PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17442311-3	2007	Here we show that misoxidised MHC class I heavy chains activate XBP1 processing in a similar manner to tunicamycin, with tunicamycin and dithiothreitol (DTT) inducing differential XBP1 processing.	Dithiothreitol	137-151	X-box binding protein 1	Homo sapiens	180-184	
29339455-10	2018	Dithiothreitol increased levels of the activated, spliced XBP1 in ERalpha (+) MCF-7 and T47D breast cancer cells but did not affect NAT1 or ESR1 expression.	Dithiothreitol	0-14	X-box binding protein 1	Homo sapiens	58-62	
27556805-9	2016	RESULTS: Proof of principle came in our results by the fact that the 26 nt non-conventional splice site in Xbp1 was detected as the top hit by our new RSR algorithm in heterozygote (Het) samples from both Thapsigargin (Tg) and Dithiothreitol (Dtt) treated experiments but absent in the negative control Ire1alpha knock-out (KO) samples.	Dithiothreitol	227-241	X-box binding protein 1	Homo sapiens	107-111	
27556805-9	2016	RESULTS: Proof of principle came in our results by the fact that the 26 nt non-conventional splice site in Xbp1 was detected as the top hit by our new RSR algorithm in heterozygote (Het) samples from both Thapsigargin (Tg) and Dithiothreitol (Dtt) treated experiments but absent in the negative control Ire1alpha knock-out (KO) samples.	Dithiothreitol	243-246	X-box binding protein 1	Homo sapiens	107-111	
24356728-0	2015	Unfolded protein response inducers tunicamycin and dithiothreitol promote myeloma cell differentiation mediated by XBP-1.	Dithiothreitol	51-65	X-box binding protein 1	Homo sapiens	115-120	
24356728-4	2015	Herein, we used low-dose pharmacological UPR inducers such as tunicamycin (TM) and dithiothreitol (DTT) to efficiently activate the IRE1-XBP-1 pathway in myeloma cells characterized by transcriptional expression increase in spliced XBP-1 and molecular chaperons, accompanied by significant differentiation and maturation of these myeloma cells, without concomitant cytotoxicity.	Dithiothreitol	83-97	X-box binding protein 1	Homo sapiens	137-142	
24356728-4	2015	Herein, we used low-dose pharmacological UPR inducers such as tunicamycin (TM) and dithiothreitol (DTT) to efficiently activate the IRE1-XBP-1 pathway in myeloma cells characterized by transcriptional expression increase in spliced XBP-1 and molecular chaperons, accompanied by significant differentiation and maturation of these myeloma cells, without concomitant cytotoxicity.	Dithiothreitol	83-97	X-box binding protein 1	Homo sapiens	232-237	
24356728-4	2015	Herein, we used low-dose pharmacological UPR inducers such as tunicamycin (TM) and dithiothreitol (DTT) to efficiently activate the IRE1-XBP-1 pathway in myeloma cells characterized by transcriptional expression increase in spliced XBP-1 and molecular chaperons, accompanied by significant differentiation and maturation of these myeloma cells, without concomitant cytotoxicity.	Dithiothreitol	99-102	X-box binding protein 1	Homo sapiens	137-142	
24356728-4	2015	Herein, we used low-dose pharmacological UPR inducers such as tunicamycin (TM) and dithiothreitol (DTT) to efficiently activate the IRE1-XBP-1 pathway in myeloma cells characterized by transcriptional expression increase in spliced XBP-1 and molecular chaperons, accompanied by significant differentiation and maturation of these myeloma cells, without concomitant cytotoxicity.	Dithiothreitol	99-102	X-box binding protein 1	Homo sapiens	232-237	
24356728-6	2015	Moreover, siRNA knockdown of XBP-1 disrupted TM- or DTT-induced myeloma cell differentiation and maturation.	Dithiothreitol	52-55	X-box binding protein 1	Homo sapiens	29-34	
17442311-3	2007	Here we show that misoxidised MHC class I heavy chains activate XBP1 processing in a similar manner to tunicamycin, with tunicamycin and dithiothreitol (DTT) inducing differential XBP1 processing.	Dithiothreitol	153-156	X-box binding protein 1	Homo sapiens	180-184