ArticleStructure (London, England : 1993)2012
Conformational dynamics of activation for the pentameric complex of dimeric G protein-coupled receptor and heterotrimeric G protein.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 68 citations in OpenAlex.
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- Enabling simultaneous photoluminescence spectroscopy and X-ray footprinting mass spectrometry to study protein conformation and interactions.Analytical methods : advancing methods and applications · 2025Article
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- MEMBRANE PROTEIN STRUCTURES AND INTERACTIONS FROM COVALENT LABELING COUPLED WITH MASS SPECTROMETRY.Mass spectrometry reviews · 2022Review
- Nanoparticles and photochemistry for native-like transmembrane protein footprinting.Nature communications · 2021Article
- Diethylpyrocarbonate Footprints a Membrane Protein in Micelles.Journal of the American Society for Mass Spectrometry · 2021Article
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
- Protein Footprinting: Auxiliary Engine to Power the Structural Biology Revolution.Journal of molecular biology · 2020Review
- Development of Container Free Sample Exposure for Synchrotron X-ray Footprinting.Analytical chemistry · 2020Article
- Assembly of a GPCR-G Protein Complex.Cell · 2019Article
- Using X-ray Footprinting and Mass Spectrometry to Study the Structure and Function of Membrane Proteins.Protein and peptide letters · 2019Review
- Recent advances in computational studies of GPCR-G protein interactions.Advances in protein chemistry and structural biology · 2019Review
- Article
- Structural basis of ligand interaction with atypical chemokine receptor 3.Nature communications · 2017Article
- Conformational insight into multi-protein signaling assemblies by hydrogen-deuterium exchange mass spectrometry.Current opinion in structural biology · 2016Review
- Instant Integrated Ultradeep Quantitative-structural Membrane Proteomics Discovered Post-translational Modification Signatures for Human Cys-loop Receptor Subunit Bias.Molecular & cellular proteomics : MCP · 2016Article
- Dynamic peptides of human TPP1 fulfill diverse functions in telomere maintenance.Nucleic acids research · 2016Article
- Synchrotron X-ray footprinting as a method to visualize water in proteins.Journal of synchrotron radiation · 2016Article
- Cross-linking and other structural proteomics techniques: how chemistry is enabling mass spectrometry applications in structural biology.Chemical science · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Photoactivation of rhodopsin (Rho), a G protein-coupled receptor, causes conformational changes that provide a specific binding site for the rod G protein, G(t). In this work we employed structural mass spectrometry techniques to elucidate the structural changes accompanying transition of ground state Rho to photoactivated Rho (Rho(∗)) and in the pentameric complex between dimeric Rho(∗) and heterotrimeric G(t). Observed differences in hydroxyl radical labeling and deuterium uptake between Rho(∗) and the (Rho(∗))(2)-G(t) complex suggest that photoactivation causes structural relaxation of Rho following its initial tightening upon G(t) coupling. In contrast, nucleotide-free G(t) in the complex is significantly more accessible to deuterium uptake allowing it to accept GTP and mediating complex dissociation. Thus, we provide direct evidence that in the critical step of signal amplification, Rho(∗) and G(t) exhibit dissimilar conformational changes when they are coupled in the (Rho(∗))(2)-G(t) complex.
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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.