PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9182559-1	1997	Endopeptidase 24.16 or mitochondrial oligopeptidase, abbreviated here as EP 24.16 (MOP), is a thiol- and metal-dependent oligopeptidase that is found in multiple intracellular compartments in mammalian cells.	Metals	105-110	neurolysin	Homo sapiens	0-19	
33440488-8	2017	Building upon this work, here we report an engineered metal-chelation based method to dynamically regulate mechanical and physical properties of MEP-based protein hydrogels.	Metals	54-59	neurolysin	Homo sapiens	145-148	
33440488-9	2017	We engineered a bihistidine metal binding motif in the host domain of the MEP.	Metals	28-33	neurolysin	Homo sapiens	74-77	
33440488-11	2017	Thus, the bihistidine mutant can serve as a metal ion responsive-folding switch to regulate the conformational equilibrium of the MEP.	Metals	44-49	neurolysin	Homo sapiens	130-133	
33440488-14	2017	This dynamic change is due to the metal chelation-induced shift of the conformational equilibrium of the MEP and consequently the effective cross-linking density of the hydrogel.	Metals	34-39	neurolysin	Homo sapiens	105-108	
15647004-1	2005	Thimet oligopeptidase (TOP) is a soluble metalloendopeptidase belonging to a family of enzymes including neurolysin and neprilysin that utilize the HEXXH metal-binding motif.	Metals	41-46	neurolysin	Homo sapiens	105-115	
9182559-1	1997	Endopeptidase 24.16 or mitochondrial oligopeptidase, abbreviated here as EP 24.16 (MOP), is a thiol- and metal-dependent oligopeptidase that is found in multiple intracellular compartments in mammalian cells.	Metals	105-110	neurolysin	Homo sapiens	83-86