ArticleNature2012
Structure of the agonist-bound neurotensin receptor.
Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 236 papers.
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.
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.
Who cites it
236 citing papers in PubMed, 494 citations in OpenAlex.
- First-in-human evaluation of [Annals of medicine · 2026Article
- Docking of virtual libraries identifies small-molecule agonists of neurotensin receptors with analgesic activity.Nature communications · 2026Article
- Amonafide Targeting NTSR1-PI3K/AKT/mTOR Signaling Attenuates Vascular Remodeling in Pulmonary Arterial Hypertension.Journal of the American Heart Association · 2026Article
- Article
- Stabilization versus flexibility: Detergent-dependent trade-offs in neurotensin receptor 1 GPCR ensembles.Protein science : a publication of the Protein Society · 2026Article
- Mapping the Ligand-dependent Remodeling of the Conformational Entropy Landscape in Neurotensin Receptor 1 by NMR-guided Molecular Simulations.bioRxiv : the preprint server for biology · 2026Article
- Advances in neurotensin receptor 1-targeted molecular probes for tumor molecular imaging and therapy.Frontiers in oncology · 2026Review
- RePol: A high-throughput screen for optimizing membrane protein solubilization and purification using polymers.Protein science : a publication of the Protein Society · 2026Article
- Structure-based design of macrocyclic peptides to generate functional antibodies against G protein-coupled receptors.Nature communications · 2025Article
- Stabilization versus flexibility: detergent-dependent trade-offs in neurotensin receptor 1 GPCR ensembles.bioRxiv : the preprint server for biology · 2025Article
- In Vivo Cytosolic Delivery of Biomolecules into Neurons for Super-Resolution Imaging and Genome Modification.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Article
- Evolutionary scenarios for the specific recognition of nonhomologous endogenous peptides by G protein-coupled receptor paralogs.The Journal of biological chemistry · 2025Article
- Re-evaluation of Cyclic Peptide Binding to Neurotensin Receptor 1 by Shifting the Peptide Register during Synthesis.ACS medicinal chemistry letters · 2025Article
- Unnatural Amino Acids: Strategies, Designs, and Applications in Medicinal Chemistry and Drug Discovery.Journal of medicinal chemistry · 2024Review
- Dually Labeled Neurotensin NTSJournal of medicinal chemistry · 2024Article
- Design, Synthesis, andACS pharmacology & translational science · 2024Article
- pJournal of chemical information and modeling · 2024Article
- Chelator boosted tumor-retention and pharmacokinetic properties: development ofEuropean journal of nuclear medicine and molecular imaging · 2024Article
- Structural basis of neuropeptide Y signaling through YMedComm · 2024Article
176 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
Abstract
Neurotensin (NTS) is a 13-amino-acid peptide that functions as both a neurotransmitter and a hormone through the activation of the neurotensin receptor NTSR1, a G-protein-coupled receptor (GPCR). In the brain, NTS modulates the activity of dopaminergic systems, opioid-independent analgesia, and the inhibition of food intake; in the gut, NTS regulates a range of digestive processes. Here we present the structure at 2.8 Å resolution of Rattus norvegicus NTSR1 in an active-like state, bound to NTS(8-13), the carboxy-terminal portion of NTS responsible for agonist-induced activation of the receptor. The peptide agonist binds to NTSR1 in an extended conformation nearly perpendicular to the membrane plane, with the C terminus oriented towards the receptor core. Our findings provide, to our knowledge, the first insight into the binding mode of a peptide agonist to a GPCR and may support the development of non-peptide ligands that could be useful in the treatment of neurological disorders, cancer and obesity.
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What OpenQuestion holds
Registered trials
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.