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dc.contributor.authorFinney, Joel
dc.contributor.authorMoon, Hee-Jung
dc.contributor.authorRonnebaum, Trey
dc.contributor.authorLantz, Mason
dc.contributor.authorMure, Minae
dc.date.accessioned2018-09-14T17:15:03Z
dc.date.available2018-09-14T17:15:03Z
dc.date.issued2014-03-15
dc.identifier.citationJoel Finney, Hee-Jung Moon, Trey Ronnebaum, Mason Lantz, Minae Mure Arch Biochem Biophys. 2014 Mar 15; 546: 19–32. Published online 2014 Jan 6. doi: 10.1016/j.abb.2013.12.022en_US
dc.identifier.urihttp://hdl.handle.net/1808/26722
dc.description.abstractCopper amine oxidases (CAOs) are a class of enzymes that contain Cu2+ and a tyrosine-derived quinone cofactor, catalyze the conversion of a primary amine functional group to an aldehyde, and generate hydrogen peroxide and ammonia as byproducts. These enzymes can be classified into two non-homologous families: 2,4,5-trihydroxyphenylalanine quinone (TPQ)-dependent CAOs and the lysine tyrosylquinone (LTQ)-dependent lysyl oxidase (LOX) family of proteins. In this review, we will focus on recent developments in the field of research concerning human CAOs and the LOX family of proteins. The aberrant expression of these enzymes is linked to inflammation, fibrosis, tumor metastasis/invasion and other diseases. Consequently, there is a critical need to understand the functions of these proteins at the molecular level, so that strategies targeting these enzymes can be developed to combat human diseases.en_US
dc.publisherElsevieren_US
dc.subjectCooper amine oxidaseen_US
dc.subjectLysyl oxidaseen_US
dc.subjectQuinoproteinen_US
dc.titleHuman Copper-Dependent Amine Oxidasesen_US
dc.typeArticleen_US
kusw.kuauthorMoon, Hee-Jung
kusw.kuauthorMure, Minae
kusw.kudepartmentPharmacology & Toxicologyen_US
kusw.kudepartmentChemistryen_US
dc.identifier.doihttps://doi.org/10.1016/j.abb.2013.12.022en_US
kusw.oaversionScholarly/refereed, publisher versionen_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.identifier.pmidPMC5995473en_US
dc.rights.accessrightsopenAccessen_US


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