PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9271078-6	1997	Cells that were Ca2+ depleted for 2 h slowly secreted an abnormal slightly smaller complex oligosaccharide form of alpha1-antitrypsin at approximately the same rate as the non-glycosylated protein generated by treatment with tunicamycin.	Tunicamycin	225-236	serpin family A member 1	Homo sapiens	115-133	
15845869-9	2005	Agents that perturb the synthesis and/or activity of ER chaperones such as tunicamycin and calcium ionophore A23187, have different effects on the solubility and degradation of alpha1-AT Z as well as on its residual secretion.	Tunicamycin	75-86	serpin family A member 1	Homo sapiens	177-186	
9854035-4	1999	Secretion of alpha1-antitrypsin, an unrelated N-glycoprotein, was also inhibited by monensin, BFA and tunicamycin, but not by CCCP, castanospermine or N-methyldeoxynojirimycin.	Tunicamycin	102-113	serpin family A member 1	Homo sapiens	13-31	
2580532-4	1985	For example, three glycoproteins are exported with rapid kinetics and secretion of only one, alpha 1-protease inhibitor, is inhibited by tunicamycin treatment.	Tunicamycin	137-148	serpin family A member 1	Homo sapiens	93-119	
8477700-6	1993	In addition, inhibition of PiM and PiZ alpha 1-AT glycosylation and secretion by tunicamycin did not result in the accumulation of the protein, but instead in its rapid lag-free degradation.	Tunicamycin	81-92	serpin family A member 1	Homo sapiens	39-49	
2111144-5	1990	Inhibition of de novo glycosylation by tunicamycin impaired the secretion of M-type alpha 1-antitrypsin by about 75% whereas inhibition of oligosaccharide processing by the mannosidase II inhibitor swainsonine did not alter the secretion of M-type alpha 1-antitrypsin.	Tunicamycin	39-50	serpin family A member 1	Homo sapiens	84-103	
2111144-7	1990	Even unglycosylated alpha 1-antitrypsin secreted by human monocytes treated with tunicamycin formed a complex with elastase.	Tunicamycin	81-92	serpin family A member 1	Homo sapiens	20-39	
2471524-1	1989	Previous studies in this laboratory (1) have shown that tunicamycin-treatment inhibits the secretion of three secretory glycoproteins--alpha 2-macroglobulin, ceruloplasmin, and alpha 1-protease inhibitor in human hepatoma (Hep G2) cell cultures.	Tunicamycin	56-67	serpin family A member 1	Homo sapiens	177-203	
2471524-3	1989	Using percoll density gradient centrifugation, we found that tunicamycin-treatment markedly inhibited the transport of alpha 2-macroglobulin, ceruloplasmin and alpha 1-protease inhibitor from the rough endoplasmic reticulum.	Tunicamycin	61-72	serpin family A member 1	Homo sapiens	160-186	
24743137-6	2014	Time-lapse confocal microscopy indicated that A1AT co-localized with Golgi in the endothelium whilst inhibition of the classical secretory pathway with tunicamycin significantly increased intracellular retention of A1AT.	Tunicamycin	152-163	serpin family A member 1	Homo sapiens	215-219	
6323296-3	1984	alpha 1-AT export to medium was delayed by tunicamycin, inhibited by cycloheximide but unaffected by colchicine.	Tunicamycin	43-54	serpin family A member 1	Homo sapiens	0-10	
6200362-4	1984	In the presence of tunicamycin an unglycosylated form of M alpha 1-antitrypsin appears in the incubation medium but no corresponding unglycosylated version of the Z protein is secreted.	Tunicamycin	19-30	serpin family A member 1	Homo sapiens	59-78