PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22244833-10	2012	The affinity of FAD for the oxidase and the stability of the active complex were remarkably low when Noxa1 and Noxo1 were used compared with p67(phox) and p47(phox).	Flavin-Adenine Dinucleotide	16-19	CD33 molecule	Homo sapiens	141-144	
22244833-10	2012	The affinity of FAD for the oxidase and the stability of the active complex were remarkably low when Noxa1 and Noxo1 were used compared with p67(phox) and p47(phox).	Flavin-Adenine Dinucleotide	16-19	CD33 molecule	Homo sapiens	145-149	
22244833-10	2012	The affinity of FAD for the oxidase and the stability of the active complex were remarkably low when Noxa1 and Noxo1 were used compared with p67(phox) and p47(phox).	Flavin-Adenine Dinucleotide	16-19	CD33 molecule	Homo sapiens	159-163	
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.	Flavin-Adenine Dinucleotide	68-71	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.	Flavin-Adenine Dinucleotide	68-71	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.	Flavin-Adenine Dinucleotide	195-198	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.	Flavin-Adenine Dinucleotide	195-198	CD33 molecule	Homo sapiens	35-39