PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23153812-4 2012 The substituent on the alpha-carbon to the N1-hydrazine moiety (methyl or hydrogen) had a great influence on the activity and hMAO-B selectivity. Carbon 29-35 monoamine oxidase B Homo sapiens 126-132 19053775-6 2008 The X-ray crystal structure of the mofegiline-MAO-B adduct shows a covalent bond between the flavin cofactor N(5) with the distal allylamine carbon atom as well as the absence of the fluorine atom. Carbon 141-147 monoamine oxidase B Homo sapiens 46-51 18713667-5 2008 The behavior of the tert-butoxyl radical mediated oxidation of MPTP contrasts with this reaction as catalyzed by monoamine oxidase B (MAO-B) that occurs selectively at the allylic alpha-carbon. Carbon 186-192 monoamine oxidase B Homo sapiens 113-132 18713667-5 2008 The behavior of the tert-butoxyl radical mediated oxidation of MPTP contrasts with this reaction as catalyzed by monoamine oxidase B (MAO-B) that occurs selectively at the allylic alpha-carbon. Carbon 186-192 monoamine oxidase B Homo sapiens 134-139 12214665-2 2002 The initial step in the overall reaction is the two-electron ring alpha-carbon oxidation to give the 1-methyl-4-phenyl-2,3-dihydropyridinium species, a reaction that is catalyzed by monoamine oxidase B. Carbon 72-78 monoamine oxidase B Homo sapiens 182-201 18313306-2 2008 The two stereocenters present in this compound provide an opportunity to examine the enantioselectivity and diastereoselectivity of the MAO-B-catalyzed ring alpha-carbon oxidation of cyclic tertiary amines to give the corresponding conjugated iminiumyl metabolites. Carbon 163-169 monoamine oxidase B Homo sapiens 136-141 7548753-2 1995 This behavior led us to speculate that the pathway for the MAO-B catalyzed oxidation of these tetrahydropyridines may not necessarily proceed via an initial single electron transfer step as proposed by others but rather through an initial alpha-carbon hydrogen atom abstraction step. Carbon 245-251 monoamine oxidase B Homo sapiens 59-64 9313858-1 1997 The MAO-B catalyzed alpha-carbon oxidation of amines has been proposed to proceed via either a single electron transfer (SET) or hydrogen atom transfer (HAT) pathway. Carbon 26-32 monoamine oxidase B Homo sapiens 4-9 9568282-1 1998 Two catalytic pathways have been proposed for the flavoenzyme monoamine oxidase B (MAO-B)--one based on an initial single electron transfer (SET) step from the nitrogen lone pair and the second based on an initial alpha-carbon hydrogen atom transfer (HAT) step. Carbon 220-226 monoamine oxidase B Homo sapiens 62-81 9568282-1 1998 Two catalytic pathways have been proposed for the flavoenzyme monoamine oxidase B (MAO-B)--one based on an initial single electron transfer (SET) step from the nitrogen lone pair and the second based on an initial alpha-carbon hydrogen atom transfer (HAT) step. Carbon 220-226 monoamine oxidase B Homo sapiens 83-88 9879512-5 1998 The analogues in which the oxygen atom is closest to the alpha-carbon (9 and 10) inactivate MAO B, but activity slowly returns with time. Carbon 63-69 monoamine oxidase B Homo sapiens 92-97 9377092-1 1997 The monoamine oxidases A and B (MAO-A and MAO-B) catalyze the alpha-carbon oxidation of a variety of 4-substituted 1-methyl-1,2,3,6-tetrahydropyridine derivatives to yield the corresponding 2,3-dihydropyridinium species. Carbon 68-74 monoamine oxidase B Homo sapiens 42-47 7931241-11 1994 In the case of MAO-B inhibition, the 2 and 3 carbon-chain compounds had similar inhibitory potencies but this increased substantially when the chain length was increased to 4 carbons. Carbon 45-51 monoamine oxidase B Homo sapiens 15-20 7618520-10 1995 Inhibitors with relatively short carbon chain lengths (i.e. four to six carbons) were found to be more potent at inhibiting brain MAO-B activity in vivo especially after oral administration. Carbon 33-39 monoamine oxidase B Homo sapiens 130-135 7618520-10 1995 Inhibitors with relatively short carbon chain lengths (i.e. four to six carbons) were found to be more potent at inhibiting brain MAO-B activity in vivo especially after oral administration. Carbon 72-79 monoamine oxidase B Homo sapiens 130-135 7931241-11 1994 In the case of MAO-B inhibition, the 2 and 3 carbon-chain compounds had similar inhibitory potencies but this increased substantially when the chain length was increased to 4 carbons. Carbon 175-182 monoamine oxidase B Homo sapiens 15-20 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. Carbon 102-108 monoamine oxidase B Homo sapiens 82-88 3954792-0 1986 Stereospecific deuterium substitution at the alpha-carbon position of dopamine and its effect on oxidative deamination catalyzed by MAO-A and MAO-B from different tissues. Carbon 51-57 monoamine oxidase B Homo sapiens 142-147 34011531-7 2021 Docking into MAO B crystal structure suggested that even though both the isomers occupied its active site, only the orientation of RP-101075 presented the C-H on the a-carbon that was ideal for the C-H bond cleavage, which is a requisite for oxidative deamination. Carbon 168-174 monoamine oxidase B Homo sapiens 13-18 2788162-4 1989 These results indicate that the monoamine oxidase B-catalyzed oxidation of this substrate may not proceed via a reaction pathway involving alpha-carbon deprotonation of an aminium radical intermediate. Carbon 145-151 monoamine oxidase B Homo sapiens 32-51 28011206-5 2017 In addition, 6c inhibited self-induced Abeta1-42 aggregation and Cu2+-induced Abeta1-42 aggregation by 89.5% and 79.7% at 25muM respectively, as well as acted as a selective monoamine oxidase B inhibitor (IC50=0.29muM) and a selective biometal chelator. Carbon 13-15 monoamine oxidase B Homo sapiens 174-193 26592858-6 2016 In case of compounds having an aromatic nucleus at the amino terminus, increasing the carbon number between N and the aromatic ring increases the potency as well as selectivity toward hMAO-B. Carbon 86-92 monoamine oxidase B Homo sapiens 184-190