Evidence map›Paper›PMID 41581885›Full record

ArticleThe Journal of biological chemistry2026

A new functional assay reveals that membrane binding is critical for overactivation of the phosphoinositide 3-kinase H1047R mutant.

Alexandra Papafotika, Maria Pavlaki, Vasiliki Lazani, Vasiliki Elpida Karamani, Dimitris Aggelidis, Anna Kapella, Danai Maria Kotzampasi, Bogos Agianian, Argiris Efstratiadis, Zoe Cournia and 1 more

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Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Alexandra PapafotikaBiomedical Research Institute, Foundation for Research and Technology, Ioannina, Greece; Laboratory of Biological Chemistry, Department of Medicine, School of Health Sciences, University of Ioannina, Ioannina, Greece.
Maria PavlakiDepartment of Molecular Biology and Genetics, Democritus University of Thrace, Alexandroupolis, Greece.
Vasiliki LazaniBiomedical Research Institute, Foundation for Research and Technology, Ioannina, Greece; Laboratory of Biological Chemistry, Department of Medicine, School of Health Sciences, University of Ioannina, Ioannina, Greece.
Vasiliki Elpida KaramaniBiomedical Research Institute, Foundation for Research and Technology, Ioannina, Greece; Laboratory of Biological Chemistry, Department of Medicine, School of Health Sciences, University of Ioannina, Ioannina, Greece.
Dimitris AggelidisBiomedical Research Institute, Foundation for Research and Technology, Ioannina, Greece; Laboratory of Biological Chemistry, Department of Medicine, School of Health Sciences, University of Ioannina, Ioannina, Greece.
Anna KapellaBiomedical Research Foundation, Academy of Athens, Athens, Greece.
Danai Maria KotzampasiBiomedical Research Foundation, Academy of Athens, Athens, Greece; Department of Biology, University of Crete, Heraklion, Greece.
Bogos AgianianDepartment of Molecular Biology and Genetics, Democritus University of Thrace, Alexandroupolis, Greece; Department of Biochemistry and Department of Medicine, Albert Einstein Cancer Center, Albert Einstein College of Medicine, Bronx, New York, USA.
Argiris EfstratiadisBiomedical Research Foundation, Academy of Athens, Athens, Greece.
Zoe CourniaBiomedical Research Foundation, Academy of Athens, Athens, Greece.
Savvas ChristoforidisBiomedical Research Institute, Foundation for Research and Technology, Ioannina, Greece; Laboratory of Biological Chemistry, Department of Medicine, School of Health Sciences, University of Ioannina, Ioannina, Greece. Electronic address: savvas_christoforidis@bri.forth.gr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PIK3CA encodes the catalytic subunit of class I PI3Kα (p110α), a key enzyme in receptor-mediated signaling that phosphorylates phosphatidylinositol-4,5-bisphosphate to the 3,4,5-triphosphate lipid. This gene is frequently mutated in cancers, with H1047R and E545K being the most prevalent mutations. However, the mechanisms of mutants' overactivation remain incompletely understood. Here, we report the development of a PI3Kα activity assay using reconstituted liposomes, which we employed to address the role of lipid membranes on mutant overactivation. The assay was validated by assessing typical enzymatic features and by confirming the IC

Indexed as

Cell MembraneClass I Phosphatidylinositol 3-KinasesPhosphatidylinositol 3-KinasesHumansLiposomesMolecular Dynamics SimulationMutationClass I Phosphatidylinositol 3-KinasesLiposomesPhosphatidylinositol 3-KinasesPIK3CA protein, humanassay developmentcancerenzymatic activityenzyme mutationlipid–protein interactionsliposomeMD simulationsmutant overactivationoncogenePI3Kinase

Identifiers

PMID41581885
PMCPMC12934285

What Socratic holds

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LicenceCC BY
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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.