Evidence map›Paper›PMID 39488732›Full record

ArticleBiophysical journal2024

Evaluating the impact of the membrane thickness on the function of the intramembrane protease GlpG.

Oskar Engberg, Anjana V Mathath, Viola Döbel, Christian Frie, Marius K Lemberg, Debashree Chakraborty, Daniel Huster

Abstract read
In one paragraph

Article in Biophysical journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. The Evolution of Lipids from Solvents to Substrates.Annual review of biophysics · 2026
    Review
  4. Article
  5. Article
  6. 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

7 authors.

Oskar EngbergInstitute for Medical Physics and Biophysics, University of Leipzig, Leipzig, Germany.
Anjana V MathathBiophysical and Computational Chemistry Laboratory, Department of Chemistry, National Institute of Technology Karnataka, Mangalore, Karnataka, India.
Viola DöbelInstitute for Medical Physics and Biophysics, University of Leipzig, Leipzig, Germany.
Christian FrieCenter for Biochemistry and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne, Germany.
Marius K LembergCenter for Biochemistry and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne, Germany.
Debashree ChakrabortyBiophysical and Computational Chemistry Laboratory, Department of Chemistry, National Institute of Technology Karnataka, Mangalore, Karnataka, India.
Daniel HusterInstitute for Medical Physics and Biophysics, University of Leipzig, Leipzig, Germany. Electronic address: daniel.huster@medizin.uni-leipzig.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular membranes exhibit a huge diversity of lipids and membrane proteins that differ in their properties and chemical structure. Cells organize these molecules into distinct membrane compartments characterized by specific lipid profiles and hydrophobic thicknesses of the respective domains. If a hydrophobic mismatch occurs between a membrane protein and the surrounding lipids, there can be functional consequences such as reduced protein activity. This phenomenon has been extensively studied for single-pass transmembrane proteins, rhodopsin, and small polypeptides such as gramicidin. Here, we investigate the E. coli rhomboid intramembrane protease GlpG as a model to systematically explore the impact of membrane thickness on GlpG activity. We used fully saturated 1,2-dilauroyl-sn-glycero-3-phosphocholine (DLPC) and 1,2-dimyristoyl-sn-glycero-3-phosphocholine(DMPC) model lipids and altered membrane thickness by varying the cholesterol content. Physical membrane parameters were determined by

Indexed as

Cell MembraneEscherichia coli ProteinsCholesterolDimyristoylphosphatidylcholineDNA-Binding ProteinsEndopeptidasesEscherichia coliLipid BilayersMembrane ProteinsCholesterolDimyristoylphosphatidylcholineDNA-Binding ProteinsEndopeptidasesEscherichia coli ProteinsGlpG protein, E coliLipid BilayersMembrane Proteins

Identifiers

PMID39488732
PMCPMC11628809

What Socratic 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 Socratic graph.