ArticleNature communications2021
Activation pathway of a G protein-coupled receptor uncovers conformational intermediates as targets for allosteric drug design.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.
What it found
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Who cites it
113 citing papers in PubMed, 219 citations in OpenAlex.
- Structural insights on the ligand selectivity of the mouse trace amine-associated receptor TAAR7e.iScience · 2026Article
- Cryptic pockets in proteins: Harnessing conformational dynamics for rational drug design.Acta pharmaceutica Sinica. B · 2026Article
- Molecular architecture of OXGR1 reveals an evolutionary conserved mechanisms for metabolite surveillance.The EMBO journal · 2026Article
- Resurrecting Full-Length Ancestral Schizorhodopsins and Heliorhodopsins with Structure-Guided, Indel-Aware Sequence Reconstruction.ACS omega · 2026Article
- Berberine Ameliorates Angiotensin II-Induced Endothelial Dysfunction by Blocking AT1R, Inhibiting PDE4b and Activating AKT/eNOS Pathway.Chinese journal of integrative medicine · 2026Article
- Mechanistic basis of N-terminal domain-mediated allostery in SIRT6: integrating molecular dynamics simulations and biochemical assays.Molecular diversity · 2026Article
- Rational design of a Kappa opioid receptor peptide agonist with attenuated β-arrestin signaling.Nature communications · 2026Article
- Macrocyclic and Hydroxamate Ligands forInorganic chemistry · 2026Article
- Assessing the Performance of BioEmu in Understanding Protein Dynamics.International journal of molecular sciences · 2026Article
- From empirical screening to lipid trolling: the evolution of extrahelical allosteric modulators of AMedicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026Review
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- Sequence constraints predispose Class D GPCRs to follow an atypical activation mechanism.bioRxiv : the preprint server for biology · 2026Article
- All roads lead to Rome: Emergence of Mechanistic Divergence Shapes Activation of Class B1 G-Protein Coupled Receptors.bioRxiv : the preprint server for biology · 2026Article
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- Selective modulation of orexinergic receptors by neem-derived phytochemicals: Computational analysis of structure-activity relationships.Toxicology reports · 2025Article
- An update for AlphaFold3 versus experimental structures: assessing the precision of small molecule binding in GPCRs.Acta pharmacologica Sinica · 2025Article
- Exploring the distinct activation mechanisms of neuromedin B receptor through multiple replica molecular dynamics simulations and Markov state modeling.Acta pharmacologica Sinica · 2025Article
- AI-Integrated QSAR Modeling for Enhanced Drug Discovery: From Classical Approaches to Deep Learning and Structural Insight.International journal of molecular sciences · 2025Review
- Evaluation of Small-Molecule Binding Site Prediction Methods on Membrane-Embedded Protein Interfaces.Journal of chemical information and modeling · 2025Article
53 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G protein-coupled receptors (GPCRs) are the most common proteins targeted by approved drugs. A complete mechanistic elucidation of large-scale conformational transitions underlying the activation mechanisms of GPCRs is of critical importance for therapeutic drug development. Here, we apply a combined computational and experimental framework integrating extensive molecular dynamics simulations, Markov state models, site-directed mutagenesis, and conformational biosensors to investigate the conformational landscape of the angiotensin II (AngII) type 1 receptor (AT
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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.