Evidence map›Paper›PMID 41108533›Full record

ReviewBioEssays : news and reviews in molecular, cellular and developmental biology2025

The Allosteric Mechanism of G-Protein-Coupled Receptors is Induced Fit, Not Conformational Selection.

Kazem Asadollahi, Paul R Gooley, Thomas R Weikl

Abstract readReview
In one paragraph

Review in BioEssays : news and reviews in molecular, cellular and developmental biology, 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. The Allosteric Mechanism of G-Protein-Coupled Receptors is Induced Fit, Not Conformational Selection.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    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

3 authors.

Kazem AsadollahiDepartment of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Paul R GooleyDepartment of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Thomas R WeiklDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam, Germany.ORCID https://orcid.org/0000-0002-0911-5328

Funding

Max-Planck-Gesellschaft
6 · The paper itself

Abstract

The allosteric mechanism of G-protein-coupled receptors (GPCRs) involves a population shift from inactive to active receptor conformations in response to the binding of ligand agonists. Two possible kinetic mechanisms for this population shift are induced fit and conformational selection. In the induced-fit mechanism, ligands bind to inactive receptor conformations prior to the conformational transition of the receptor. In the conformational-selection mechanism, ligands bind to active conformations after the conformational transition. For the peptide-activated neurotensin receptor 1, stopped-flow mixing experiments that probe the chemical relaxation into binding equilibrium and conformational transition rates measured with NMR experiments indicate an induced-fit mechanism. For the small-molecule-activated

Indexed as

Receptors, G-Protein-CoupledAllosteric RegulationAnimalsHumansKineticsLigandsProtein BindingProtein ConformationReceptors, NeurotensinLigandsneurotensin type 1 receptorReceptors, G-Protein-CoupledReceptors, Neurotensinbinding kineticsconformational changesG‐protein‐coupled receptorsprotein allosterystopped‐flow mixing experiments

Identifiers

PMID41108533
PMCPMC12632437

What OpenQuestion 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 OpenQuestion graph.