{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,9,4]],"date-time":"2024-09-04T14:36:46Z","timestamp":1725460606066},"reference-count":41,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2003,7,1]],"date-time":"2003-07-01T00:00:00Z","timestamp":1057017600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Life Sciences"],"published-print":{"date-parts":[[2003,7]]},"DOI":"10.1016\/s0024-3205(03)00415-6","type":"journal-article","created":{"date-parts":[[2003,6,3]],"date-time":"2003-06-03T00:12:50Z","timestamp":1054599170000},"page":"955-967","source":"Crossref","is-referenced-by-count":5,"title":["Differential substrate specificity of monoamine oxidase in the rat heart and renal cortex"],"prefix":"10.1016","volume":"73","author":[{"given":"J.T","family":"Guimar\u00e3es","sequence":"first","affiliation":[]},{"given":"C","family":"Vindis","sequence":"additional","affiliation":[]},{"given":"P","family":"Soares-da-Silva","sequence":"additional","affiliation":[]},{"given":"A","family":"Parini","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0024-3205(03)00415-6_BIB1","series-title":"Catecholamines","first-page":"119","article-title":"Monoamine oxidase","author":"Youdim","year":"1988"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB2","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1096\/fasebj.9.8.7768351","article-title":"Monoamine oxidases: old friends hold many surprises","volume":"9","author":"Singer","year":"1995","journal-title":"Faseb J"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB3","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1016\/0006-2952(68)90066-X","article-title":"Some observations upon a new inhibitor of monoamine oxidase in brain tissue","volume":"17","author":"Johnston","year":"1968","journal-title":"Biochem Pharmacol"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB4","first-page":"393","article-title":"Some puzzling pharmacological effects of monoamine oxidase inhibitors","volume":"5","author":"Knoll","year":"1972","journal-title":"Adv Biochem Psychopharmacol"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB5","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1126\/science.3875898","article-title":"Distinct monoamine oxidase A and B populations in primate brain","volume":"230","author":"Westlund","year":"1985","journal-title":"Science"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB6","doi-asserted-by":"crossref","first-page":"1977","DOI":"10.1523\/JNEUROSCI.12-05-01977.1992","article-title":"Quantitative enzyme radioautography with 3H-Ro 41-1049 and 3H-Ro 19-6327 in vitro: localization and abundance of MAO-A and MAO-B in rat CNS, peripheral organs, and human brain","volume":"12","author":"Saura","year":"1992","journal-title":"J Neurosci"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB7","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/0003-9861(78)90237-0","article-title":"Bovine liver monoamine oxidase. A modified purification procedure and preliminary evidence for two subunits and one FAD","volume":"189","author":"Minamiura","year":"1978","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB8","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1111\/j.1432-1033.1971.tb19689.x","article-title":"The covalently-bound flavin of hepatic monoamine oxidase. 1. Isolation and sequence of a flavin peptide and evidence for binding at the 8alpha position","volume":"24","author":"Kearney","year":"1971","journal-title":"Eur J Biochem"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB9","doi-asserted-by":"crossref","first-page":"1995","DOI":"10.1016\/0006-2952(78)90057-6","article-title":"Substrate-selective activation of rat liver mitochondrial monoamine oxidase by oxygen","volume":"27","author":"Fowler","year":"1978","journal-title":"Biochem Pharmacol"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB10","first-page":"365","article-title":"Beta-phenylethylamine: a specific substrate for type B monoamine oxidase of brain","volume":"187","author":"Yang","year":"1973","journal-title":"J Pharmacol Exp Ther"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB11","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1007\/BF00512469","article-title":"The deamination of noradrenaline and 5-hydroxytryptamine by rat brain and heart monoamine oxidase and their inhibition by cimoxatone, toloxatone and MD 770222","volume":"323","author":"Strolin Benedetti","year":"1983","journal-title":"Naunyn Schmiedebergs Arch Pharmacol"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB12","first-page":"546","article-title":"The inhibition or rat heart type A monoamine oxidase by clorgyline as a method for the estimation of enzyme active centers","volume":"16","author":"Fowler","year":"1979","journal-title":"Mol Pharmacol"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB13","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1111\/j.2042-7158.1975.tb09532.x","article-title":"Evidence for a clorgyline-resistant monoamine metabolizing activity in the rat heart","volume":"27","author":"Lyles","year":"1975","journal-title":"J Pharm Pharmacol"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB14","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/S0031-6989(79)80021-1","article-title":"An explanation for deamination of phenylethylamine by multiple types of monoamine oxidase","volume":"11","author":"Dial","year":"1979","journal-title":"Pharmacol Res Commun"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB15","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/0006-2952(79)90388-5","article-title":"Effect of beta-phenylethylamine concentration on its substrate specificity for type A and type B monoamine oxidase","volume":"28","author":"Suzuki","year":"1979","journal-title":"Biochem Pharmacol"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB16","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/0006-2952(91)90471-G","article-title":"New directions in monoamine oxidase A and B selective inhibitors and substrates","volume":"41","author":"Youdim","year":"1991","journal-title":"Biochem Pharmacol"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB17","first-page":"279","article-title":"From moclobemide to Ro 19-6327 and Ro 41-1049: the development of a new class of reversible, selective MAO-A and MAO-B inhibitors","volume":"29","author":"Da Prada","year":"1990","journal-title":"J Neural Transm Suppl"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB18","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1111\/j.1432-1033.1996.00996.x","article-title":"Investigation on the structure of the active site of monoamine oxidase-B by affinity labeling with the selective inhibitor lazabemide and by site-directed mutagenesis","volume":"236","author":"Cesura","year":"1996","journal-title":"Eur J Biochem"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB19","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1111\/j.1471-4159.1981.tb00464.x","article-title":"Differences in the structure of A and B forms of human monoamine oxidase","volume":"37","author":"Cawthon","year":"1981","journal-title":"J Neurochem"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB20","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1042\/bj1350173","article-title":"The nature of the electrophoretically separable multiple forms of rat liver monoamine oxidase","volume":"135","author":"Houslay","year":"1973","journal-title":"Biochem J"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB21","doi-asserted-by":"crossref","first-page":"4934","DOI":"10.1073\/pnas.85.13.4934","article-title":"cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties","volume":"85","author":"Bach","year":"1988","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB22","doi-asserted-by":"crossref","first-page":"3637","DOI":"10.1073\/pnas.88.9.3637","article-title":"Human monoamine oxidase A and B genes exhibit identical exon\u2013intron organization","volume":"88","author":"Grimsby","year":"1991","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB23","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1016\/0024-3205(95)02356-9","article-title":"Identification of a region important for human monoamine oxidase B substrate and inhibitor selectivity","volume":"58","author":"Grimsby","year":"1996","journal-title":"Life Sci"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB24","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1046\/j.1471-4159.1996.66020797.x","article-title":"Influence of C terminus on monoamine oxidase A and B catalytic activity","volume":"66","author":"Chen","year":"1996","journal-title":"J Neurochem"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB25","doi-asserted-by":"crossref","first-page":"14033","DOI":"10.1074\/jbc.272.22.14033","article-title":"A key amino acid responsible for substrate selectivity of monoamine oxidase A and B","volume":"272","author":"Tsugeno","year":"1997","journal-title":"J Biol Chem"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB26","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/0003-2697(87)90021-2","article-title":"Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction","volume":"162","author":"Chomczynski","year":"1987","journal-title":"Anal Biochem"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB27","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal Biochem"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB28","series-title":"GraphPad Prism (version 1.0)","author":"Motulsky","year":"1994"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB29","doi-asserted-by":"crossref","first-page":"3099","DOI":"10.1016\/0006-2952(73)90196-2","article-title":"Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction","volume":"22","author":"Cheng","year":"1973","journal-title":"Biochem Pharmacol"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB30","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1038\/ng1097-206","article-title":"Increased stress response and beta-phenylethylamine in MAOB-deficient mice","volume":"17","author":"Grimsby","year":"1997","journal-title":"Nat Genet"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB31","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1111\/j.1748-1716.1992.tb09376.x","article-title":"Type A and B monoamine oxidase activities in the human and rat kidney","volume":"145","author":"Fernandes","year":"1992","journal-title":"Acta Physiol Scand"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB32","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1016\/S1357-2725(96)00166-5","article-title":"Opossum kidney (OK) cells in culture synthesize and degrade the natriuretic hormone dopamine: a comparison with rat renal tubular cells","volume":"29","author":"Guimaraes","year":"1997","journal-title":"Int J Biochem Cell Biol"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB33","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/S0024-3205(97)01171-5","article-title":"The activity of MAO A and B in rat renal cells and tubules","volume":"62","author":"Guimaraes","year":"1998","journal-title":"Life Sci"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB34","doi-asserted-by":"crossref","first-page":"S622","DOI":"10.1042\/bst025s622","article-title":"Unusual pattern of beta-phenylethylamine deamination in the rat heart","volume":"25","author":"Guimaraes","year":"1997","journal-title":"Biochem Soc Trans"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB35","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1111\/j.1471-4159.1982.tb07922.x","article-title":"Monoamine oxidases A and B as components of a membrane complex","volume":"38","author":"White","year":"1982","journal-title":"J Neurochem"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB36","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/1357-2725(95)00130-1","article-title":"Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects","volume":"28","author":"Lyles","year":"1996","journal-title":"Int J Biochem Cell Biol"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB37","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1038\/281692a0","article-title":"Differences in A and B forms of monoamine oxidase revealed by limited proteolysis and peptide mapping","volume":"281","author":"Cawthon","year":"1979","journal-title":"Nature"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB38","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1126\/science.7063850","article-title":"Human liver MAO-A and MAO-B separated by immunoaffinity chromatography with MAO-B-specific monoclonal antibody","volume":"215","author":"Denney","year":"1982","journal-title":"Science"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB39","doi-asserted-by":"crossref","first-page":"970","DOI":"10.1016\/S0006-291X(88)80969-0","article-title":"Molecular cloning of a cDNA for rat liver monoamine oxidase B","volume":"157","author":"Ito","year":"1988","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB40","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1271\/bbb1961.54.253","article-title":"Primary structure of rat monoamine oxidase A deduced from cDNA and its expression in rat tissues","volume":"54","author":"Kuwahara","year":"1990","journal-title":"Agric Biol Chem"},{"key":"10.1016\/S0024-3205(03)00415-6_BIB41","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1042\/bj3250269","article-title":"Alternative splicing of ClC-6 (a member of the CIC chloride-channel family) transcripts generates three truncated isoforms one of which, ClC-6c, is kidney-specific","volume":"325","author":"Eggermont","year":"1997","journal-title":"Biochem J"}],"container-title":["Life Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0024320503004156?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0024320503004156?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,3,20]],"date-time":"2020-03-20T21:51:59Z","timestamp":1584741119000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0024320503004156"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,7]]},"references-count":41,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2003,7]]}},"alternative-id":["S0024320503004156"],"URL":"https:\/\/doi.org\/10.1016\/s0024-3205(03)00415-6","relation":{},"ISSN":["0024-3205"],"issn-type":[{"value":"0024-3205","type":"print"}],"subject":[],"published":{"date-parts":[[2003,7]]}}}