Glyceryl Dioleate
Glyceryl Dioleate structure
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Common Name | Glyceryl Dioleate | ||
|---|---|---|---|---|
| CAS Number | 25637-84-7 | Molecular Weight | 620.986 | |
| Density | 0.9±0.1 g/cm3 | Boiling Point | 678.3±35.0 °C at 760 mmHg | |
| Molecular Formula | C39H72O5 | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | 189.2±19.4 °C | |
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Acid-labile mPEG-vinyl ether-1,2-dioleylglycerol lipids with tunable pH sensitivity: synthesis and structural effects on hydrolysis rates, DOPE liposome release performance, and pharmacokinetics.
Mol. Pharm. 9(11) , 3266-76, (2012) A family of 3-methoxypoly(ethylene glycol)-vinyl ether-1,2-dioleylglycerol (mPEG-VE-DOG) lipopolymer conjugates, designed on the basis of DFT calculations to possess a wide range of proton affinities, was synthesized and tested for their hydrolysis kinetics i... |
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Stability of a liposomal formulation containing lipoyl or dihydrolipoyl acylglycerides.
J. Liposome Res. 24(4) , 304-12, (2014) The acylglycerides of lipoic and dihydrolipoic acids may serve as slow-release sources for cutaneous delivery of these antioxidants when formulated in a liposomal vehicle.Testing was conducted to determine the storage stability of lipoyl glycerides in phospho... |
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Defective triglyceride biosynthesis in CETP-deficient SW872 cells.
J. Lipid Res. 56 , 1669-78, (2015) We previously reported that reducing the expression of cholesteryl ester transfer protein (CETP) disrupts cholesterol homeostasis in SW872 cells and causes an ∼50% reduction in TG. The causes of this reduced TG content, investigated here, could not be attribu... |
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Identification of a botanical inhibitor of intestinal diacylglyceride acyltransferase 1 activity via in vitro screening and a parallel, randomized, blinded, placebo-controlled clinical trial.
Nutr. Metab. 12 , 27, (2015) Diacylglyceride acyltransferase 1 (DGAT1) is the enzyme that adds the final fatty acid on to a diacylglyceride during triglyceride (TG) synthesis. DGAT1 plays a key role in the repackaging of dietary TG into circulating TG rich chylomicrons. A growing amount ... |
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Lipid-based liquid crystalline nanoparticles as oral drug delivery vehicles for poorly water-soluble drugs: cellular interaction and in vivo absorption.
Int. J. Nanomedicine 7 , 3703-18, (2012) Lipid-based liquid crystalline nanoparticles (LCNPs) have attracted growing interest as novel drug-delivery systems for improving the bioavailability of both hydrophilic and hydrophobic drugs. However, their cellular interaction and in vivo behavior have not ... |
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The Energy of COPI for Budding Membranes.
PLoS ONE 10 , e0133757, (2015) As a major actor of cellular trafficking, COPI coat proteins assemble on membranes and locally bend them to bud 60 nm-size coated particles. Budding requires the energy of the coat assembly to overcome the one necessary to deform the membrane which primarily ... |
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Substrate chirality and specificity of diacylglycerol kinases and the multisubstrate lipid kinase.
Biochemistry 46(49) , 14225-31, (2007) The alpha, zeta, and epsilon isoforms of diacylglycerol kinase exhibit a high degree of stereospecificity in the phosphorylation of diacylglycerol. In comparison, a multiple lipid kinase, MuLK, shows much less stereospecificity, phosphorylating 1,2-dioleoylgl... |
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In vitro stereoselective hydrolysis of diacylglycerols by hormone-sensitive lipase.
Biochim. Biophys. Acta 1801(1) , 77-83, (2010) Hormone-sensitive lipase (HSL) contributes importantly to the mobilization of fatty acids in adipocytes and shows a substrate preference for the diacylglycerols (DAGs) originating from triacylglycerols. To determine whether HSL shows any stereopreference duri... |
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A comparison of the membrane binding properties of C1B domains of PKCgamma, PKCdelta, and PKCepsilon.
Biophys. J. 96(9) , 3638-47, (2009) The C1 domains of classical and novel PKCs mediate their diacylglycerol-dependent translocation. Using fluorescence resonance energy transfer, we studied the contribution of different negatively charged phospholipids and diacylglycerols to membrane binding. T... |
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The membrane binding kinetics of full-length PKCα is determined by membrane lipid composition.
Biochim. Biophys. Acta 1821(11) , 1434-42, (2012) Protein kinase Cα (PKCα) is activated by its translocation to the membrane. Activity assays show the importance of PIP(2) in determining the specific activity of this enzyme. A FRET stopped flow fluorescence study was carried out to monitor the rapid kinetics... |