Evidence map›Paper›PMID 39215029›Full record

ArticleNature communications2024

Lipid-polymer nanoparticles to probe the native-like environment of intramembrane rhomboid protease GlpG and its activity.

Henry Sawczyc, Takashi Tatsuta, Carl Öster, Spyridon Kosteletos, Sascha Lange, Claudia Bohg, Thomas Langer, Adam Lange

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Liposome-Based Interventions in Knee Osteoarthritis.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Review
  6. Article
  7. 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

8 authors.

Henry SawczycResearch Unit Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125, Berlin, Germany.ORCID 0000-0001-9883-0405
Takashi TatsutaMax-Planck-Institute for Biology of Ageing, Department of Mitochondrial Proteostasis, Joseph-Stelzmann-Str. 9b, 50931, Cologne, Germany.ORCID 0000-0003-0003-0587
Carl ÖsterResearch Unit Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125, Berlin, Germany.
Spyridon KosteletosResearch Unit Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125, Berlin, Germany.ORCID 0009-0005-5798-309X
Sascha LangeResearch Unit Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125, Berlin, Germany.
Claudia BohgResearch Unit Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125, Berlin, Germany.ORCID 0000-0003-0793-3199
Thomas LangerMax-Planck-Institute for Biology of Ageing, Department of Mitochondrial Proteostasis, Joseph-Stelzmann-Str. 9b, 50931, Cologne, Germany.ORCID 0000-0003-1250-1462
Adam LangeResearch Unit Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125, Berlin, Germany. alange@fmp-berlin.de.ORCID 0000-0002-7534-5973

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) EXC 2008/1 (UniSysCat)-390540038
6 · The paper itself

Abstract

Polymers can facilitate detergent-free extraction of membrane proteins into nanodiscs (e.g., SMALPs, DIBMALPs), incorporating both integral membrane proteins as well as co-extracted native membrane lipids. Lipid-only SMALPs and DIBMALPs have been shown to possess a unique property; the ability to exchange lipids through 'collisional lipid mixing'. Here we expand upon this mixing to include protein-containing DIBMALPs, using the rhomboid protease GlpG. Through lipidomic analysis before and after incubation with DMPC or POPC DIBMALPs, we show that lipids are rapidly exchanged between protein and lipid-only DIBMALPs, and can be used to identify bound or associated lipids through 'washing-in' exogenous lipids. Additionally, through the requirement of rhomboid proteases to cleave intramembrane substrates, we show that this mixing can be performed for two protein-containing DIBMALP populations, assessing the native function of intramembrane proteolysis and demonstrating that this mixing has no deleterious effects on protein stability or structure.

Indexed as

EndopeptidasesEscherichia coli ProteinsMembrane ProteinsNanoparticlesDimyristoylphosphatidylcholineDNA-Binding ProteinsLipidomicsMembrane LipidsPhosphatidylcholinesPolymersProteolysis1-palmitoyl-2-oleoylphosphatidylcholineDimyristoylphosphatidylcholineDNA-Binding ProteinsEndopeptidasesEscherichia coli ProteinsGlpG protein, E coliMembrane LipidsMembrane ProteinsPhosphatidylcholinesPolymers

Identifiers

PMID39215029
PMCPMC11364529

What OpenQuestion holds

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Registered trials

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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.