PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29743981-0	2018	Induction of NLRP3 Inflammasome Activation by Heme in Human Endothelial Cells.	Heme	46-50	NLR family pyrin domain containing 3	Homo sapiens	13-18	
29743981-11	2018	Our results identified endothelial cells as a target of heme-mediated NLRP3 activation that can contribute to the inflammation triggered by sterile hemolysis.	Heme	56-60	NLR family pyrin domain containing 3	Homo sapiens	70-75	
31091351-6	2019	Moreover, heme itself stimulated significant Mphi pro-IL-1beta gene and protein expression via an S100A8-mediated mechanism and greatly amplified S100A8-driven NLRP3 inflammasome-mediated IL-1beta secretion.	Heme	10-14	NLR family pyrin domain containing 3	Homo sapiens	160-165	
29743981-3	2018	Heme, released from RBCs, is a DAMP and induces IL-1beta production through the activation of the nucleotide-binding domain and leucine-rich repeat-containing family and pyrin domain containing 3 (NLRP3) in macrophages; however, other cellular targets of heme-mediated inflammasome activation were not investigated.	Heme	0-4	NLR family pyrin domain containing 3	Homo sapiens	197-202	
29743981-3	2018	Heme, released from RBCs, is a DAMP and induces IL-1beta production through the activation of the nucleotide-binding domain and leucine-rich repeat-containing family and pyrin domain containing 3 (NLRP3) in macrophages; however, other cellular targets of heme-mediated inflammasome activation were not investigated.	Heme	255-259	NLR family pyrin domain containing 3	Homo sapiens	197-202	
29743981-5	2018	We found that heme upregulated NLRP3 expression and induced active IL-1beta production in human umbilical vein endothelial cells (HUVECs).	Heme	14-18	NLR family pyrin domain containing 3	Homo sapiens	31-36	
29743981-8	2018	Unfettered production of reactive oxygen species played a critical role in heme-mediated NLRP3 activation.	Heme	75-79	NLR family pyrin domain containing 3	Homo sapiens	89-94	
29743981-9	2018	Activation of NLRP3 by heme required structural integrity of the heme molecule, as neither protoporphyrin IX nor iron-induced IL-1beta production.	Heme	23-27	NLR family pyrin domain containing 3	Homo sapiens	14-19	
29743981-9	2018	Activation of NLRP3 by heme required structural integrity of the heme molecule, as neither protoporphyrin IX nor iron-induced IL-1beta production.	Heme	65-69	NLR family pyrin domain containing 3	Homo sapiens	14-19	
27821769-2	2016	Heme has been described as a potent proinflammatory molecule that is able to induce multiple innate immune responses, such as those triggered by TLR4 and the NLRP3 inflammasome, as well as necroptosis in macrophages.	Heme	0-4	NLR family pyrin domain containing 3	Homo sapiens	158-163	
25225402-4	2014	We found that heme, but not porphyrins without iron, activated LPS-primed macrophages promoting the processing of IL-1beta dependent on nucleotide-binding domain and leucine rich repeat containing family, pyrin domain containing 3 (NLRP3).	Heme	14-18	NLR family pyrin domain containing 3	Homo sapiens	232-237	
25225402-5	2014	The activation of NLRP3 by heme required spleen tyrosine kinase, NADPH oxidase-2, mitochondrial reactive oxygen species, and K(+) efflux, whereas it was independent of heme internalization, lysosomal damage, ATP release, the purinergic receptor P2X7, and cell death.	Heme	27-31	NLR family pyrin domain containing 3	Homo sapiens	18-23