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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Abhydrolase domain containing 6

Top mentioned proteins: ACID, fatty acid amide hydrolase, CAN, ABHD12, CB1
Papers on ABHD6
Porcupine Controls Hippocampal AMPAR Levels, Composition, and Synaptic Transmission.
Bredt et al., San Diego, United States. In Cell Rep, Feb 2016
We systematically surveyed these and found that PORCN and ABHD6 increase GluA1 levels in transfected cells.
Potent and selective N-(4-sulfamoylphenyl)thiourea-based GPR55 agonists.
Nevalainen et al., Kuopio, Finland. In Eur J Med Chem, Feb 2016
The designed compounds were not active when tested against various endocannabinoid targets (CB1R, CB2R, FAAH, MGL, ABHD6 and ABHD12), indicating compounds' selectivity for the GPR55.
α/β Hydrolase Domain-containing 6 (ABHD6) Degrades the Late Endosomal/Lysosomal Lipid Bis(monoacylglycero)phosphate.
Zimmermann et al., Graz, Austria. In J Biol Chem, Jan 2016
α/β Hydrolase domain-containing 6 (ABHD6) can act as monoacylglycerol hydrolase and is believed to play a role in endocannabinoid signaling as well as in the pathogenesis of obesity and liver steatosis.
Activation of CB2 receptor is required for the therapeutic effect of ABHD6 inhibition in experimental autoimmune encephalomyelitis.
Zhang et al., Bethesda, United States. In Neuropharmacology, Dec 2015
Alpha/beta-hydrolase domain 6 (ABHD6) is a novel 2-arachidonoylglycerol (2-AG) hydrolytic enzyme, that can fine-tune the endocannabinoid signaling in the central nervous system.
Revisiting 1,3,4-Oxadiazol-2-ones: Utilization in the Development of ABHD6 Inhibitors.
Nevalainen et al., Kuopio, Finland. In Bioorg Med Chem, Nov 2015
This article describes our systematic approach to exploring the utility of the 1,3,4-oxadiazol-2-one scaffold in the development of ABHD6 inhibitors.
Comparative molecular field analysis and molecular dynamics studies of α/β hydrolase domain containing 6 (ABHD6) inhibitors.
Poso et al., Lublin, Poland. In J Mol Model, Oct 2015
α/β hydrolase domain containing 6 (ABHD6)--an enzyme forming part of the endocannabinoid system--is a newly discovered post-genomic protein acting as a 2-AG (2-arachidonoylglycerol) serine hydrolase.
Nuclear diacylglycerol lipase-α in rat brain cortical neurons: evidence of 2-arachidonoylglycerol production in concert with phospholipase C-β activity.
Sallés et al., Vitoria-Gasteiz, Spain. In J Neurochem, Mar 2015
2-AG, 2-arachidonoylglycerol; AA, arachidonic acid; ABHD6, α-β-hydrolase domain-6; COX-2, cyclooxygenase-2; DAGK, diacylglycerol kinase; DAGs, diacylglycerols; LPP, lipid phosphate phosphatase; MAGL, monoacylglycerol lipase; NAM, N-arachidonoylmaleimide; PA, phosphatidic acid; PGG2 -G, prostaglandin G2 -glycerol; PLD, phospholipase D; PtdCho, phosphatidylcholine; PtdInsP2 , phosphatidylinositol-4,5-bisphosphate; THL, tetrahydrolipstatin.
Effect of selective inhibition of monoacylglycerol lipase (MAGL) on acute nausea, anticipatory nausea, and vomiting in rats and Suncus murinus.
Cravatt et al., Guelph, Canada. In Psychopharmacology (berl), Feb 2015
An activity-based protein profiling analysis of samples of tissue collected from the visceral insular cortex in rats and whole brain tissues in shrews revealed that MJN110 selectively inhibited MAGL and the alternative 2-AG hydrolase, ABHD6.
Optimization of 1,2,5-thiadiazole carbamates as potent and selective ABHD6 inhibitors.
Parkkari et al., Kuopio, Finland. In Chemmedchem, Feb 2015
At present, inhibitors of α/β-hydrolase domain 6 (ABHD6) are viewed as a promising approach to treat inflammation and metabolic disorders.
Robust hydrolysis of prostaglandin glycerol esters by human monoacylglycerol lipase (MAGL).
Laitinen et al., Kuopio, Finland. In Mol Pharmacol, 2014
The primary route of inactivation of the endocannabinoid 2-arachidonoylglycerol in the central nervous system is through enzymatic hydrolysis, mainly carried out by monoacylglycerol lipase (MAGL), along with a small contribution by the α/β-hydrolase domain (ABHD) proteins ABHD6 and ABHD12.
α/β-Hydrolase domain-6-accessible monoacylglycerol controls glucose-stimulated insulin secretion.
Prentki et al., Montréal, Canada. In Cell Metab, 2014
Here we show that in β cells, glucose stimulates production of lipolysis-derived long-chain saturated monoacylglycerols, which further increase upon inhibition of the membrane-bound monoacylglycerol lipase α/β-Hydrolase Domain-6 (ABHD6).
Optimization and characterization of a triazole urea inhibitor for diacylglycerol lipase beta (DAGL-β)
Rosen et al., Bethesda, United States. In Unknown Journal, 2012
Out of more than 20 serine hydrolases (SHs) profiled by gel-based competitive ABPP, ML294 is observed to have one anti-target, alpha/beta hydrolase domain-containing protein 6 (ABHD6).
Optimization and characterization of triazole urea inhibitors for abhydrolase domain containing protein 6 (ABHD6)
Rosen et al., Bethesda, United States. In Unknown Journal, 2012
Three of the key enzymes responsible for 2-AG hydrolysis (and thus inactivation) are monoacylglycerol lipase (MAGL), abhydrolase domain containing proteins 6 (ABHD6), and ABHD12.
Inhibitors of the endocannabinoid-degrading enzymes, or how to increase endocannabinoid's activity by preventing their hydrolysis.
Muccioli et al., Leuven, Belgium. In Recent Pat Cns Drug Discov, 2012
To date four enzymes - Fatty Acid Amide Hydrolase (FAAH), N-Acylethanolamine-hydrolyzing Acid Amidase (NAAA), Monoacylglycerol Lipase (MAGL), α/β-Hydrolase Domain 6 (ABHD6) - were shown to control endocannabinoid levels in tissues or in intact cells.
The serine hydrolases MAGL, ABHD6 and ABHD12 as guardians of 2-arachidonoylglycerol signalling through cannabinoid receptors.
Laitinen et al., Kuopio, Finland. In Acta Physiol (oxf), 2012
We review recent research on monoacylglycerol lipase (MAGL), ABHD6 and ABHD12, three serine hydrolases that together account for approx.
Dual inhibition of alpha/beta-hydrolase domain 6 and fatty acid amide hydrolase increases endocannabinoid levels in neurons.
Stella et al., Seattle, United States. In J Biol Chem, 2011
Dual inhibition of alpha/beta-hydrolase domain 6 and fatty acid amide hydrolase increases endocannabinoid levels in neurons.
The serine hydrolase ABHD6 controls the accumulation and efficacy of 2-AG at cannabinoid receptors.
Stella et al., Seattle, United States. In Nat Neurosci, 2010
ABHD6 is a rate-limiting step of 2-AG signaling
High expression of the evolutionarily conserved alpha/beta hydrolase domain containing 6 (ABHD6) in Ewing tumors.
Staege et al., Halle, Germany. In Cancer Sci, 2009
High expression of ABHD6 in Ewing family tumors (EFT) in comparison to normal tissues and other tumors suggests that ABHD6 might be an interesting new diagnostic or therapeutic target for EFT.
An unannotated alpha/beta hydrolase superfamily member, ABHD6 differentially expressed among cancer cell lines.
Ji et al., Shanghai, China. In Mol Biol Rep, 2009
report the tissue distribution, subcellular location and differential distribution among cancer cell lines of Abhd6, one unannotated member of this group
A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol.
Cravatt et al., Los Angeles, United States. In Chem Biol, 2007
Data reveal that 85% of brain 2-arachidonoylglycerol hydrolase activity can be ascribed to monoacylglycerol lipase(MAGL), and the remaining 15% is catalyzed by ABHD6 and ABHD12.
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