Search results for "Vesicle"
showing 7 items of 787 documents
Extracellular membrane vesicle shedding and the blood-brain barrier
2010
Kinetic evidence for the incorporation of the [(pentamethylcyclopentadienyl) (2,2′-bipyridyl)(aquo)rhodium(III)] complex into DPPC vesicles
2008
Abstract The binding of the [(pentamethylcyclopentadienyl) (2,2′-bipyridyl)(aquo)rhodium(III)] complex [Cp*RhIII(bpy)H2O]2+, to l -α-dipalmitoylphosphatidyl choline (DPPC) vesicles has been estimated by studying the kinetics of the electron transfer reaction between the rhodium(III) complex and formiate ions. Kinetic measurements carried out under anaerobic conditions in absence and presence of DPPC show that the total reaction is composed of two steps. The rate of the first reaction increases with the phospholipid concentration, while that of the second process is independent of the concentration of DPPC. This is consistent with a reaction, where the two reacting species are partitioned be…
Shedding of vesicles from mesoangioblast A6 stem cells
2006
Proapoptotic effects of oligodendroglioma cells on primary brain cells in culture.
2009
Internalization of novel non-viral vector TAT-streptavidin into human cells
2007
BMC Biotechnology, 7 (1)
Binding and internalization of human papillomavirus type 33 virus-like particles by eukaryotic cells
1995
Infection of cells by human papillomaviruses (HPVs) associated with malignant genital lesions has not been studied because of the lack of an in vitro system and the unavailability of virions. We have now used virus-like particles (VLPs) of HPV type 33 to analyze the initial events in the interaction of the HPV capsid with cell lines. Binding of VLPs to HeLa cells was observed in biochemical assays and by immunofluorescence. VLP binding was inhibited by antisera raised against VLPs but not by monoclonal antibodies recognizing either L1 or L2 epitopes accessible on VLPs. Under saturating conditions, approximately 2 x 10(4) VLPs were bound per cell, with a dissociation constant of about 100 pM…
Lipid Binding Controls Dimerization of the Coat Protein p24 Transmembrane Helix
2019
Abstract Coat protein (COP) I and COP II complexes are involved in the transport of proteins between the endoplasmic reticulum and the Golgi apparatus in eukaryotic cells. The formation of COP I/II complexes at membrane surfaces is an early step in vesicle formation and is mastered by p24, a type I transmembrane protein. Oligomerization of p24 monomers was suggested to be mediated and/or stabilized via interactions within the transmembrane domain, and the p24 transmembrane helix appears to selectively bind a single sphingomyelin C18:0 molecule. Furthermore, a potential cholesterol-binding sequence has also been predicted in the p24 transmembrane domain. Thus, sphingomyelin and/or cholestero…