scholarly journals α-Synuclein Binds Large Unilamellar Vesicles as an Extended Helix†

Biochemistry ◽  
2009 ◽  
Vol 48 (11) ◽  
pp. 2304-2306 ◽  
Author(s):  
Adam J. Trexler ◽  
Elizabeth Rhoades
Keyword(s):  
Unilamellar Vesicles ◽  
Large Unilamellar Vesicles

Evolution of the thermotropic properties of large unilamellar vesicles (LUV)

1984 ◽  
Vol 40 (7) ◽  
pp. 715-717 ◽  
Author(s):  
M. Vandenbranden ◽  
C. Stil ◽  
R. Brasseur ◽  
J. -M. Ruysschaert
Keyword(s):  
Unilamellar Vesicles ◽  
Large Unilamellar Vesicles ◽  
Thermotropic Properties

The Efficacies of Cell-Penetrating Peptides in Accumulating in Large Unilamellar Vesicles Depend on their Ability To Form Inverted Micelles

ChemBioChem ◽  
2014 ◽  
Vol 15 (6) ◽  
pp. 884-891 ◽  
Author(s):  
Jean-Marie Swiecicki ◽  
Annika Bartsch ◽  
Julien Tailhades ◽  
Margherita Di Pisa ◽  
Benjamin Heller ◽  
...  
Keyword(s):  
Cell Penetrating Peptides ◽  
Unilamellar Vesicles ◽  
Large Unilamellar Vesicles ◽  
Cell Penetrating

Interactions of Thionin fromPyrularia puberawith Dipalmitoylphosphatidylglycerol Large Unilamellar Vesicles†

Biochemistry ◽  
1997 ◽  
Vol 36 (10) ◽  
pp. 2860-2866 ◽  
Author(s):  
Wenhao Huang ◽  
Leo P. Vernon ◽  
Lee D. Hansen ◽  
John D. Bell
Keyword(s):  
Unilamellar Vesicles ◽  
Large Unilamellar Vesicles

Surface changes induced by osmotic shrinkage on large unilamellar vesicles

1996 ◽  
Vol 84 (1) ◽  
pp. 35-45 ◽  
Author(s):  
E.A. Disalvo ◽  
A.M. Campos ◽  
E. Abuin ◽  
E.A. Lissi
Keyword(s):  
Unilamellar Vesicles ◽  
Large Unilamellar Vesicles ◽  
Surface Changes

scholarly journals Asymmetric reassociation of calf spleen NAD+ glycohydrolase into liposomes

1987 ◽  
Vol 246 (2) ◽  
pp. 319-324 ◽  
Author(s):  
H M Muller ◽  
F Schuber
Keyword(s):  
Outer Surface ◽  
Active Site ◽  
Gel Filtration ◽  
Water Soluble ◽  
Unilamellar Vesicles ◽  
Phosphatidylcholine Liposomes ◽  
Nad Glycohydrolase ◽  
Large Unilamellar Vesicles ◽  
Solubilized Enzyme

NAD+ glycohydrolase (NAD+ nucleosidase, EC 3.2.2.6) can be solubilized from calf spleen microsomes (microsomal fractions) by steapsin or by detergents to yield respectively a hydrophilic (i.e. water-soluble) and a hydrophobic form of the enzyme. The detergent-solubilized enzyme was successfully reassociated into phosphatidylcholine liposomes either by a cholate-dialysis or by a gel-filtration procedure. In both cases the incorporation of NAD+ glycohydrolase was found to be completely asymmetric, i.e. the active site of the enzyme was exposed only at the outer surface of the vesicles. By contrast, as judged by flotation experiments, the hydrophilic form of NAD+ glycohydrolase could not be reassociated into liposomes. These results are in agreement with the hypothesis that calf spleen NAD+ glycohydrolase is an amphipathic protein. When incorporated into large unilamellar vesicles composed of phosphatidylcholine, NAD+ glycohydrolase was not found to catalyse vectorial transfer of NAD+ by transglycosidation with nicotinamide as acceptor.

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