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