PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26891670-7 2016 The main focus of drug design is the catalytic activity of MAO, but the imidazoline I2 site in the entrance cavity of MAO B is also a pharmacological target. Imidazolines 72-83 monoamine oxidase B Homo sapiens 118-123 24666288-14 2014 Imidazoline-2 (I-2) receptors interact with monoamine oxidase A and monoamine oxidase B leading to research that has focused on the effect of I-2 receptors and depression and the suggestion of a possible antidepressant action of the imidazolines. Imidazolines 233-245 monoamine oxidase B Homo sapiens 68-87 24601544-8 2014 This change in the presence of tranylcypromine may be responsible for the greater affinity of tranylcypromine-modified MAO B for imidazoline ligands. Imidazolines 129-140 monoamine oxidase B Homo sapiens 119-124 22426510-0 2012 Targeting imidazoline site on monoamine oxidase B through molecular docking simulations. Imidazolines 10-21 monoamine oxidase B Homo sapiens 30-49 22512575-2 2012 Since the I(1) imidazoline receptor is involved in central inhibition of sympathicus that produce hypotensive effect, the I(2) receptor is allosteric modulator of monoamine oxidase B (MAO-B) and the I(3) receptor regulates insulin secretion from pancreatic beta-cells, design and synthesis of selective I(1)/I(2)/I(3) imidazoline ligands are very important for the development of new effective therapeutic agents. Imidazolines 15-26 monoamine oxidase B Homo sapiens 184-189 22426510-3 2012 Furthermore, crystallographic studies identified the imidazoline-binding domain on monoamine oxidase B (MAO-B), which opens the possibility of molecular docking studies focused on this binding site. Imidazolines 53-64 monoamine oxidase B Homo sapiens 83-102 22426510-3 2012 Furthermore, crystallographic studies identified the imidazoline-binding domain on monoamine oxidase B (MAO-B), which opens the possibility of molecular docking studies focused on this binding site. Imidazolines 53-64 monoamine oxidase B Homo sapiens 104-109 9380016-0 1997 Localization of the imidazoline binding domain on monoamine oxidase B. Imidazolines 20-31 monoamine oxidase B Homo sapiens 50-69 20855894-1 2010 Crystallographic and biochemical studies have been employed to identify the binding site and mechanism for potentiation of imidazoline binding in human monoamine oxidase B (MAO B). Imidazolines 123-134 monoamine oxidase B Homo sapiens 152-171 20855894-1 2010 Crystallographic and biochemical studies have been employed to identify the binding site and mechanism for potentiation of imidazoline binding in human monoamine oxidase B (MAO B). Imidazolines 123-134 monoamine oxidase B Homo sapiens 173-178 17056035-0 2006 The imidazoline I2-site ligands BU 224 and 2-BFI inhibit MAO-A and MAO-B activities, hydrogen peroxide production, and lipolysis in rodent and human adipocytes. Imidazolines 4-15 monoamine oxidase B Homo sapiens 67-72 17704848-3 2006 Receptor I2, displaying high similarity of sequence with monoamine oxidase-B (MAO-B), is structurally related to MAO-B, but the I2 imidazoline binding site (I2BS) with ligand is distinct from the catalytic site of MAO-B. Imidazolines 131-142 monoamine oxidase B Homo sapiens 78-83 15028609-1 2003 An I(2) imidazoline binding site on monoamine oxidase-B (MAO-B) is known to be encoded by a noncatalytic part of the enzyme, different from that which recognizes mechanism-based inhibitors. Imidazolines 8-19 monoamine oxidase B Homo sapiens 36-55 15028609-1 2003 An I(2) imidazoline binding site on monoamine oxidase-B (MAO-B) is known to be encoded by a noncatalytic part of the enzyme, different from that which recognizes mechanism-based inhibitors. Imidazolines 8-19 monoamine oxidase B Homo sapiens 57-62 10688633-0 2000 Imidazoline-binding domains on monoamine oxidase B and subpopulations of enzyme. Imidazolines 0-11 monoamine oxidase B Homo sapiens 31-50 10688633-1 2000 A series of phenoxy-substituted methylimidazoline derivatives were synthesized and used to define the ligand recognition properties of the imidazoline-binding domain (IBD) on monoamine oxidase (MAO)-B and its role in substrate processing. Imidazolines 38-49 monoamine oxidase B Homo sapiens 175-200 10688633-3 2000 IC(50) values for inhibition of MAO-B activity by imidazoline/guanidinium ligands were one to two orders of magnitude greater than ligand concentrations that probably saturate the IBD, but were equal to the K(d) values of these ligands in competitive binding assays with the reversible MAO-B inhibitor [(3)H]Ro 19-6327. Imidazolines 50-61 monoamine oxidase B Homo sapiens 32-37 10688633-3 2000 IC(50) values for inhibition of MAO-B activity by imidazoline/guanidinium ligands were one to two orders of magnitude greater than ligand concentrations that probably saturate the IBD, but were equal to the K(d) values of these ligands in competitive binding assays with the reversible MAO-B inhibitor [(3)H]Ro 19-6327. Imidazolines 50-61 monoamine oxidase B Homo sapiens 286-291 10367991-1 1999 The I2-imidazoline receptor is expressed in brain and platelets and could represent a new binding domain on MAO-B enzyme. Imidazolines 7-18 monoamine oxidase B Homo sapiens 108-113 10367991-10 1999 Significant correlations between I2-imidazoline receptors and MAO-B activity were observed. Imidazolines 36-47 monoamine oxidase B Homo sapiens 62-67 10367991-13 1999 The dissociation between I2-imidazoline receptors and MAO-B in platelets suggests that the enzyme contributes to but not exclusively represents the I2-imidazoline receptor. Imidazolines 151-162 monoamine oxidase B Homo sapiens 54-59 20832472-1 2010 An allosteric binding site with high affinity for imidazoline I(2) ligands has been proposed to exist on monoamine oxidase-B (MAO-B). Imidazolines 50-61 monoamine oxidase B Homo sapiens 105-124 20832472-1 2010 An allosteric binding site with high affinity for imidazoline I(2) ligands has been proposed to exist on monoamine oxidase-B (MAO-B). Imidazolines 50-61 monoamine oxidase B Homo sapiens 126-131 17480205-1 2007 The two forms of monoamine oxidase, monoamine oxidase A and monoamine oxidase B, have been associated with imidazoline-binding sites (type 2). Imidazolines 107-118 monoamine oxidase B Homo sapiens 60-79 10415893-0 1999 Imidazoline binding domains on MAO-B. Imidazolines 0-11 monoamine oxidase B Homo sapiens 31-36 9380016-1 1997 Monoamine oxidase B (MAO-B) was recently identified as a member of the family of imidazoline binding proteins. Imidazolines 81-92 monoamine oxidase B Homo sapiens 0-19 9380016-1 1997 Monoamine oxidase B (MAO-B) was recently identified as a member of the family of imidazoline binding proteins. Imidazolines 81-92 monoamine oxidase B Homo sapiens 21-26 9380016-3 1997 Based on species-specific fragmentation patterns and immunoprecipitation of labeled peptides, the imidazoline binding domain was localized to residues K149 to M222 of human MAO-B. Imidazolines 98-109 monoamine oxidase B Homo sapiens 173-178 9380016-6 1997 Identification of an imidazoline binding domain on MAO-B provides a new opportunity for the potential pharmacological development of imidazoline/guanidinium compounds and also presents additional avenues for structure/function analysis of the monoamine oxidase enzymes. Imidazolines 21-32 monoamine oxidase B Homo sapiens 51-56 9380016-6 1997 Identification of an imidazoline binding domain on MAO-B provides a new opportunity for the potential pharmacological development of imidazoline/guanidinium compounds and also presents additional avenues for structure/function analysis of the monoamine oxidase enzymes. Imidazolines 133-144 monoamine oxidase B Homo sapiens 51-56 30455149-3 2019 Among the 2-imidazolines, good potency inhibitors were discovered with compound 9p (IC50 = 0.012 microM) being the most potent MAO-B inhibitor, while compound 9d (IC50 = 0.751 microM) was the most potent MAO-A inhibitor of the series. Imidazolines 11-24 monoamine oxidase B Homo sapiens 127-132 7499273-1 1995 Relationship to subtypes of imidazoline-binding proteins and tissue-specific interaction of imidazoline ligands with monoamine oxidase B. Imidazolines 28-39 monoamine oxidase B Homo sapiens 117-136 7499273-1 1995 Relationship to subtypes of imidazoline-binding proteins and tissue-specific interaction of imidazoline ligands with monoamine oxidase B. Imidazolines 92-103 monoamine oxidase B Homo sapiens 117-136 7499273-9 1995 Restricted access to the imidazoline binding domain on platelet MAO-B was not altered by membrane washing with 500 mM KCl or by solubilization and partial purification of the enzyme suggesting that there are distinct subpopulations of MAO. Imidazolines 25-36 monoamine oxidase B Homo sapiens 64-69