PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26716738-4	2015	In addition, proposed amine oxidase activity of circulating extracellular renalase requires the presence of FAD, which has not been detected either in blood or urinary renalase.	Flavin-Adenine Dinucleotide	108-111	renalase, FAD dependent amine oxidase	Homo sapiens	74-82	
31657440-2	2019	They are known to be oxidized to NAD(P)+ by mammalian renalase, an FAD-linked enzyme mainly present in heart and kidney, and by related bacterial enzymes.	Flavin-Adenine Dinucleotide	67-70	renalase, FAD dependent amine oxidase	Homo sapiens	54-62	
31657440-10	2019	These findings indicate that two different classes of enzymes using either FAD (renalase) or FMN (PNPOs and PNPO-RPs) as a cofactor play an as yet unsuspected role in removing damaged forms of NAD(P).	Flavin-Adenine Dinucleotide	75-78	renalase, FAD dependent amine oxidase	Homo sapiens	80-88	
26817339-1	2015	Renalase is a newly-discovered enzyme--amine oxidase containing flavin adenine dinucleotide that determines its activity.	Flavin-Adenine Dinucleotide	64-91	renalase, FAD dependent amine oxidase	Homo sapiens	0-8	
26309615-4	2015	A common missense polymorphism in the flavin-adenine dinucleotide-binding domain of human renalase (Glu37Asp) has recently been described.	Flavin-Adenine Dinucleotide	38-65	renalase, FAD dependent amine oxidase	Homo sapiens	90-98	
23130169-5	2012	METHODS AND RESULTS: Using in vitro enzymatic assays and in vivo administration of recombinant renalase, we show that the protein functions as a flavin adenine dinucleotide- and nicotinamide adenine dinucleotide-dependent oxidase that lowers blood pressure by degrading plasma epinephrine.	Flavin-Adenine Dinucleotide	145-172	renalase, FAD dependent amine oxidase	Homo sapiens	95-103	
25567503-1	2014	Renalase was described in 2005 as a new flavoprotein expressed mainly in the kidney that functions as a flavin adenine dinucleotide (FAD)- and nicotinamide adenine dinucleotide (NADH)-dependent amine oxidase.	Flavin-Adenine Dinucleotide	104-131	renalase, FAD dependent amine oxidase	Homo sapiens	0-8	
25567503-1	2014	Renalase was described in 2005 as a new flavoprotein expressed mainly in the kidney that functions as a flavin adenine dinucleotide (FAD)- and nicotinamide adenine dinucleotide (NADH)-dependent amine oxidase.	Flavin-Adenine Dinucleotide	133-136	renalase, FAD dependent amine oxidase	Homo sapiens	0-8	
24923329-3	2014	A common missense polymorphism in the flavin-adenine dinucleotide-binding domain of human renalase (Glu37Asp) has been described.	Flavin-Adenine Dinucleotide	38-65	renalase, FAD dependent amine oxidase	Homo sapiens	90-98	
21699903-0	2011	FAD-binding site and NADP reactivity in human renalase: a new enzyme involved in blood pressure regulation.	Flavin-Adenine Dinucleotide	0-3	renalase, FAD dependent amine oxidase	Homo sapiens	46-54	
21699903-4	2011	Renalase adopts the p-hydroxybenzoate hydroxylase fold topology, comprising a Rossmann-fold-based flavin adenine dinucleotide (FAD)-binding domain and a putative substrate-binding domain, the latter of which contains a five-stranded anti-parallel beta-sheet.	Flavin-Adenine Dinucleotide	98-125	renalase, FAD dependent amine oxidase	Homo sapiens	0-8	
21699903-4	2011	Renalase adopts the p-hydroxybenzoate hydroxylase fold topology, comprising a Rossmann-fold-based flavin adenine dinucleotide (FAD)-binding domain and a putative substrate-binding domain, the latter of which contains a five-stranded anti-parallel beta-sheet.	Flavin-Adenine Dinucleotide	127-130	renalase, FAD dependent amine oxidase	Homo sapiens	0-8	
21073414-3	2010	Special attention is paid to unsolved and questionable problems including: 1) prediction of the presence of FAD in the protein structure based on amino acid sequence similarity of renalase with known FAD-dependent enzymes; 2) identity of plasma and urinary renalase; 3) mechanism underlying conversion of inactive renalase into the active form.	Flavin-Adenine Dinucleotide	108-111	renalase, FAD dependent amine oxidase	Homo sapiens	180-188	
22227817-3	2012	It had been proposed that renalase had a flavin adenine dinucleotide (FAD)-binding domain and that FAD was an essential cofactor for its stability and monoamine oxidase activity.	Flavin-Adenine Dinucleotide	41-68	renalase, FAD dependent amine oxidase	Homo sapiens	26-34	
22227817-3	2012	It had been proposed that renalase had a flavin adenine dinucleotide (FAD)-binding domain and that FAD was an essential cofactor for its stability and monoamine oxidase activity.	Flavin-Adenine Dinucleotide	70-73	renalase, FAD dependent amine oxidase	Homo sapiens	26-34	
20975995-2	2010	A common missense polymorphism in the flavin-adenine dinucleotide-binding domain of human renalase (Glu37Asp) has recently been described.	Flavin-Adenine Dinucleotide	38-65	renalase, FAD dependent amine oxidase	Homo sapiens	90-98