Evidence map›Paper›PMID 38195620›Full record

ArticleScientific reports2024

Kinetic study of membrane protein interactions: from three to two dimensions.

Vladimir Adrien, Myriam Reffay, Nicolas Taulier, Alice Verchère, Laura Monlezun, Martin Picard, Arnaud Ducruix, Isabelle Broutin, Frédéric Pincet, Wladimir Urbach

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.3field-weighted citation impact, top 25% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 2 countries.

Vladimir Adrien *Laboratoire de Physique de l'École normale superieure, École Normale Supérieure, Université Paris Sciences et Lettres, CNRS, Sorbonne Université, Université Paris Cité, F-75005, Paris, France. vladimir.adrien@aphp.fr.
Myriam Reffay *Laboratoire Matière et Systèmes Complexes, UMR 7057, CNRS and Université de Paris Cité, 75205, Paris Cedex 13, France.
Nicolas TaulierSorbonne Université, CNRS, INSERM, Laboratoire d'Imagerie Biomédicale-LIB, 75006, Paris, France.
Alice VerchèreLaboratoire CiTCoM, Faculté de Santé, Université Paris Cité, CNRS, 75006, Paris, France.
Laura MonlezunUniversité Paris Cité, CNRS, Expression Génétique Microbienne, Institut de Biologie Physico-Chimique, Paris, France.
Martin PicardUniversité Paris Cité, Laboratoire de Biologie Physico-Chimique des Protéines Membranaires CNRS UMR7099, 75005, Paris, France.
Arnaud DucruixLaboratoire CiTCoM, Faculté de Santé, Université Paris Cité, CNRS, 75006, Paris, France.
Isabelle BroutinLaboratoire CiTCoM, Faculté de Santé, Université Paris Cité, CNRS, 75006, Paris, France.
Frédéric PincetLaboratoire de Physique de l'École normale superieure, École Normale Supérieure, Université Paris Sciences et Lettres, CNRS, Sorbonne Université, Université Paris Cité, F-75005, Paris, France. frederic.pincet@ens.fr.
Wladimir UrbachLaboratoire de Physique de l'École normale superieure, École Normale Supérieure, Université Paris Sciences et Lettres, CNRS, Sorbonne Université, Université Paris Cité, F-75005, Paris, France. urbach@lps.ens.fr.
Centre National de la Recherche Scientifique · FRUniversité Paris Cité · FRInstitut de Biologie Physico-Chimique · FRSorbonne Paris Cité · FRSorbonne Université · FR

Funding

National Science Foundation DMR-0944772
6 · The paper itself

Abstract

Molecular interactions are contingent upon the system's dimensionality. Notably, comprehending the impact of dimensionality on protein-protein interactions holds paramount importance in foreseeing protein behaviour across diverse scenarios, encompassing both solution and membrane environments. Here, we unravel interactions among membrane proteins across various dimensionalities by quantifying their binding rates through fluorescence recovery experiments. Our findings are presented through the examination of two protein systems: streptavidin-biotin and a protein complex constituting a bacterial efflux pump. We present here an original approach for gauging a two-dimensional binding constant between membrane proteins embedded in two opposite membranes. The quotient of protein binding rates in solution and on the membrane represents a metric denoting the exploration distance of the interacting sites-a novel interpretation.

Indexed as

BiotinMembrane ProteinsFluorescenceKineticsStreptavidinBiotinMembrane ProteinsStreptavidin

Identifiers

PMID38195620
PMCPMC10776792
OpenAlexW4390781731

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.