›Paper›PMID 30054032›Full record

ArticleBiophysical journal2018

Supramolecular Organization of Apolipoprotein-A-I-Derived Peptides within Disc-like Arrangements.

Evgeniy S Salnikov, G M Anantharamaiah, Burkhard Bechinger

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Molecular Mechanisms Governing Peptide Nanodisc Assembly and Stability.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. The hydrodynamic motion of Nanodiscs.Chemistry and physics of lipids · 2019
    Article
  10. Article
  11. 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

3 authors at 2 institutions in 2 countries.

Evgeniy S SalnikovDepartment of Chemistry, University of Strasbourg, Strasbourg, France.
G M AnantharamaiahUniversity of Alabama at Birmingham, Birmingham, Alabama.
Burkhard BechingerDepartment of Chemistry, University of Strasbourg, Strasbourg, France. Electronic address: bechinger@unistra.fr.
Université de Strasbourg · FRUniversity of Alabama at Birmingham · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apolipoprotein A-I is the major protein component of high-density lipoproteins and fulfils important functions in lipid metabolism. Its structure consists of a chain of tandem domains of amphipathic helices. Using this protein as a template membrane scaffolding protein, class A amphipathic helical peptides were designed to support the amphipathic helix theory and later as therapeutic tools in biomedicine. Here, we investigated the lipid interactions of two apolipoprotein-A-I-derived class A amphipathic peptides, 14A (Ac-DYLKA FYDKL KEAF-NH

Indexed as

Amino Acid SequenceApolipoprotein A-IMagnetic Resonance SpectroscopyModels, MolecularPeptide FragmentsProtein ConformationApolipoprotein A-IPeptide Fragments

Identifiers

PMID30054032
PMCPMC6085177
OpenAlexW2840068146

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.