二癸酰基卵磷脂

Biochem. Biophys. Res. Commun. 217(1) , 179-85, (1995)

Addition of short-chain phospholipids to the gramicidin S-DNA-dioleoyl phosphatidylethanolamine complex enhanced up to 6-fold beta-galactosidase expression in several cell-lines in vitro. Among the compounds tested, the most potent in enhancing transfection w...

Nat. Commun. 4 , 1510, (2013)

Phosphorus supply is a major factor responsible for reduced crop yields. As a result, plants utilize various adaptive mechanisms against phosphorus depletion, including lipid remodelling. Here we report the involvement of a novel plant lipid, glucuronosyldiac...

Diabetes 42(7) , 1032-40, (1993)

To investigate the short-term effects of didecanoyl-L-alpha-phosphatidylcholine on the nasal mucosa and the mechanism by which didecanoyl-L-alpha-phosphatidylcholine enhances the nasal absorption of insulin, an in vitro model was developed. The mucosa from th...

J. Pharm. Sci. 83(12) , 1706-11, (1994)

The transepithelial transport of biosynthetic human growth hormone (hGH) formulated with the absorption enhancers didecanoyl-L-alpha-phosphatidylcholine (DDPC) and alpha-cyclodextrin (alpha-CD) was studied after intranasal administration to rabbits. Plasma co...

Comp. Biochem. Physiol. A. Physiol. 118(2) , 211-4, (1997)

Ion transport in both the frog skin (a high-resistance epithelium) and the rabbit nasal airway epithelium (a low-resistance epithelium) are dominated by electrogenic Na+ absorption via apical membrane amiloride-sensitive Na+ channels, and short-circuit curren...

Am. J. Physiol. 271(4 Pt 1) , L646-55, (1996)

We investigated the mechanism of interference of mucosal application of the short-chain phospholipid didecanoyl-L-alpha-phosphatidylcholine (DDPC; 0.1-0.5%) with ion transport pathways in isolated rabbit nasal airway epithelium (RNAE). Transports of Na+ and C...

Biochim. Biophys. Acta 733(1) , 75-86, (1983)

J. Mol. Biol. 355(3) , 548-61, (2006)

Membrane protein insertion and folding was studied for the major outer membrane protein of Fusobacterium nucleatum (FomA), which is a voltage-dependent general diffusion porin. The transmembrane domain of FomA forms a beta-barrel that is predicted to consist ...

Pharm. Res. 14(4) , 541-5, (1997)

J. Lipid Res. 47(2) , 302-9, (2006)

Critical to biological processes such as membrane fusion and secretion, ion-lipid interactions at the membrane-water interface still raise many unanswered questions. Using reconstituted phosphatidylcholine membranes, we confirm here that multilamellar vesicle...