PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24165164-7	2014	Furthermore, ability to inhibit both MAO-A and MAO-B can be potentialized by the formation of hydrogen bonds between these compounds and FAD and/or the residues in the active site.	Hydrogen	94-102	monoamine oxidase A	Homo sapiens	37-42	
32970293-4	2021	The most potent inhibitor was a 1-tetralone derivative (1h) with IC50 values of 0.036 and 0.0011 microM for MAO-A and MAO-B, respectively.	Hydrogen	56-58	monoamine oxidase A	Homo sapiens	108-113	
31271801-8	2019	Docking simulations showed binding affinities of compounds 1 to 5 for hMAO-B were higher than those for hMAO-A or AChE and suggested these five chalcones form hydrogen bonds with MAO-B at Cys172 but that they do not form hydrogen bonds with hMAO-A or AChE.	Hydrogen	159-167	monoamine oxidase A	Homo sapiens	104-110	
30167931-8	2018	Some structural features are highly conserved in the two isozymes, such as a Tyr-Tyr aromatic sandwich in front of the flavin ring and a Lys residue hydrogen-bonded to the cofactor N5 atom, whereas a pair of gating residues (Phe208/Ile335 in MAO A; Ile199/Tyr326 in MAO B) specifically determines the different substrate and inhibitor properties of the two enzymes.	Hydrogen	149-157	monoamine oxidase A	Homo sapiens	242-247	
29925480-6	2018	Docking simulation implied that Cys323 and Tyr444 of MAO-A are key residues for hydrogen-bond interaction with chelerythrine.	Hydrogen	80-88	monoamine oxidase A	Homo sapiens	53-58	
34682298-6	2021	The relative tight binding might result from a hydrogen bond interaction of the three compounds with a Tyr444 residue in hMAO-A, whereas no hydrogen bond interaction was proposed in hMAO-B.	Hydrogen	47-55	monoamine oxidase A	Homo sapiens	121-127	
31795294-0	2019	Path Integral Calculation of the Hydrogen/Deuterium Kinetic Isotope Effect in Monoamine Oxidase A-Catalyzed Decomposition of Benzylamine.	Hydrogen	33-41	monoamine oxidase A	Homo sapiens	78-97	
31795294-3	2019	In this work, we focus on MAO A-catalyzed benzylamine decomposition in order to elucidate nuclear quantum effects through the calculation of the hydrogen/deuterium (H/D) kinetic isotope effect.	Hydrogen	145-153	monoamine oxidase A	Homo sapiens	26-31	
30686752-7	2019	Docking simulations also implied that 6 interacted with hMAO-A at Phe208 and with hMAO-B at Ile199 by carbon hydrogen bondings.	Hydrogen	109-117	monoamine oxidase A	Homo sapiens	56-62	
28251489-8	2017	Molecular docking simulation predicted that eckol and dieckol exhibit higher binding affinity towards hMAO-A and hMAO-B through hydrogen bonding and hydrophobic interactions.	Hydrogen	128-136	monoamine oxidase A	Homo sapiens	102-108	
28109809-8	2017	Molecular docking simulation revealed that 4 interacts with Asn181 residue of MAO-A or Asn116 residue of MAO-B by formation of hydrogen bond.	Hydrogen	127-135	monoamine oxidase A	Homo sapiens	78-83	
25541201-4	2015	Molecular docking showed that compounds 7h and 12c were nicely bound to hMAO-A via two hydrogen bonds (SER209, GLU216), one Pi-Pi interaction and three hydrogen bonds (SER209, GLU216, TYR69), one Sigma-Pi interaction, respectively.	Hydrogen	87-95	monoamine oxidase A	Homo sapiens	72-78	
25541201-4	2015	Molecular docking showed that compounds 7h and 12c were nicely bound to hMAO-A via two hydrogen bonds (SER209, GLU216), one Pi-Pi interaction and three hydrogen bonds (SER209, GLU216, TYR69), one Sigma-Pi interaction, respectively.	Hydrogen	152-160	monoamine oxidase A	Homo sapiens	72-78	
20410615-4	2010	Docking studies show that the imine moiety is located in hydrophobic pocket, bringing the propargyl group close to FAD which indicates that the different inhibitory potency toward MAO-A may be ascribable to both the distance between alkynyl group and N5 of FAD, and hydrogen bonding interactions between inhibitors and enzymes.	Hydrogen	266-274	monoamine oxidase A	Homo sapiens	180-185