Evidence map›Paper›PMID 38071229›Full record

ArticleNature communications2023

Unravelling the mechanism of neurotensin recognition by neurotensin receptor 1.

Kazem Asadollahi, Sunnia Rajput, Lazarus Andrew de Zhang, Ching-Seng Ang, Shuai Nie, Nicholas A Williamson, Michael D W Griffin, Ross A D Bathgate, Daniel J Scott, Thomas R Weikl and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. 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. Article
  5. Binding memory of liquid molecules.Nature communications · 2025
    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

12 authors at 2 institutions in 2 countries.

Kazem AsadollahiDepartment of Biochemistry and Pharmacology, University of Melbourne, Parkville, VIC, 3010, Australia.ORCID 0000-0002-7811-2964
Sunnia RajputBio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.
Lazarus Andrew de ZhangThe Florey, University of Melbourne, Parkville, VIC, 3010, Australia.
Ching-Seng AngBio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.
Shuai NieBio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.
Nicholas A WilliamsonBio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.ORCID 0000-0002-2173-3452
Michael D W GriffinDepartment of Biochemistry and Pharmacology, University of Melbourne, Parkville, VIC, 3010, Australia.ORCID 0000-0001-9845-7735
Ross A D BathgateDepartment of Biochemistry and Pharmacology, University of Melbourne, Parkville, VIC, 3010, Australia.ORCID 0000-0001-6301-861X
Daniel J ScottDepartment of Biochemistry and Pharmacology, University of Melbourne, Parkville, VIC, 3010, Australia.ORCID 0000-0001-6332-2793
Thomas R WeiklDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14476, Potsdam, Germany.ORCID 0000-0002-0911-5328
Guy N L JamesonBio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.ORCID 0000-0001-9416-699X
Paul R GooleyDepartment of Biochemistry and Pharmacology, University of Melbourne, Parkville, VIC, 3010, Australia. prg@unimelb.edu.au.ORCID 0000-0002-0323-449X
The University of Melbourne · AUMax Planck Institute of Colloids and Interfaces · DE

Funding

Department of Health | National Health and Medical Research Council (NHMRC) 1081844Department of Health | National Health and Medical Research Council (NHMRC) 1141034
6 · The paper itself

Abstract

The conformational ensembles of G protein-coupled receptors (GPCRs) include inactive and active states. Spectroscopy techniques, including NMR, show that agonists, antagonists and other ligands shift the ensemble toward specific states depending on the pharmacological efficacy of the ligand. How receptors recognize ligands and the kinetic mechanism underlying this population shift is poorly understood. Here, we investigate the kinetic mechanism of neurotensin recognition by neurotensin receptor 1 (NTS

Indexed as

NeurotensinReceptors, NeurotensinLigandsProtein BindingReceptors, G-Protein-CoupledLigandsNeurotensinReceptors, G-Protein-CoupledReceptors, Neurotensin

Identifiers

PMID38071229
PMCPMC10710507
OpenAlexW4389509341

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.