Evidence map›Paper›PMID 39479198›Full record

ArticleRSC applied interfaces2025

Metal ion cofactors modulate integral enzyme activity by varying differential membrane curvature stress.

Paulina Piller, Paul Reiterer, Enrico F Semeraro, Georg Pabst

Abstract read
In one paragraph

Article in RSC applied interfaces, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

4 authors.

Paulina PillerBiophysics, Institute of Molecular Biosciences, University of Graz NAWI Graz Graz Austria georg.pabst@uni-graz.at +43 316 380 4989.ORCID https://orcid.org/0000-0001-9063-5074
Paul ReitererBiophysics, Institute of Molecular Biosciences, University of Graz NAWI Graz Graz Austria georg.pabst@uni-graz.at +43 316 380 4989.
Enrico F SemeraroBiophysics, Institute of Molecular Biosciences, University of Graz NAWI Graz Graz Austria georg.pabst@uni-graz.at +43 316 380 4989.ORCID https://orcid.org/0000-0002-6096-1108
Georg PabstBiophysics, Institute of Molecular Biosciences, University of Graz NAWI Graz Graz Austria georg.pabst@uni-graz.at +43 316 380 4989.ORCID https://orcid.org/0000-0003-1967-1536

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metal ions are well-known cofactors of protein function and stability. In the case of the integral membrane enzyme OmpLA (outer membrane phospholipase A) the active dimer is stabilized by calcium ions. We studied the lipid hydrolysis kinetics of OmpLA in charge-neutral and charged membranes with symmetric or asymmetric transbilayer lipid distributions. In charge-neutral membranes, OmpLA was more active in symmetric bilayers due to the lower differential curvature stress between membrane leaflets. Strikingly, this behavior was completely reversed in charged bilayers. Measurements revealed intrinsic molecular shape changes in the charged lipids upon addition of calcium. This effectively reduces the differential curvature stress in charged asymmetric membranes leading to increased protein activity. This conclusion is further supported by similar effects observed upon the addition of sodium ions, which also alter the shape of the lipids, but do not specifically interact with the protein. Additional lipid-protein interactions likely contribute to this phenomenon. Our findings demonstrate that ion cofactors not only interact directly with membrane proteins but also modulate protein activity indirectly by altering the effective molecular shape of charged lipid species.

Identifiers

PMID39479198
PMCPMC11514723

What Socratic holds

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LicenceCC BY
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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 Socratic graph.