PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31265934-7	2019	Molecular modeling studies into the human MAO-B enzyme-binding site supported by a HYDE analysis suggested that the imine linker similarly contributes to the total binding energy in methanimines 17-22 as the amide spacer in their carboxamide analogs 11-16.	Imines	116-121	monoamine oxidase B	Homo sapiens	42-47	
27010708-3	2016	Recently, we demonstrated that the rate-limiting step of MAO B catalyzed conversion of amines into imines represents the hydride anion transfer from the substrate alpha-CH2 group to the N5 atom of the flavin cofactor moiety.	Imines	99-105	monoamine oxidase B	Homo sapiens	57-62