PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19789505-3 2009 MATERIAL/METHODS: We investigated MAO labeling with mechanism-based inhibitor [3H]pargyline activities of MAO A, MAO B, and SSAO in healthy and inflamed human dental pulp. Pargyline 82-91 monoamine oxidase A Homo sapiens 106-111 23499958-6 2013 The inhibition of both MAO-A and MAO-B by clorgyline and pargyline, respectively, enhanced the effects of cocaine on DARPP-32 phosphorylation. Pargyline 57-66 monoamine oxidase A Homo sapiens 23-28 21341713-1 2011 TEMPO-substituted pargyline analogues differentially inhibit recombinant human monoamine oxidase A (MAO A) and B (MAO B) in intact yeast mitochondria, suggesting these membrane-bound enzymes are located on differing faces of the mitochondrial outer membrane [Upadhyay, A., and Edmondson, D. E. (2009) Biochemistry 48, 3928]. Pargyline 18-27 monoamine oxidase A Homo sapiens 79-98 21341713-1 2011 TEMPO-substituted pargyline analogues differentially inhibit recombinant human monoamine oxidase A (MAO A) and B (MAO B) in intact yeast mitochondria, suggesting these membrane-bound enzymes are located on differing faces of the mitochondrial outer membrane [Upadhyay, A., and Edmondson, D. E. (2009) Biochemistry 48, 3928]. Pargyline 18-27 monoamine oxidase A Homo sapiens 100-105 26263056-7 2015 The developed method was successfully applied for detection of the MAO-A and MAO-B inhibitive activities by model drugs, including pargyline, clorgyline, as well as beta-carboline alkaloids from Peganum harmala. Pargyline 131-140 monoamine oxidase A Homo sapiens 67-72 1686901-0 1991 Synthesis, biological evaluation and quantitative structure activity relationship analysis of nuclear-substituted pargylines as competitive inhibitors of MAO-A and MAO-B. Pargyline 114-124 monoamine oxidase A Homo sapiens 154-159 9564606-2 1998 In comparative studies with other, structurally similar acetylenic inhibitors of MAO, pargyline, an MAO-B > MAO-A inhibitor used in doses of 90 mg/day for three or more weeks, produced elevations in these trace amines which were similar to those found with the highest dose of selegiline studied. Pargyline 86-95 monoamine oxidase A Homo sapiens 111-116 19296688-0 2009 Development of spin-labeled pargyline analogues as specific inhibitors of human monoamine oxidases A and B. Pargyline 28-37 monoamine oxidase A Homo sapiens 80-106 17561096-4 2007 Silencing MAO-A by siRNA, pharmacological MAO-A inhibitors (pargyline and Ro41-1049), and the antioxidant/ROS scavenger butylated hydroxytoluene (BHT) inhibited the signaling cascade, suggesting that ROS generated during tyramine oxidation by MAO-A are required. Pargyline 60-69 monoamine oxidase A Homo sapiens 10-15 12777388-15 2003 This study shows that the MAO A structure is "more flexible" than that of MAO B and that clorgyline and pargyline inactivation of MAO A and B, respectively, increases the structural stability of both enzymes. Pargyline 104-113 monoamine oxidase A Homo sapiens 26-31 12777388-15 2003 This study shows that the MAO A structure is "more flexible" than that of MAO B and that clorgyline and pargyline inactivation of MAO A and B, respectively, increases the structural stability of both enzymes. Pargyline 104-113 monoamine oxidase A Homo sapiens 130-141 9503561-4 1997 MAO-A preferentially deaminates serotonin (5HT) and is selectively inhibited by harmine and clorgyline, while MAO-B preferentially deaminates phenethylamine and benzylamine, and is selectively inhibited by (-)deprenyl as well as low concentrations of pargyline. Pargyline 251-260 monoamine oxidase A Homo sapiens 0-5 7953696-9 1994 Administration of deprenyl or pargyline, together with pCA, itself a MAO-A inhibitor, will lead to inhibition of both MAO-A and MAO-B activities. Pargyline 30-39 monoamine oxidase A Homo sapiens 69-74 7953696-9 1994 Administration of deprenyl or pargyline, together with pCA, itself a MAO-A inhibitor, will lead to inhibition of both MAO-A and MAO-B activities. Pargyline 30-39 monoamine oxidase A Homo sapiens 118-123 7931265-2 1994 Kinetic considerations show that the rate of reaction of MAO-A with low concentrations of free pargyline will be very much slower than that of MAO-B. Pargyline 95-104 monoamine oxidase A Homo sapiens 57-62 7931265-3 1994 Failure to use adequate reaction times for the concentration of pargyline added can lead to gross underestimation of the quantity of MAO-A present. Pargyline 64-73 monoamine oxidase A Homo sapiens 133-138 1686901-1 1991 A series of nuclear substituted derivatives of pargyline has been prepared and tested (under controlled conditions designed to measure the competitive component of the inhibition) as competitive inhibitors of MAO-A and -B. Pargyline 47-56 monoamine oxidase A Homo sapiens 209-221 2495009-1 1989 The concentrations of monoamine oxidase-A and -B were determined in homogenates of human cerebral cortex, caudatus and placenta and in human platelet-rich plasma and platelet membranes by determining the specific binding of tritium-labelled pargyline. Pargyline 241-250 monoamine oxidase A Homo sapiens 22-48 6791210-5 1981 Chronic treatment with the MAO-A inhibitor clorgyline and the MAO-B inhibitor pargyline showed significant inhibition of the alternate MAO enzyme as well, although this crossover effect was greater for pargyline than clorgyline. Pargyline 202-211 monoamine oxidase A Homo sapiens 27-32 7264664-2 1981 [3H]Pargyline was bound to MAO A in a crude mitochondrial fraction from the placental trophoblast of a male newborn and to MAO B in blood platelets from the umbilical vein of the same newborn. Pargyline 4-13 monoamine oxidase A Homo sapiens 27-32 7264664-6 1981 When SDS-solubilized, [3H]pargyline-labeled MAO A and B proteins from the same male newborn were subjected to limited proteolysis and one-dimensional peptide mapping in SDS gels, different patterns of [3H]pargyline-labeled peptides were obtained. Pargyline 26-35 monoamine oxidase A Homo sapiens 44-49 6847697-8 1983 Furthermore, when SDS-solubilized, [3H]pargyline-labeled MAO A and B proteins from these cell lines were subjected to limited proteolysis and one-dimensional peptide mapping in SDS gels, different patterns of [3H]pargyline-labeled peptides were obtained. Pargyline 39-48 monoamine oxidase A Homo sapiens 57-62 111275-0 1979 Selectivity of clorgyline and pargyline as inhibitors of monoamine oxidases A and B in vivo in man. Pargyline 30-39 monoamine oxidase A Homo sapiens 57-83 33085988-2 2021 The result indicated that 7,8-dihydroxy-3-(4-nitrophenyl)coumarin (3j) was most effective against MAO-A (inhibition concentration [IC50 ] = 6.46 +- 0.02 microM) and MAO-B (IC50 = 3.8 +- 0.3 microM) enzymes than other synthesized compounds and reference compounds (pargyline and moclobemide). Pargyline 265-274 monoamine oxidase A Homo sapiens 98-103