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Organisms can be classified into one of three domains based on differences in the sequences of nucleotides in the cell's ribosomal RNAs (rRNA), the cell's membrane lipid structure, and its sensitivity to antibiotics. The three domains are the Archaea, the Bacteria, and the Eukarya. Prokaryotic organisms belong either to the domain Archaea or.
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This study provides biochemical, pharmacological, cell biology,. Biochemical and pharmacological characterization of human α/β-hydrolase domain containing 6 (ABHD6) and 12 (ABHD12) J. Lipid Res., 53 (2012), pp. 2413-2424. View PDF View article CrossRef View in Scopus Google Scholar.
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α/β-Hydrolase domain 6 (ABHD6) is a monoacylglycerol hydrolase that degrades the endocannabinoid 2-arachidonoylglycerol (2-AG). Although complete or peripheral ABHD6 loss of function is protective against diet-induced obesity and insulin resistance, the role of ABHD6 in the central control of energy balance is unknown.
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Human alpha/beta hydrolase domain 6 (hABHD6) is an enzyme that hydrolyzes 2-arachidonoylglycerol (2-AG), a potent agonist at both cannabinoid CB1 and CB2 receptors.. (5 μL of 550 mM) for 1 hr, respectively. The samples were desalted with a Bio-Spin 6 Column in 50 mM ammonium bicarbonate buffer containing 0.05% w/v octyl-β-glucoside, pH 8.0.
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Domain (biology) The hierarchy of biological classification 's eight major taxonomic ranks. Life is divided into domains, which are subdivided into further groups. Intermediate minor rankings are not shown. In biological taxonomy, a domain ( / dəˈmeɪn / or / doʊˈmeɪn /) ( Latin: regio [1] ), also dominion, [2] superkingdom, realm, or.
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Objective. α/β-Hydrolase domain-6 (ABHD6) is a newly identified monoacylglycerol (MAG) lipase. We recently reported that it negatively regulates glucose stimulated insulin secretion (GSIS) in the β cells by hydrolyzing lipolysis-derived MAG that acts as a metabolic coupling factor and signaling molecule via exocytotic regulator Munc13-1.
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Glucose must be metabolized by pancreatic β cells to promote glucose-stimulated insulin secretion (GSIS). Zhao et al. found that saturated long-chain monoacylglycerol acts as metabolic coupling factor for GSIS, activating the exocytotic effector Munc13-1, and that the monoacylglycerol signal is controlled by α/β-Hydrolase Domain 6 (ABHD6).
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Interleukin-6 (IL-6) is a polyfunctional cytokine that plays a central role in host defense because of its wide range of immune and hemopoietic activities and because of its potent ability to induce the acute-phase responses of the liver ().IL-6 binds first to its cognate α-chain receptor (IL-6R) with low affinity, and then the complex binds to the signal-transducing molecule gp130 to form a.
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Here, we report the x-ray structure (2.4 Å) of the IL-6R ectodomains. The N-terminal strand of the Ig-like domain (D 1) is disulfide-bonded to domain D 2, and domains D 2 and D 3, the cytokine-binding domain, are structurally similar to known cytokine-binding domains. The head-to-tail packing of two closely associated IL-6R molecules observed.
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Communications Biology - A vgrG database was established, which revealed six widely distributed domain families with similar genetic configurations.. VgrG (PDB 6sk0) contains a DUF2345 domain.
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α/β-Hydrolase domain 6 (ABHD6) is an enzyme that has been recently reported to regulate 2-arachidonylglycerol (2-AG) hydrolysis [ 6 ]. 2-AG serves as an important lipid precursor for the eicosanoid signalling pathway and also functions as an endogenous signalling lipid for the activation of cannabinoid receptor 1 and 2 (CB1 and CB2.
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