PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34079010-6	2021	Hence, although levels of spliced XBP1 and CHOP mRNA and ATF4 protein increase with Ipom-F, the accompanying increase in the levels of ER lumenal BiP and GRP94 seen with tunicamycin are not observed.	Tunicamycin	170-181	heat shock protein 90 beta family member 1	Homo sapiens	154-159	
1506413-2	1992	Expression of the glucose regulated proteins (GRP78 and GRP94) is greatly increased after cells are exposed to stress agents (including A23187 and tunicamycin) which inhibit ER function.	Tunicamycin	147-158	heat shock protein 90 beta family member 1	Homo sapiens	56-61	
28841673-2	2017	We demonstrated the induction of ER stress in response to tunicamycin stimulation, as evidenced by increased expression of chaperone proteins Grp78, Grp94, and enhanced eukaryotic initiation factor 2 subunit 1 (eIF2alpha) phosphorylation in hepatocellular carcinoma cells.	Tunicamycin	58-69	heat shock protein 90 beta family member 1	Homo sapiens	149-154	
31894252-7	2020	Subsequent to experimentally inducing ER stress in AGR2vH-overexpressing CCA cells using tunicamycin, the UPR pathway was activated by the upregulation of UPR marker genes (activating transcription factor 6, eukaryotic initiation factor 2a and spliced X-box binding protein 1), UPR proteins [binding immunoglobulin protein/glucose-regulated protein (GRP)78 kDa and phosphorylated eukaryotic translation initiation factor 2a] and UPR downstream targets (GRP94).	Tunicamycin	89-100	heat shock protein 90 beta family member 1	Homo sapiens	453-458	
24146856-9	2013	The ER-stress inducer tunicamycin increased gp96-expression in a concentration- and time-dependent manner.	Tunicamycin	22-33	heat shock protein 90 beta family member 1	Homo sapiens	44-48	
28011957-11	2016	Tunicamycin treatment, as expected, increased the expression of Grp94, PDI, CHOP and inactivated PARP.	Tunicamycin	0-11	heat shock protein 90 beta family member 1	Homo sapiens	64-69	
25881988-7	2015	Tunicamycin treatment increased (P < 0.01) and TUDCA treatment decreased (P < 0.01) the expression level of ER chaperones, GRP78 and GRP94.	Tunicamycin	0-11	heat shock protein 90 beta family member 1	Homo sapiens	139-144	
21527262-4	2011	Time-dependent induction of the ER chaperones, glucose-regulated protein (GRP) 78 and GRP94, was observed after treatment with tunicamycin (TM) (80 mug/mL).	Tunicamycin	127-138	heat shock protein 90 beta family member 1	Homo sapiens	86-91	
21527262-4	2011	Time-dependent induction of the ER chaperones, glucose-regulated protein (GRP) 78 and GRP94, was observed after treatment with tunicamycin (TM) (80 mug/mL).	Tunicamycin	140-142	heat shock protein 90 beta family member 1	Homo sapiens	86-91	
18029041-2	2008	A time-dependent induction of ER chaperons, glucose regulated protein (GRP)78 and GRP94, was observed after treatment with tunicamycin (TM), and cell death was also induced concomitantly in both cells.	Tunicamycin	123-134	heat shock protein 90 beta family member 1	Homo sapiens	82-87	
15572843-9	2004	The tunicamycin-induced up-regulation of GRP78 and GRP94 and phosphorylation of PERK was suppressed by treatment with 4-PBA, indicating that 4-PBA suppresses ER stress responses by decreasing unfolded protein.	Tunicamycin	4-15	heat shock protein 90 beta family member 1	Homo sapiens	51-56	
10424404-6	1999	Interestingly, while the majority of the breast cancer cell lines can respond to tunicamycin- and thapsigargin-induced stress by increasing the steady state levels of grp94 and grp78 transcripts, the induction at the GRP protein level is variable and does not always correspond with the transcript level.	Tunicamycin	81-92	heat shock protein 90 beta family member 1	Homo sapiens	167-172