PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28774660-1	2017	Iodotyrosine deiodinase (IYD) is unusual for its reliance on flavin to promote reductive dehalogenation under aerobic conditions.	4,6-dinitro-o-cresol	61-67	iodotyrosine deiodinase	Homo sapiens	0-23	
30052294-3	2019	The co-crystal of F-Tyr and a T239A variant of human IYD have now been characterized to provide a structural basis for control of its flavin reactivity.	4,6-dinitro-o-cresol	134-140	iodotyrosine deiodinase	Homo sapiens	53-56	
30052294-6	2019	Even substitution of Thr with Ser decreases the midpoint potential of human IYD between its oxidized and semiquinone forms of flavin by almost 80 mV.	4,6-dinitro-o-cresol	126-132	iodotyrosine deiodinase	Homo sapiens	76-79	
28774660-1	2017	Iodotyrosine deiodinase (IYD) is unusual for its reliance on flavin to promote reductive dehalogenation under aerobic conditions.	4,6-dinitro-o-cresol	61-67	iodotyrosine deiodinase	Homo sapiens	25-28	
26151430-4	2015	Time-dependent quenching of flavin fluorescence was used to monitor halotyrosine association to IYD.	4,6-dinitro-o-cresol	28-34	iodotyrosine deiodinase	Homo sapiens	96-99	
19436071-6	2009	Substrate coordination to IYD induces formation of an additional helix and coil that act as an active site lid to shield the resulting substrate.flavin complex from solvent.	4,6-dinitro-o-cresol	145-151	iodotyrosine deiodinase	Homo sapiens	26-29