ArticleBiochemistry2010
Electron paramagnetic resonance studies of functionally active, nitroxide spin-labeled peptide analogues of the C-terminus of a G-protein alpha subunit.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 27 citations in OpenAlex.
- A highly dynamic active state for transducin-bound phosphodiesterase-6 in vertebrate phototransduction.bioRxiv : the preprint server for biology · 2026Article
- A rapid, tag-free way to purify functional GPCRs.The Journal of biological chemistry · 2024Article
- Is Cys(MTSL) the Best α-Amino Acid Residue to Electron Spin Labeling of Synthetically Accessible Peptide Molecules with Nitroxides?ACS omega · 2022Article
- Novel fluorescent GPCR biosensor detects retinal equilibrium binding to opsin and active G protein and arrestin signaling conformations.The Journal of biological chemistry · 2020Article
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
- Conformational equilibria of light-activated rhodopsin in nanodiscs.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Conformational selection and equilibrium governs the ability of retinals to bind opsin.The Journal of biological chemistry · 2015Article
- Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin binding.Biochemistry · 2014Article
- Molecular basis of cannabinoid CB1 receptor coupling to the G protein heterotrimer Gαiβγ: identification of key CB1 contacts with the C-terminal helix α5 of Gαi.The Journal of biological chemistry · 2013Article
- Structure and dynamics of an imidazoline nitroxide side chain with strongly hindered internal motion in proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
- Molecular dynamics of β-hairpin models of epigenetic recognition motifs.Journal of the American Chemical Society · 2012Article
- Mapping molecular flexibility of proteins with site-directed spin labeling: a case study of myoglobin.Biochemistry · 2012Article
- The spin label amino acid TOAC and its uses in studies of peptides: chemical, physicochemical, spectroscopic, and conformational aspects.Biophysical reviews · 2012Article
- Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Signal protein-derived peptides as functional probes and regulators of intracellular signaling.Journal of amino acids · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The C-terminal tail of the transducin alpha subunit, Gtalpha(340-350), is known to bind and stabilize the active conformation of rhodopsin upon photoactivation (R*). Five spin-labeled analogues of Gtalpha(340-350) demonstrated native-like activity in their ability to bind and stabilize R*. The spin-label 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid (TOAC) was employed at interior sites within the peptide, whereas a Proxyl (3-carboxyl-2,2,5,5-tetramethyl-pyrrolidinyloxy) spin-label was employed at the amino terminus of the peptide. Upon binding to R*, the electron paramagnetic resonance spectrum of TOAC(343)-Gtalpha(340-350) revealed greater immobilization of the nitroxide when compared to that of the N-terminally modified Proxyl-Gtalpha(340-350) analogue. A doubly labeled Proxyl/TOAC(348)-Gtalpha(340-350) was examined by DEER spectrocopy to determine the distribution of distances between the two nitroxides in the peptides when in solution and when bound to R*. TOAC and Proxyl spin-labels in this GPCR-G-protein alpha-peptide system provide unique biophysical probes that can be used to explore the structure and conformational changes at the rhodopsin-G-protein interface.
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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.