PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19650872-6 2009 Substitution of the homologous serine in the MAO-B isoform, i.e. Ser200, with either Glu or Ala does not affect the catalytic activity of the corresponding over-expressed proteins. Glutamic Acid 85-88 monoamine oxidase B Homo sapiens 45-50 9724550-3 1998 Previously, Glu-34 and Tyr-44 of MAO B have been identified as residues which engage in noncovalent interactions with FAD that are required for subsequent covalent FAD binding and generation of catalytic activity. Glutamic Acid 12-15 monoamine oxidase B Homo sapiens 33-38 7840641-5 1995 In MAO B, this region is postulated to consist of a beta 1-sheet-alpha-helix-beta 2-sheet motif which culminates with a Glu at the C-terminal end of the second beta-sheet. Glutamic Acid 120-123 monoamine oxidase B Homo sapiens 3-8 35107654-4 2022 For the MAO-B inhibitor safinamide, recently introduced to the market, an additional inhibition of pathological release of glutamate has been postulated. Glutamic Acid 123-132 monoamine oxidase B Homo sapiens 8-13 31686637-3 2020 The monoamine oxidase B (MAO-B) degrades dopamine, promoting the glutamate accumulation and oxidative stress with the release of free radicals, causing excitotoxicity. Glutamic Acid 65-74 monoamine oxidase B Homo sapiens 4-23 31686637-3 2020 The monoamine oxidase B (MAO-B) degrades dopamine, promoting the glutamate accumulation and oxidative stress with the release of free radicals, causing excitotoxicity. Glutamic Acid 65-74 monoamine oxidase B Homo sapiens 25-30 30160213-9 2019 Among all antiparkinsonian agents, MAOB inhibitors are those with the greatest neuroprotective potential because of inhibition of dopamine metabolism, induction of neurotrophic factors, and, in the case of safinamide, inhibition of glutamate release. Glutamic Acid 232-241 monoamine oxidase B Homo sapiens 35-39 28777756-2 2017 Safinamide is a drug with an innovative mechanism of action, dopaminergic and non-dopaminergic, that includes the reversible inhibition of the monoamine oxidase-B (MAO-B) enzyme and the modulation of excessive glutamate release through the use- and state-dependent blockade of the sodium channels. Glutamic Acid 210-219 monoamine oxidase B Homo sapiens 164-169 17849100-3 2007 In the present study, the system was modified with glutamate oxidase instead of tyramine oxidase to detect L-glutamate sensitively ( approximately 10 nM) and rapidly with high temporal resolution (<1 s). Glutamic Acid 107-118 monoamine oxidase B Homo sapiens 80-96 14697882-11 2004 65 (2001) 129], we have identified three amino acids residues (Phe 423, Glu 427, and Thr 428) that appear to play a role in generating catalytically active MAO B. Glutamic Acid 72-75 monoamine oxidase B Homo sapiens 156-161 14697882-13 2004 Thus, it appears that Phe 423, Glu 427 and Thr 428 do not directly affect the active site, but they could modulate activity through an independent function such as non-covalent binding of FAD during synthesis of the MAO B polypeptide chain. Glutamic Acid 31-34 monoamine oxidase B Homo sapiens 216-221