@article {752,
	title = {Tuning the hemolytic and antibacterial activities of amphiphilic polynorbornene derivatives.},
	journal = {J Am Chem Soc},
	volume = {126},
	year = {2004},
	month = {2004 Dec 8},
	pages = {15870-5},
	abstract = {Amphiphilic cationic polynorbornene derivatives, soluble in water, were prepared from modular norbornene monomers, with a wide range of molecular weights (M(n) = 1600-137 500 g/mol) and narrow polydispersities (PDI = 1.1-1.3). The antibacterial activity determined by growth inhibition assays and the hemolytic activity against human red blood cells were measured and compared to determine the selectivity of the polymers for bacterial over mammalian cells. The effects of monomer repeat unit hydrophobicity and polymer molecular weight on antibacterial and hemolytic activities were determined. The hydrophobicity of the repeat unit was observed to have dramatic effects on antibacterial and hemolytic activities. Lipid membrane disruption activities of the polymers was confirmed by measuring polymer-induced dye leakage from large unilamellar vesicles. By tuning the overall hydrophobicity of the polymer through random copolymerizations of modular norbornene derivatives, highly selective, nonhemolytic antibacterial activities were obtained. For appropriate monomer composition, selectivity against bacteria versus human red blood cells was determined to be over 100.},
	keywords = {Anti-Bacterial Agents, Bacillus subtilis, Cell Membrane, Cholesterol, Erythrocytes, Escherichia coli, Hemolysis, Humans, Liposomes, Microbial Sensitivity Tests, Molecular Weight, Norbornanes, Polymers, Structure-Activity Relationship},
	issn = {0002-7863},
	doi = {10.1021/ja045664d},
	author = {Ilker, M Firat and N{\"u}sslein, Klaus and Tew, Gregory N and Coughlin, E Bryan}
}
@article {715,
	title = {Lipid rafts, caveolae, caveolin-1, and entry by Chlamydiae into host cells.},
	journal = {Exp Cell Res},
	volume = {287},
	year = {2003},
	month = {2003 Jul 1},
	pages = {67-78},
	abstract = {Obligate intracellular bacterial pathogens of the genus Chlamydia are reported to enter host cells by both clathrin-dependent and clathrin-independent processes. C. trachomatis serovar K recently was shown to enter cells via caveolae-like lipid raft domains. We asked here how widespread raft-mediated entry might be among the Chlamydia. We show that C. pneumoniae, an important cause of respiratory infections in humans that additionally is associated with cardiovascular disease, and C. psittaci, an important pathogen in domestic mammals and birds that also infects humans, each enter host cells via cholesterol-rich lipid raft microdomains. Further, we show that C. trachomatis serovars E and F also use these domains to enter host cells. The involvement of these membrane domains in the entry of these organisms was indicated by the sensitivity of their entry to the raft-disrupting agents Nystatin and filipin, and by their intracellular association with caveolin-1, a 22-kDa protein associated with the formation of caveolae in rafts. In contrast, caveolin-marked lipid raft domains do not mediate entry of C. trachomatis serovars A, 36B, and C, nor of LGV serovar L2 and MoPn. Finally, we show that entry of each of these chlamydial strains is independent of cellular expression of caveolin-1. Thus, entry via the Nystatin and filipin-sensitive pathway is dependent on lipid rafts containing cholesterol, rather than invaginated caveolae per se.},
	keywords = {Anti-Bacterial Agents, Caveolae, Caveolin 1, Caveolins, Chlamydia, Chlamydia Infections, Cholesterol, Dose-Response Relationship, Drug, Eukaryotic Cells, Filipin, HeLa Cells, Host-Parasite Interactions, Humans, Membrane Microdomains, Nystatin, Species Specificity},
	issn = {0014-4827},
	author = {Stuart, Elizabeth S and Webley, Wilmore C and Norkin, Leonard C}
}
@article {710,
	title = {Extracellular simian virus 40 transmits a signal that promotes virus enclosure within caveolae.},
	journal = {Exp Cell Res},
	volume = {246},
	year = {1999},
	month = {1999 Jan 10},
	pages = {83-90},
	abstract = {It was reported earlier that entry of simian virus 40 (SV40) into cells is promoted by a signal transmitted by the virus from the cell surface and that SV40 enters cells through caveolae. It is shown here that bound SV40 begins to partition into a caveolae-enriched Triton X-100-insoluble membrane fraction at 30 min postadsorption. Maximal levels of SV40 were seen in that fraction at 1 h. The sterol-binding agent nystatin, which selectively disrupts the cholesterol-enriched caveolae-containing membrane microdomain, selectively blocked the SV40-induced signal. This implies that the SV40 signal is transmitted from that membrane microdomain. The tyrosine kinase inhibitor genistein, which was earlier shown to block the SV40-induced signal and infectious entry, did not block the partitioning of SV40 into the detergent-insoluble membrane fraction. This shows that the signal is not required for the translocation of SV40 to the detergent-insoluble membrane and is consistent with the finding that the signal is likely transmitted from that membrane microdomain. However, electron microscopy of the Triton X-100-insoluble membrane fraction showed that genistein caused SV40 particles to accumulate at the annuli or mouths of the caveolae. In contrast, most SV40 particles were found enclosed within caveolae in parallel samples from untreated control cells. Together, these results imply that SV40 initially binds to flat detergent-soluble membrane. The virus then translocates to a caveolae-containing detergent-insoluble membrane microdomain. From the flat portion of that membrane microdomain the virus induces a signal which promotes its entry into caveolae.},
	keywords = {Animals, Blotting, Northern, Blotting, Western, Caveolin 1, Caveolins, Cell Line, Cell Membrane, Cercopithecus aethiops, Cholesterol, Endocytosis, Genes, myc, Genistein, Kidney, Membrane Proteins, Microscopy, Electron, Nystatin, Octoxynol, Signal Transduction, Simian virus 40, Solubility},
	issn = {0014-4827},
	doi = {10.1006/excr.1998.4301},
	author = {Chen, Y and Norkin, L C}
}
