PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25045021-1	2014	The mitochondrial amidoxime reducing component (mARC) is a molybdenum-containing enzyme and capable of reducing N-hydroxylated structures such as amidoxime prodrugs.	Nitrogen	112-113	activity regulated cytoskeletal-associated protein	Mus musculus	48-52	
29767695-9	2018	Finally, mARC, discovered less than a decade ago, works in concert with cytochrome b5 type B and NAD(H) cytochrome b5 reductase to reduce a variety of N-hydroxylated substrates, although the physiologic significance is still unclear.	Nitrogen	97-98	activity regulated cytoskeletal-associated protein	Mus musculus	9-13	
25045021-3	2014	All groups are reduced by mARC proteins, and the enzymes are therefore involved in the interconversion of N-oxygenated metabolites originating from cytochrome P450s and flavin-containing monooxygenases.	Nitrogen	106-107	activity regulated cytoskeletal-associated protein	Mus musculus	26-30	
22924387-0	2012	The mitochondrial Amidoxime Reducing Component (mARC) is involved in detoxification of N-hydroxylated base analogues.	Nitrogen	87-88	activity regulated cytoskeletal-associated protein	Mus musculus	48-52	
25144769-12	2014	With respect to high fat diet, changes in the mARC proteins occur that result in increased N-reductive activity.	Nitrogen	91-92	activity regulated cytoskeletal-associated protein	Mus musculus	46-50	
22924387-4	2012	Here, we demonstrate the reductive detoxification of toxic and mutagenic N-hydroxylated nucleobases and their corresponding nucleosides by the mammalian mARC-containing enzyme system.	Nitrogen	73-74	activity regulated cytoskeletal-associated protein	Mus musculus	153-157	
22924387-8	2012	On the basis of the high specific activities with N-hydroxylated base analogues relative to other N-hydroxylated substrates, our data suggest that mARC proteins might be involved in protecting cellular DNA from misincorporation of toxic N-hydroxylated base analogues during replication by converting them to the correct purine or pyrimidine bases, respectively.	Nitrogen	50-51	activity regulated cytoskeletal-associated protein	Mus musculus	147-151	
22924387-8	2012	On the basis of the high specific activities with N-hydroxylated base analogues relative to other N-hydroxylated substrates, our data suggest that mARC proteins might be involved in protecting cellular DNA from misincorporation of toxic N-hydroxylated base analogues during replication by converting them to the correct purine or pyrimidine bases, respectively.	Nitrogen	98-99	activity regulated cytoskeletal-associated protein	Mus musculus	147-151	
22924387-8	2012	On the basis of the high specific activities with N-hydroxylated base analogues relative to other N-hydroxylated substrates, our data suggest that mARC proteins might be involved in protecting cellular DNA from misincorporation of toxic N-hydroxylated base analogues during replication by converting them to the correct purine or pyrimidine bases, respectively.	Nitrogen	98-99	activity regulated cytoskeletal-associated protein	Mus musculus	147-151