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Structure of the third intracellular loop of the human cannabinoid 1 receptor.

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The third cytoplasmic loop (IC3) is a determinant in the dynamic life cycle of G protein-coupled receptors, including the activation, internalization, desensitization, and resensitization processes. Here, we characterize the structural features of the IC3 of the cannabinoid 1 receptor (CB1) in

Reverse-phase HPLC separation of hemp seed (Cannabis sativa L.) protein hydrolysate produced peptide fractions with enhanced antioxidant capacity.

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Hemp seed protein hydrolysate (HPH) was produced through simulated gastrointestinal tract (GIT) digestion of hemp seed protein isolate followed by partial purification and separation into eight peptide fractions by reverse-phase (RP)-HPLC. The peptide fractions exhibited higher oxygen radical

Lack of positive allosteric modulation of mutated alpha(1)S267I glycine receptors by cannabinoids.

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Loss of inhibitory synaptic transmission within the dorsal horn of the spinal cord plays a key role in the development of chronic pain following inflammation or nerve injury. Inhibitory postsynaptic transmission in the adult spinal cord involves mainly glycine. Ajulemic acid and HU210 are

A critical role for a tyrosine residue in the cannabinoid receptors for ligand recognition.

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Previous mutation and modeling studies have identified an aromatic cluster in the transmembrane helix (TMH) 3-4-5 region as important for ligand binding at the CB(1) and CB(2) cannabinoid receptors. Through novel mixed mode Monte Carlo/Stochastic Dynamics (MC/SD) calculations, we tested the

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