PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16620812-2	2006	We demonstrate herein that TGase is functionally active in Leishmania parasites by using labeled polyamine that becomes conjugated into protein substrates.	Polyamines	97-106	transglutaminase 1	Homo sapiens	27-32	
25399055-7	2015	Here we present some PCD plant models, focusing on the role of the enzyme responsible for PA conjugation to proteins: transglutaminase (TGase), an enzyme linked with the process of PCD also in some animal models.	Polyamines	90-92	transglutaminase 1	Homo sapiens	118-134	
25399055-7	2015	Here we present some PCD plant models, focusing on the role of the enzyme responsible for PA conjugation to proteins: transglutaminase (TGase), an enzyme linked with the process of PCD also in some animal models.	Polyamines	90-92	transglutaminase 1	Homo sapiens	136-141	
27101214-2	2016	The best-known TGase activity, namely the transamidation of specific proteins by polyamines (PAs), has been studied in plants to verify if TGase is a mediator of PAs mechanism of action to re-interpret some of PAs effects.	Polyamines	81-91	transglutaminase 1	Homo sapiens	15-20	
27101214-2	2016	The best-known TGase activity, namely the transamidation of specific proteins by polyamines (PAs), has been studied in plants to verify if TGase is a mediator of PAs mechanism of action to re-interpret some of PAs effects.	Polyamines	81-91	transglutaminase 1	Homo sapiens	139-144	
20441570-4	2010	The secreted pollen TGase catalysed the cross-linking of both PAs (polyamines) into proteins (released by the pollen tube) and His6-Xpr-GFP into endogenous or exogenously added substrates.	Polyamines	62-65	transglutaminase 1	Homo sapiens	20-25	
20441570-4	2010	The secreted pollen TGase catalysed the cross-linking of both PAs (polyamines) into proteins (released by the pollen tube) and His6-Xpr-GFP into endogenous or exogenously added substrates.	Polyamines	67-77	transglutaminase 1	Homo sapiens	20-25	
16368535-2	2006	A previous study showed that transglutaminase (TGase) 2 catalyzes the incorporation of polyamines into HPV 18 E7 protein, and thereby diminishes its ability to bind Rb.	Polyamines	87-97	transglutaminase 1	Homo sapiens	47-52	
14529493-0	2003	Inhibitory and promotive effects of polyamines on transglutaminase-induced protein polymerization.	Polyamines	36-46	transglutaminase 1	Homo sapiens	50-66	
14529493-2	2003	We examined the effects of polyamines on TGase activity.	Polyamines	27-37	transglutaminase 1	Homo sapiens	41-46	
14529493-5	2003	These results suggested polyamines played two distinct roles as inhibitor and promoter for TGase-catalyzed protein polymerization.	Polyamines	24-34	transglutaminase 1	Homo sapiens	91-96	
12962330-2	2003	Histones are substrates for transglutaminase (TGase), and polymerized histone and polyamine binding histone have been suggested to play important roles in nucleus.	Polyamines	82-91	transglutaminase 1	Homo sapiens	28-44	
12962330-2	2003	Histones are substrates for transglutaminase (TGase), and polymerized histone and polyamine binding histone have been suggested to play important roles in nucleus.	Polyamines	82-91	transglutaminase 1	Homo sapiens	46-51	
12962330-3	2003	We examined whether histone polymerization catalyzed by TGase was influenced by polyamines such as putrescine (PUT), spermidine (SPD), and spermine (SPM).	Polyamines	80-90	transglutaminase 1	Homo sapiens	56-61	
11697888-0	2001	Transglutaminase activity is involved in polyamine-induced programmed cell death.	Polyamines	41-50	transglutaminase 1	Homo sapiens	0-16	
11697888-7	2001	Inhibitors of polyamine oxidation or inhibitors of TGase activity prevented polyamine-induced apoptosis.	Polyamines	76-85	transglutaminase 1	Homo sapiens	51-56	
11697888-8	2001	Moreover, tissue TGase overexpression significantly increased cell sensitivity to polyamine, suggesting that this effect is likely related to enhanced intracellular TGase activity.	Polyamines	82-91	transglutaminase 1	Homo sapiens	17-22	
11697888-8	2001	Moreover, tissue TGase overexpression significantly increased cell sensitivity to polyamine, suggesting that this effect is likely related to enhanced intracellular TGase activity.	Polyamines	82-91	transglutaminase 1	Homo sapiens	165-170	
11697888-9	2001	These data indicate that polyamines may modulate cell viability through a novel TGase-dependent process.	Polyamines	25-35	transglutaminase 1	Homo sapiens	80-85