PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11466310-16	2001	Methionine synthase reductase reduces cytochrome c in an NADPH-dependent reaction at a rate (0.44 micromol min(-1) mg(-1) at 25 degrees C) that is comparable with that reported for NR1, a soluble dual flavoprotein of unknown function, but is approximately 100-fold slower than that of P-450 reductase.	NADP	57-62	NADPH dependent diflavin oxidoreductase 1	Homo sapiens	181-184	
15900210-6	2005	However, further analysis of NDOR1 revealed a polymorphic c.1564G>A transition (NDOR1*1), detected in 24/200 Caucasian and 1/49 Japanese individuals, producing a valine to isoleucine substitution at codon 522 in the NADPH binding region.	NADP	219-224	NADPH dependent diflavin oxidoreductase 1	Homo sapiens	29-34	
15900210-6	2005	However, further analysis of NDOR1 revealed a polymorphic c.1564G>A transition (NDOR1*1), detected in 24/200 Caucasian and 1/49 Japanese individuals, producing a valine to isoleucine substitution at codon 522 in the NADPH binding region.	NADP	219-224	NADPH dependent diflavin oxidoreductase 1	Homo sapiens	83-88	
15900210-8	2005	NDOR1_v1 showed a 10-fold decrease in affinity for NADPH, and a 90% reduction in ferricyanide reductase activity.	NADP	51-56	NADPH dependent diflavin oxidoreductase 1	Homo sapiens	0-5	
12871939-1	2003	A novel human cytosolic flavin reductase, Nr1, was recently described that contains FMN, FAD, and NADPH cofactors.	NADP	98-103	NADPH dependent diflavin oxidoreductase 1	Homo sapiens	42-45	
12871939-2	2003	Though the targets of the related NADPH-dependent flavoprotein reductases, cytochrome P450 reductase, methionine synthase reductase, and nitric oxide synthase, are known, the cellular function of Nr1 is not clear.	NADP	34-39	NADPH dependent diflavin oxidoreductase 1	Homo sapiens	196-199	
12631275-2	2003	The FAD/NADPH- and FMN-binding domains of NR1 have been expressed and purified and their redox properties studied by stopped-flow and steady-state kinetic methods, and by potentiometry.	NADP	8-13	NADPH dependent diflavin oxidoreductase 1	Homo sapiens	42-45	
12631275-3	2003	The midpoint reduction potentials of the oxidized/semiquinone (-315 +/- 5 mV) and semiquinone/dihydroquinone (-365 +/- 15 mV) couples of the FAD/NADPH domain are similar to those for the FAD/NADPH domain of human CPR, but the rate of hydride transfer from NADPH to the FAD/NADPH domain of NR1 is approximately 200-fold slower.	NADP	145-150	NADPH dependent diflavin oxidoreductase 1	Homo sapiens	289-292	
12631275-5	2003	Stopped-flow studies indicate that hydride transfer from the FAD/NADPH domain of NR1 to NADP+ is faster than hydride transfer in the physiological direction (NADPH to FAD), consistent with the measured reduction potentials of the FAD couples [midpoint potential for FAD redox couples is -340 mV, cf-320 mV for NAD(P)H].	NADP	65-70	NADPH dependent diflavin oxidoreductase 1	Homo sapiens	81-84	
12631275-5	2003	Stopped-flow studies indicate that hydride transfer from the FAD/NADPH domain of NR1 to NADP+ is faster than hydride transfer in the physiological direction (NADPH to FAD), consistent with the measured reduction potentials of the FAD couples [midpoint potential for FAD redox couples is -340 mV, cf-320 mV for NAD(P)H].	NADP	88-93	NADPH dependent diflavin oxidoreductase 1	Homo sapiens	81-84	
12631275-5	2003	Stopped-flow studies indicate that hydride transfer from the FAD/NADPH domain of NR1 to NADP+ is faster than hydride transfer in the physiological direction (NADPH to FAD), consistent with the measured reduction potentials of the FAD couples [midpoint potential for FAD redox couples is -340 mV, cf-320 mV for NAD(P)H].	NADP	158-163	NADPH dependent diflavin oxidoreductase 1	Homo sapiens	81-84