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dc.contributor.authorMäki, Joni M.es_ES
dc.date.accessioned2013-09-24T11:35:03Z-
dc.date.available2013-09-24T11:35:03Z-
dc.date.issued2009-
dc.identifier.issn0213-3911es_ES
dc.identifier.urihttp://hdl.handle.net/10201/36017-
dc.description.abstractLysyl oxidase (LOX) catalyzes the oxidation of the side chain of a peptidyl lysine converting specific lysine and hydroxylysine residues of a–aminoadipic-d- semialdehydes, which form covalent crosslinks in collagens and elastin. Five different but closely related lysyl oxidase isoenzymes have been identified to date, and they seem to have overlapping functions in many tissues. Modification of the extracellular matrix by lysyl oxidases has been shown to be a critical contributor to the development of various organs and certain pathological conditions.es_ES
dc.formatapplication/pdfes_ES
dc.format.extent10es_ES
dc.languageenges_ES
dc.publisherMurcia : F. Hernándezes_ES
dc.relation.ispartofHistology and histopathologyes_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.subjectCopper enzymees_ES
dc.subjectAneurysmes_ES
dc.subject.other577 - Bioquímica. Biología molecular. Biofísicaes_ES
dc.titleLysyl oxidases in mammalian development and certain pathological conditionses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
Aparece en las colecciones:Vol.24, nº5 (2009)

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