@article {4703,
	title = {Electrostatically mediated interactions between cationic lipid-DNA particles and an anionic surface},
	journal = {Archives of Biochemistry and Biophysics},
	volume = {366},
	number = {1},
	year = {1999},
	note = {ISI Document Delivery No.: 202JKTimes Cited: 7Cited Reference Count: 29},
	month = {Jun},
	pages = {31-39},
	type = {Article},
	abstract = {In an effort to model the interaction of lipid-based DNA delivery systems with anionic surfaces, such as a cell membrane, we have utilized microelectrophoresis to characterize how electrokinetic measurements can provide information on surface charge and binding characteristics. We have established that cationic lipids, specifically N-N-dioleoyl-N,N-dimethylammonium chloride (DODAC), incorporated into liposomes prepared with I,2-dioleoyl-i-glycero-3-phosphoethanolamine (DOPE) or 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) at 50 mol\%, change the inherent electrophoretic mobility of anionic latex polystyrene beads. Self-assembling lipid-DNA particles (LDPs), prepared at various cationic lipid to negative DNA phosphate charge ratios, effected no changes in bead mobility when the LDP charge ratio (+/-) was equal to or less than 1. Increasing the LDP concentration in a solution of 0.1\% (w/v) anionic beads resulted in a charge reversal effect when a net charge of LDP to total bead charge ratio (+/-) of 1:1 was observed. LDP formulations, utilizing either DOPE or DOPC, showed similar titration profiles with a charge reversal observed at a 1:1 net LDP to bead charge ratio (+/-). It was confirmed through centrifugation studies that the DNA in the LDP was associated with the anionic latex beads through electrostatic interactions. LDP binding, rather than the binding of dissociated cationic lipids, resulted in the observed electrophoretic mobility changes of the anionic latex beads. (C) 1999 Academic Press.},
	keywords = {BILAYERS, CELLS, ELECTROSTATIC INTERACTIONS, FUSION, GENE-TRANSFER, lipid-DNA particles, lipoplex, LIPOSOMES, microelectrophoresis, PHOSPHATIDYLETHANOLAMINE, PLASMID DNA, VESICLES},
	isbn = {0003-9861},
	url = {<Go to ISI>://000080648400005},
	author = {Wong, F. M. P. and Bally, M. B. and Brooks, D. E.}
}
@article {4405,
	title = {Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {95},
	number = {21},
	year = {1998},
	note = {ISI Document Delivery No.: 129DLTimes Cited: 84Cited Reference Count: 37},
	month = {Oct},
	pages = {12129-12134},
	type = {Article},
	abstract = {The Pointed (PNT) domain and an adjacent mitogen-activated protein (MAP) kinase phosphorylation site are defined by sequence conservation among a subset of ets transcription factors and are implicated in two regulatory strategies, protein interactions and posttranslational modifications, respectively. By using NMR, we have determined the structure of a 110-residue fragment of murine Ets-1 that includes the PNT domain and MAP kinase site. The Ets-1 PNT domain forms a monomeric five-helix bundle. The architecture is distinct from that of any known DNA- or protein-binding module, including the helix-loop-helix fold proposed for the PNT domain of the ets protein TEL. The MAP kinase site is in a highly flexible region of both the unphosphorylated and phosphorylated forms of the Ets-1 fragment. Phosphorylation alters neither the structure nor monomeric state of the PNT domain. These results suggest that the Ets-1 PNT domain functions in heterotypic protein interactions and support the possibility that target recognition is coupled to structuring of the MAP kinase site.},
	keywords = {beta, CHRONIC MYELOMONOCYTIC LEUKEMIA, FUSION, GENE, NMR, OLIGOMERIZATION, TEL, TRANSCRIPTION FACTORS, TRANSLOCATION, TROPONIN-C},
	isbn = {0027-8424},
	url = {<Go to ISI>://000076447900013},
	author = {Slupsky, C. M. and Gentile, L. N. and Donaldson, L. W. and Mackereth, C. D. and Seidel, J. J. and Graves, B. J. and McIntosh, L. P.}
}
