id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-299281-5z1xminb	nan	Oligomerization of a membrane protein correlates with its retention in the Golgi complex	1993-09-02		.txt	text/plain	8150	420	53	Our data suggest that SDS-resistant oligomers form as newly synthesized molecules of Gml arrive at the Golgi complex and may interact (directly or indirectly) with an actinbased cytoskeletal matrix. Together, these observations suggest that SDS-resistant oligomer formation is an intrinsic property of Gml and mutant Gml proteins that are retained in the Golgi complex, but not of mutants that efficiently reach the plasma membrane. HeLa cells expressing Gml were metabolically labeled for 5 min, chased for the indicated times, solubilized, and immunoprecipitated with anti-VSV G antibody (Fig. 3) . HeLa cells expressing Gml or VSV G were metabolically radiolabeled for 5 min, and then chased for 0 or 60 rain, and microsomes prepared as described in Materials and Methods. On sucrose gradients, Gml solubilized from cytochalasin D-treated cells migrated as an SDS-sensitive oligomer (in the pellet), and VSV G trimerization was unaffected (data not shown).	./cache/cord-299281-5z1xminb.txt	./txt/cord-299281-5z1xminb.txt