Evidence map›Paper›PMID 35769914›Full record

ArticleFrontiers in molecular biosciences2022

Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy.

Federico Baserga, Antreas Vorkas, Fucsia Crea, Luiz Schubert, Jheng-Liang Chen, Aoife Redlich, Mariafrancesca La Greca, Julian Storm, Sabine Oldemeyer, Kirsten Hoffmann and 2 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 40% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Polarized ATR-FTIR Spectroscopy Reveals Light-Induced Peptide Insertion of LAH4 Into Photoswitchable Membranes.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  2. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  3. Proton-Coupled Electron Transfer in Cytochrome c Oxidase: Heme a Controls the Protonation Dynamics of E286.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025
    Article
  4. 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

12 authors at 1 institution in 1 country.

Federico BasergaDepartment of Physics, Experimental Molecular Biophysics, Freie Universität Berlin, Berlin, Germany.
Antreas VorkasDepartment of Physics, Genetic Biophysics, Freie Universität Berlin, Berlin, Germany.
Fucsia CreaDepartment of Physics, Experimental Molecular Biophysics, Freie Universität Berlin, Berlin, Germany.
Luiz SchubertDepartment of Physics, Experimental Molecular Biophysics, Freie Universität Berlin, Berlin, Germany.
Jheng-Liang ChenDepartment of Physics, Genetic Biophysics, Freie Universität Berlin, Berlin, Germany.
Aoife RedlichDepartment of Physics, Experimental Molecular Biophysics, Freie Universität Berlin, Berlin, Germany.
Mariafrancesca La GrecaDepartment of Physics, Genetic Biophysics, Freie Universität Berlin, Berlin, Germany.
Julian StormDepartment of Physics, Genetic Biophysics, Freie Universität Berlin, Berlin, Germany.
Sabine OldemeyerDepartment of Physics, Experimental Molecular Biophysics, Freie Universität Berlin, Berlin, Germany.
Kirsten HoffmannDepartment of Physics, Genetic Biophysics, Freie Universität Berlin, Berlin, Germany.
Ramona SchlesingerDepartment of Physics, Genetic Biophysics, Freie Universität Berlin, Berlin, Germany.
Joachim HeberleDepartment of Physics, Experimental Molecular Biophysics, Freie Universität Berlin, Berlin, Germany.
Freie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is well known that lipids neighboring integral membrane proteins directly influence their function. The opposite effect is true as well, as membrane proteins undergo structural changes after activation and thus perturb the lipidic environment. Here, we studied the interaction between these molecular machines and the lipid bilayer by observing changes in the lipid vibrational bands

Indexed as

cytochrome c oxidasehydrogen bondinglateral pressurelipid-protein interactionphotoswitchable lipidsprotein structural changesrhodopsin

Identifiers

PMID35769914
PMCPMC9234331
OpenAlexW4282592213

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.