PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29746241-4	2018	However, in the two decades subsequent to the initial discovery, purification and in vitro analysis of bacterial MutYs and mammalian homologs, such as human MUTYH and mouse Mutyh, have demonstrated that proper Fe-S cluster coordination is required for OG:A substrate recognition and adenine excision.	Iron	210-214	mutY DNA glycosylase	Homo sapiens	157-162	
29746241-8	2018	The methods described herein have not only been leveraged to provide insight into the roles of the MutY Fe-S cluster but have also been provided crucial information needed to delineate the impact of inherited variants of the human homolog MUTYH associated with a colorectal cancer syndrome known as MUTYH-associated polyposis or MAP.	Iron	104-108	mutY DNA glycosylase	Homo sapiens	239-244	
29746241-9	2018	Notably, many MAP-associated variants have been found adjacent to the Fe-S cluster further underscoring the intimate relationship between the cofactor, MUTYH-mediated DNA repair, and disease.	Iron	70-74	mutY DNA glycosylase	Homo sapiens	152-157	
29746250-0	2018	Cellular Assays for Studying the Fe-S Cluster Containing Base Excision Repair Glycosylase MUTYH and Homologs.	Iron	33-37	mutY DNA glycosylase	Homo sapiens	90-95	
29746250-1	2018	Many DNA repair enzymes, including the human adenine glycosylase MUTYH, require iron-sulfur (Fe-S) cluster cofactors for DNA damage recognition and subsequent repair.	Iron	93-97	mutY DNA glycosylase	Homo sapiens	65-70	
33574380-10	2021	These findings suggest that MUTYH deficiency is associated with hepatocarcinogenesis in patients with NASH with hepatic iron accumulation.	Iron	120-124	mutY DNA glycosylase	Homo sapiens	28-33	
26377631-5	2015	P281L MUTYH was found to be severely compromised both in DNA binding and base excision activity, consistent with the location of this variation in the iron-sulfur cluster (FCL) DNA binding motif of MUTYH.	Iron	151-155	mutY DNA glycosylase	Homo sapiens	6-11	
26377631-5	2015	P281L MUTYH was found to be severely compromised both in DNA binding and base excision activity, consistent with the location of this variation in the iron-sulfur cluster (FCL) DNA binding motif of MUTYH.	Iron	151-155	mutY DNA glycosylase	Homo sapiens	198-203