ArticleStructure (London, England : 1993)2020
A Conserved Proline Hinge Mediates Helix Dynamics and Activation of Rhodopsin.
Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters.Chemical reviews · 2026Review
- Article
- Distinguishing Different Hydrogen-Bonded Helices in Proteins by EfficientBiochemistry · 2024Article
- Illuminating GPCR signaling mechanisms by NMR spectroscopy with stable-isotope labeled receptors.Current opinion in pharmacology · 2023Review
- Article
- Article
- Magic angle spinning NMR of G protein-coupled receptors.Progress in nuclear magnetic resonance spectroscopy · 2022Review
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Deconstructing the transmembrane core of class A G protein-coupled receptors.Trends in biochemical sciences · 2021Review
- Residue 6.43 defines receptor function in class F GPCRs.Nature communications · 2021Article
- The Dynamics of the Neuropeptide Y Receptor Type 1 Investigated by Solid-State NMR and Molecular Dynamics Simulation.Molecules (Basel, Switzerland) · 2020Article
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Despite high-resolution crystal structures of both inactive and active G protein-coupled receptors (GPCRs), it is still not known how ligands trigger the large structural change on the intracellular side of the receptor since the conformational changes that occur within the extracellular ligand-binding region upon activation are subtle. Here, we use solid-state NMR and Fourier transform infrared spectroscopy on rhodopsin to show that Trp265
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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.