id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-336542-6asieplk	Tanco, Sebastián	Structure–Function Analysis of the Short Splicing Variant Carboxypeptidase Encoded by Drosophila melanogaster silver	2010-08-20		.txt	text/plain	7625	431	56	Overall, DmCPD1Bs conforms to the structure of N/E-type funnelins/M14B metallopeptidases, but it has two unique structural elements potentially involved in regulation of its activity: (i) two contiguous surface cysteines that may become palmitoylated and target the enzyme to membranes, thus providing control through localization, and (ii) a surface hot spot targetable by peptidases that would provide a regulatory mechanism through proteolytic inactivation. Given that the fruit fly possesses orthologs of only two out of the five proteolytically competent N/E-type funnelins found in higher vertebrates, DmCPD1Bs may represent a functional analog of at least one of the missing mammalian CPs. The silver (svr) gene was discovered in Drosophila melanogaster by Bridges in the early 1920s and it maps near the distal end of chromosome X. [3] [4] [5] [6] The long variants possess the overall modular structure and sequence features of carboxypeptidase D (CPD), a glycosylated 180-kDa enzyme studied since the middle 1990s in fruit fly, mouse, rat, duck, bovine, chicken, and humans.	./cache/cord-336542-6asieplk.txt	./txt/cord-336542-6asieplk.txt