PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2753912-3	1989	The biosynthesis and turnover of lipoprotein lipase (LPL) have been investigated in adipose 3T3-F442A cells labeled with [35S]methionine.	Methionine	126-136	lipoprotein lipase	Mus musculus	33-51	
7593632-5	1995	Epinephrine induced a dose-dependent decrease in LPL synthesis using [35S]methionine incorporation, with no change in LPL mRNA levels, demonstrating translational regulation of LPL in this cell line.	Methionine	74-84	lipoprotein lipase	Mus musculus	49-52	
1831351-5	1991	Glycosylation of lipoprotein lipase was analysed by PAGE of endoglycosidase H (endo H)-digested subunits of lipoprotein lipase immunoprecipitated from cells incubated for 1-2 h with [35S]methionine.	Methionine	187-197	lipoprotein lipase	Mus musculus	17-35	
2104849-9	1990	Lipoprotein lipase immunoprecipitated from cells incubated 1-3 h with [35S]methionine was digested with or without endoglycosidase H (endo H) or F, and resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Methionine	75-85	lipoprotein lipase	Mus musculus	0-18	
2753912-3	1989	The biosynthesis and turnover of lipoprotein lipase (LPL) have been investigated in adipose 3T3-F442A cells labeled with [35S]methionine.	Methionine	126-136	lipoprotein lipase	Mus musculus	53-56	
3597377-2	1987	Immunoprecipitation of [35S]lipoprotein lipase from fat pads pulse-labeled with [35S]methionine showed a decrease in relative synthesis of the enzyme, which correlated to the decrease in activity.	Methionine	85-95	lipoprotein lipase	Mus musculus	28-46	
3491626-2	1986	The loss of activity reached a maximum of 60-70% of control and appeared to be due to an effect on the synthesis of the enzyme as judged by a suppression of the ability to incorporate [35S]methionine into immunoprecipitable lipoprotein lipase.	Methionine	189-199	lipoprotein lipase	Mus musculus	224-242