Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Ultrastructural localization of dynorphin in the dentate gyrus in human temporal lobe epilepsy: a study of reorganized mossy fiber synapses.
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Demonstrated by preembedding immunoperoxidase electron microscopy in human surgical dentate gyrus specimens that dynorphin A immunoreactivity is localized to neuronal dense-core vesicles in mossy fiber axon terminals and dendritic shafts and spines.
"In electron microscopic preparations, dynorphin A immunoreactivity was highly associated with dense core vesicles and was localized predominantly in axon terminals in the inner molecular layer of the dentate gyrus, although some dynorphin-labeled dense core vesicles were also observed in dendritic shafts and spines."
Supersensitivity to mu-opioid receptor-mediated inhibition of the adenylyl cyclase pathway involves pertussis toxin-resistant Galpha protein subunits.
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Opioid receptor agonists stimulate [35S]GTPgammaS binding and inhibit forskolin-stimulated adenylyl cyclase activity via pertussis-toxin-sensitive Galpha(i/o) subunits.
"In control animals, the mu-opioid selective agonists, sufentanil and DAMGO, stimulated [35S]5'-(gamma-thio)-triphosphate ([35S]GTP gamma S) binding and inhibited forskolin-stimulated adenylyl cyclase activity, through a mechanism involving pertussis toxin (PTX) sensitive G alpha(i/o) subunits."
Crystal structure of the µ-opioid receptor bound to a morphinan antagonist.
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Opioid receptors couple predominantly to the inhibitory G protein Gi to inhibit adenylyl cyclase and mediate analgesia.
"The μOR couples predominantly to Gi, the inhibitory G protein for adenylyl cyclase. μOR signaling through Gi is responsible for its analgesic properties4."
Architecture of the human interactome defines protein communities and disease networks.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
NMR and structural model of dynorphin A (1-17) bound to dodecylphosphocholine micelles.
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Characterized the 3D NMR structure of human dynorphin A(1-17), the high-affinity endogenous agonist of the kappa-opioid receptor (OPRK1), showing a well-defined amphipathic alpha-helix spanning Gly3-Pro10 when bound to membrane-mimetic micelles.
"Dynorphin A (1-17) (dynorphin) acts preferentially and with high affinity at the kappa-opioid receptor, for which it is the natural, endogenous ligand."
The receptor:G-protein complex dissociates
The high affinity receptor complex binds to G-protein
The receptor:G-protein complex releases GDP
Opioid dissociates from MOR
The receptor:G-protein complex binds GTP
Opioid receptors bind opioid peptides
Liganded Gi-activating GPCR acts as a GEF for Gi
The Ligand:GPCR:Gi complex dissociates
Liganded Gi-activating GPCRs bind inactive heterotrimeric G-protein Gi