PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8132639-2	1994	We have proposed that cytidine monophospho-N-acetylneuraminic acid (CMP-NeuAc) hydroxylation is carried out by a multienzyme system involving CMP-NeuAc hydroxylase (the terminal enzyme of the system), cytochrome b5, and an NADH-dependent cytochrome b5-reducing factor (Kozutsumi, Y., Kawano, T., Yamakawa, T., and Suzuki, A.	Cytidine Monophosphate	68-71	cytochrome b5 type A (microsomal)	Mus musculus	201-214	
8132639-2	1994	We have proposed that cytidine monophospho-N-acetylneuraminic acid (CMP-NeuAc) hydroxylation is carried out by a multienzyme system involving CMP-NeuAc hydroxylase (the terminal enzyme of the system), cytochrome b5, and an NADH-dependent cytochrome b5-reducing factor (Kozutsumi, Y., Kawano, T., Yamakawa, T., and Suzuki, A.	Cytidine Monophosphate	68-71	cytochrome b5 type A (microsomal)	Mus musculus	238-251	
8056746-1	1994	We have proposed that CMP-N-acetylneuraminic acid (CMP-NeuAc) hydroxylation is mediated by an electron transport system consisting of cytochrome b5 (b5), b5 reducing factor(s), and CMP-NeuAc hydroxylase, all of which have been detected in the cytosolic fraction of mouse liver [Kozutsumi, Y., Kawano, T., Yamakawa, T., & Suzuki, A.	Cytidine Monophosphate	22-25	cytochrome b5 type A (microsomal)	Mus musculus	134-147	
1964451-0	1990	Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol.	Cytidine Monophosphate	34-37	cytochrome b5 type A (microsomal)	Mus musculus	17-30	
8358221-4	1993	The other fraction, which flowed through the column, was assumed to contain the terminal enzyme which accepts electrons from cytochrome b5, activates oxygen, and catalyses the hydroxylation of CMP-NeuAc.	Cytidine Monophosphate	193-196	cytochrome b5 type A (microsomal)	Mus musculus	125-138