PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24659529-6	2014	To improve the activity, the other five Cys residues (C2, C78, C115, C156, C202) were mutated to serine (Ser) in one hGPx1 molecule.	Serine	97-103	glutathione peroxidase 1	Homo sapiens	117-122	
33517969-13	2021	WB result showed that serine had a synergistic effect on GPx1 and SEPP expressions as SeMet concentration was 0.	Serine	22-28	glutathione peroxidase 1	Homo sapiens	57-61	
33517969-16	2021	Secondly, serine had a synergistic effect on GPx1 and SEPP expressions of SeMet in hepatocyte(L02).	Serine	10-16	glutathione peroxidase 1	Homo sapiens	45-49	
24093966-4	2014	Cys residues in hGPx1 were mutated to Ser in turn because untargeted substitution of Sec in place of Cys resulted in the decline of recombinant selenoenzyme activity.	Serine	38-41	glutathione peroxidase 1	Homo sapiens	16-21	
24093966-6	2014	Seleno-hGPx1-C2/78/115/156/202S with all Cys residues changed to Ser showed the highest activity (21,268 U/mumol), which was more than 10-fold higher than bovine liver GPx.	Serine	65-68	glutathione peroxidase 1	Homo sapiens	7-12	
15208449-7	2004	tRNA([Ser]Sec) was found to be limiting for UGA translation under conditions of high selenoprotein mRNA in both a transient reporter assay and in cells with elevated GPx-1 mRNA.	Serine	6-9	glutathione peroxidase 1	Homo sapiens	166-171	
24659529-6	2014	To improve the activity, the other five Cys residues (C2, C78, C115, C156, C202) were mutated to serine (Ser) in one hGPx1 molecule.	Serine	105-108	glutathione peroxidase 1	Homo sapiens	117-122