PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20837928-8	2010	In SVGs exposed to atorvastatin ex vivo, without exposure to LDL, basal and NADPH-stimulated O(2)( -) were significantly reduced (P<0.01 for both concentrations versus 0 mumol/L) in association with a striking reduction in Rac1 activation and 1 membrane-bound Rac1 and p67(phox) subunit.	NADP	76-81	CD33 molecule	Homo sapiens	272-275	
22907303-6	2012	Western blot was used to analyze the expression levels of xanthine oxidase (XOD), manganese-superoxide dismutase (Mn-SOD) and the subunits p67(phox) of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase in the HUVECs.	NADP	152-195	CD33 molecule	Homo sapiens	139-142	
20679349-8	2010	Furthermore, the Y198A/V204A or L199A/V204A substitution leads to not only a complete loss of the activity of the reconstituted oxidase system but also a significant decrease in p67(phox) interaction with the gp91(phox) NADPH-binding domain, although these mutations affect neither the protein integrity nor the Rac binding activity.	NADP	220-225	CD33 molecule	Homo sapiens	178-181	
20679349-8	2010	Furthermore, the Y198A/V204A or L199A/V204A substitution leads to not only a complete loss of the activity of the reconstituted oxidase system but also a significant decrease in p67(phox) interaction with the gp91(phox) NADPH-binding domain, although these mutations affect neither the protein integrity nor the Rac binding activity.	NADP	220-225	CD33 molecule	Homo sapiens	182-186	
21954286-7	2012	p67(phox) is involved in the regulation of electron flow from NADPH to oxygen, leading to superoxide radical formation inside the phagosome.	NADP	62-67	CD33 molecule	Homo sapiens	0-3	
20679349-2	2010	The membrane-integrated protein gp91(phox) serves as the catalytic core, because it contains a complete electron-transporting apparatus from NADPH to molecular oxygen for superoxide production.	NADP	141-146	CD33 molecule	Homo sapiens	37-41	
15271797-5	2004	These events appear to be regulated by intracellular oxidant production through endothelial NAD(P)H (nicotinamide adenine dinucleotide phosphate) oxidase because antioxidants and expression of a transdominant inhibitor of the NADPH oxidase, p67(V204A), effectively blocked the effects of TNF on all 3 parameters of junctional integrity.	NADP	92-99	CD33 molecule	Homo sapiens	241-244	
17969555-15	2007	Binding of p67-phox to cytochrome b558 induces a gradual conformational change of cytochrome b558, which then becomes capable of transferring electrons produced in the cytoplasm from NADPH to oxygen, reducing the latter to O2-.	NADP	183-188	CD33 molecule	Homo sapiens	11-14	
9774399-3	1998	gp91(phox) is considered to be a flavocytochrome that contains binding sites for NADPH, FAD, as well as heme.	NADP	81-86	CD33 molecule	Homo sapiens	5-9	
10438466-0	1999	The p67(phox) activation domain regulates electron flow from NADPH to flavin in flavocytochrome b(558).	NADP	61-66	CD33 molecule	Homo sapiens	4-13	
10438466-14	1999	The calculated K(d) for NADPH was 40 microM in the presence of wild type p67(phox) and was approximately 55 microM using the weakly activating p67(phox)(V205A).	NADP	24-29	CD33 molecule	Homo sapiens	73-82	
10438466-14	1999	The calculated K(d) for NADPH was 40 microM in the presence of wild type p67(phox) and was approximately 55 microM using the weakly activating p67(phox)(V205A).	NADP	24-29	CD33 molecule	Homo sapiens	73-76	
10438466-14	1999	The calculated K(d) for NADPH was 40 microM in the presence of wild type p67(phox) and was approximately 55 microM using the weakly activating p67(phox)(V205A).	NADP	24-29	CD33 molecule	Homo sapiens	77-81	
10438466-15	1999	Thus, the activation domain of p67(phox) regulates the reduction of FAD but has only a small effect on NADPH binding, consistent with a dominant effect on hydride/electron transfer from NADPH to FAD.	NADP	103-108	CD33 molecule	Homo sapiens	31-34	
10438466-15	1999	Thus, the activation domain of p67(phox) regulates the reduction of FAD but has only a small effect on NADPH binding, consistent with a dominant effect on hydride/electron transfer from NADPH to FAD.	NADP	103-108	CD33 molecule	Homo sapiens	35-39	
10438466-15	1999	Thus, the activation domain of p67(phox) regulates the reduction of FAD but has only a small effect on NADPH binding, consistent with a dominant effect on hydride/electron transfer from NADPH to FAD.	NADP	186-191	CD33 molecule	Homo sapiens	31-34	
10438466-15	1999	Thus, the activation domain of p67(phox) regulates the reduction of FAD but has only a small effect on NADPH binding, consistent with a dominant effect on hydride/electron transfer from NADPH to FAD.	NADP	186-191	CD33 molecule	Homo sapiens	35-39	
12483106-2	2003	Rac-GTP is a component of the membrane-assembled NADPH oxidase complex, and new evidence suggests that Rac-GTP interacts directly with the oxidase flavocytochrome, in addition to binding to the regulatory p67 subunit, to regulate electron transfer both independently and cooperatively from NADPH to molecular oxygen.	NADP	49-54	CD33 molecule	Homo sapiens	205-208	
9148950-1	1997	The elicitation of an oxidative burst in phagocytes rests on the assembly of a multicomponental complex (NADPH oxidase) consisting of a membrane-associated flavocytochrome (cytochrome b559), representing the redox element responsible for the NADPH-dependent reduction of oxygen to superoxide (O-2), two cytosolic components (p47(phox), p67(phox)), and the small GTPase Rac (1 or 2).	NADP	105-110	CD33 molecule	Homo sapiens	336-339	
9228059-4	1997	Mutually facilitated binding (EC50) of Rac1 and p67(phox) within the NADPH oxidase complex was demonstrated using steady state kinetic methods measuring NADPH-dependent superoxide generation.	NADP	69-74	CD33 molecule	Homo sapiens	48-51	
8961931-1	1996	NADPH-dependent superoxide generation can be reconstituted in a cell-free system using recombinant cytosolic factors (p47-phox, p67-phox, and Rac) plus flavocytochrome b558.	NADP	0-5	CD33 molecule	Homo sapiens	128-131	
2159023-6	1990	In the cell-free oxidase-activating system, the ability of the p67-phox-deficient cytosol to support oxidase activation was partly restored by the addition of p47-phox-deficient cytosol; the p67-phox-deficient cytosol, however, was not complemented by cytosol inactivated with NADPH dialdehyde, an affinity label previously found to block the NADPH-binding component of the oxidase.	NADP	277-282	CD33 molecule	Homo sapiens	63-66	
8939991-1	1996	The superoxide (O-2)-generating NADPH oxidase of phagocytes is a multicomponent complex consisting of a membrane-associated flavocytochrome (cytochrome b559), bearing the NADPH binding site and two redox centers (FAD and heme) and three cytosolic activating components: p47(phox), p67(phox), and the small GTPase Rac (1 or 2).	NADP	32-37	CD33 molecule	Homo sapiens	274-278	
8939991-1	1996	The superoxide (O-2)-generating NADPH oxidase of phagocytes is a multicomponent complex consisting of a membrane-associated flavocytochrome (cytochrome b559), bearing the NADPH binding site and two redox centers (FAD and heme) and three cytosolic activating components: p47(phox), p67(phox), and the small GTPase Rac (1 or 2).	NADP	32-37	CD33 molecule	Homo sapiens	281-284	
8939991-1	1996	The superoxide (O-2)-generating NADPH oxidase of phagocytes is a multicomponent complex consisting of a membrane-associated flavocytochrome (cytochrome b559), bearing the NADPH binding site and two redox centers (FAD and heme) and three cytosolic activating components: p47(phox), p67(phox), and the small GTPase Rac (1 or 2).	NADP	32-37	CD33 molecule	Homo sapiens	285-289