id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-329553-93tbgn2b	nan	The 17-residue transmembrane domain of beta-galactoside alpha 2,6- sialyltransferase is sufficient for Golgi retention	1992-04-02		.txt	text/plain	7954	426	55	A series of experiments has shown that the 17-residue transmembrane domain of ST is sufficient to confer localization to the Golgi apparatus when transferred to the corresponding region of a cell surface type II integral membrane protein. In this report, we have fused different regions of the NH2-terminal ST sequence to the ectodomain of dipeptidyl peptidase IV (DPPIV), a type 11 surface membrane protein (Hong and Doyle, 1990; Ogato et al ., 1989) to study their abilities in conferring Golgi localization ofthe chimeric proteins. To determine the minimum sequence ofthe N112-terminal region of ST that is sufficient for membrane anchorage and Golgi localization, we have constructed a series of chimeric cDNAs which encode different fusion proteins ( Fig. 1 B) , with decreasing lengths of the N112-terminal ST sequence fused to the ectodomain of DPPIV .	./cache/cord-329553-93tbgn2b.txt	./txt/cord-329553-93tbgn2b.txt