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Autor:
John H. Crowe, Luis A. Bagatolli, Fern Tablin, Rachna Bali, Diego Ramirez, Laura Savino, Chad Leidy, Nelly M. Tsvetkova
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (6):1229-1237
There has been ample debate on whether cell membranes can present macroscopic lipid domains as predicted by three-component phase diagrams obtained by fluorescence microscopy. Several groups have argued that membrane proteins and interactions with th
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (1):146-154
Peptide-membrane interactions have been implicated in both the toxicity and aggregation of [beta]-amyloid (A[beta]) peptides. Recent studies have provided evidence for the involvement of liquid-ordered membrane domains known as lipid rafts in the for
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (2):145-153
To understand the role of sphingomyelinase (SMase) in the function of biological membranes, we have investigated the effect of conversion of sphingomyelin (SM) to ceramide (Cer) on the assembly of domains in giant unilamellar vesicles (GUVs). The GUV
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (2):434-443
To investigate an interfacial behavior of the aglycon of glycyrrhizin (GC), glycyrrhetinic acid (GA), with a lipid raft model consisting of equimolar ternary mixtures of N-palmitoyl sphingomyelin (PSM), dioleoylphosphatidylcholine (DOPC), and cholest