@article {2352,
	title = {An Improved Synthesis of Pyridine-Thiazole Cores of Thiopeptide Antibiotics},
	journal = {Journal of Organic Chemistry},
	volume = {74},
	number = {15},
	year = {2009},
	note = {ISI Document Delivery No.: 476XOTimes Cited: 4Cited Reference Count: 29Aulakh, Virender S. Ciufolini, Marco A.},
	month = {Aug},
	pages = {5750-5753},
	type = {Article},
	abstract = {The oxidation of 2-methylthiazoles to 2-formylthiazoles simplifies the implementation of the Bagley variant of the Bohlmann-Rahtz reaction as a key step in a concise new route to pyridine cores of thiopeptide antibiotics.},
	keywords = {1ST, AMYTHIAMICIN-D, CONSTRUCTION, GE2270-A, KEY BUILDING-BLOCKS, macrocycle, MICROCOCCIN P1, ONE-POT, PROMOTHIOCIN, SYNTHESIS, THIOSTREPTON},
	isbn = {0022-3263},
	url = {<Go to ISI>://000268480300104},
	author = {Aulakh, V. S. and Ciufolini,Marco A.}
}
@article {4486,
	title = {Clq binding to liposomes is surface charge dependent and is inhibited by peptides consisting of residues 14-26 of the human ClqA chain in a sequence independent manner},
	journal = {Biochimica Et Biophysica Acta-Biomembranes},
	volume = {1418},
	number = {1},
	year = {1999},
	note = {ISI Document Delivery No.: 189EWTimes Cited: 20Cited Reference Count: 36},
	month = {Apr},
	pages = {19-30},
	type = {Article},
	abstract = {Complement activation by anionic liposomes proceeds by antibody-independent, C1q-initiated activation of the classical pathway. Purified C1q bound to anionic liposomes in an acidic lipid concentration-dependent manner. Saturation binding, but not the apparent association constant, was enhanced by increasing the cardiolipin content of the liposomes or decreasing either the pH or ionic strength of the reaction mixture. These observations indicate the involvement of electrostatic factors in the binding. A highly cationic region in the collagen-like domain of C1q comprised of residues 14-26 of the C1qA polypeptide chain was assessed for involvement in liposome binding. This region has previously been shown to mediate C1q binding to other immunoglobulin-independent activators of the classical pathway of complement. Peptides containing residues 14-26 of C1qA, denoted C1qA(14-26), inhibited C1q binding to and complement activation by anionic liposomes. The inhibitory capacity of these cationic peptides had no sequence or conformation specificity. Rather, the amount of positive charge on the peptides was the determining factor. When present in excess, peptides with five cationic residues inhibited C1q binding and complement activation; however, C1q peptides with only two cationic residues did not. In addition to the C1qA(14-26) region, other parts of C1q that contain cationic residues may also be involved in C1q binding to anionic liposomes. (C) 1999 Elsevier Science B.V. All rights reserved.},
	keywords = {1ST, ACTIVATES COMPLEMENT, C1Q A-CHAIN, CLASSICAL COMPLEMENT PATHWAY, CLEARANCE, Clq binding, COLLAGEN, COMPONENT, liposome clearance, liposome-mediated complement activation, PHAGOCYTOSIS, PROTEINS, SERUM, SYSTEM},
	isbn = {0005-2736},
	url = {<Go to ISI>://000079892300002},
	author = {Bradley, A. J. and Brooks, D. E. and Norris-Jones, R. and Devine, D. V.}
}
