ArticleFEBS letters2007
Interaction of a fragment of the cannabinoid CB1 receptor C-terminus with arrestin-2.
Article in FEBS letters, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.
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
23 citing papers in PubMed, 1 synthesis or guideline pooled it, 35 citations in OpenAlex.
- Cannabinoid Receptors: An Update on Cell Signaling, Pathophysiological Roles and Therapeutic Opportunities in Neurological, Cardiovascular, and Inflammatory Diseases.International journal of molecular sciences · 2020Pooled it
- SGIP1 in axons prevents internalization of desensitized CB1R and modifies its function.Frontiers in neuroscience · 2023Review
- Design and validation of recombinant protein standards for quantitative Western blot analysis of cannabinoid CBMicrobial cell factories · 2022Article
- SGIP1 modulates kinetics and interactions of the cannabinoid receptor 1 and G protein-coupled receptor kinase 3 signalosome.Journal of neurochemistry · 2022Article
- Cannabinoid Receptor Interacting Protein 1a (CRIP1a) in Health and Disease.Biomolecules · 2020Review
- Assessment of Biased Agonism among Distinct Synthetic Cannabinoid Receptor Agonist Scaffolds.ACS pharmacology & translational science · 2020Article
- Protein Interactors and Trafficking Pathways That Regulate the Cannabinoid Type 1 Receptor (CB1R).Frontiers in molecular neuroscience · 2020Review
- Molecular Interaction between Distal C-Terminal Domain of the CBJournal of chemical information and modeling · 2019Article
- Cannabinoid Receptor Interacting Protein 1a (CRIP1a): Function and Structure.Molecules (Basel, Switzerland) · 2019Review
- Structural Insights into CB1 Receptor Biased Signaling.International journal of molecular sciences · 2019Review
- Cannabinoid CB1 and CB2 Receptor-Mediated Arrestin Translocation: Species, Subtype, and Agonist-Dependence.Frontiers in pharmacology · 2019Article
- Cannabinoid Receptor Interacting Protein 1a Competition with β-Arrestin for CB1 Receptor Binding Sites.Molecular pharmacology · 2017Article
- Cannabinoid CBCannabis and cannabinoid research · 2017Review
- Computational analysis of the CB1 carboxyl-terminus in the receptor-G protein complex.Proteins · 2016Article
- Cannabinoid receptor-interacting protein 1a modulates CB1 receptor signaling and regulation.Molecular pharmacology · 2015Article
- Type 1 cannabinoid receptor ligands display functional selectivity in a cell culture model of striatal medium spiny projection neurons.The Journal of biological chemistry · 2014Article
- Delineation of domains within the cannabinoid CB1 and dopamine D2 receptors that mediate the formation of the heterodimer complex.Journal of molecular neuroscience : MN · 2014Article
- The cannabinoid type-1 receptor carboxyl-terminus, more than just a tail.Journal of neurochemistry · 2011Review
- Binding between a distal C-terminus fragment of cannabinoid receptor 1 and arrestin-2.Biochemistry · 2011Article
- Cannabinoid CB1 receptor-interacting proteins: novel targets for central nervous system drug discovery?British journal of pharmacology · 2010Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Desensitization of the cannabinoid CB1 receptor is mediated by the interaction with arrestin. In this study, we report the structural changes of a synthetic diphosphorylated peptide corresponding to residues 419-439 of the CB1 C-terminus upon binding to arrestin-2. This segment is pivotal to the desensitization of CB1. Using high-resolution proton NMR, we observe two helical segments in the bound peptide that are separated by the presence a glycine residue. The binding we observe is with a diphoshorylated peptide, whereas a previous study reported binding of a highly phosphorylated rhodopsin fragment to visual arrestin. The arrestin bound conformations of the peptides are compared.
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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.