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dc.contributor.authorCeballos, M.-
dc.contributor.authorVioque, Agustín-
dc.date.accessioned2008-10-16T14:28:59Z-
dc.date.available2008-10-16T14:28:59Z-
dc.date.issued2007-02-01T14:28:59Z-
dc.identifier.issn0929-8665-
dc.identifier.urihttp://hdl.handle.net/10261/7833-
dc.descriptionProtein and Peptide Letters 14 (2):137-145en_US
dc.description.abstractEndonuclease tRNase Z catalyzes the generation of the mature 3’ end of tRNA precursors through specific endonucleolytic cleavage. The enzyme has been characterized from organisms representative of all domains of life as well as from organelles, and the crystal structure of three bacterial enzymes has been determined. This review presents an overview of its properties and what is known about its structure, substrate recognition, cleavage site definition, and potential practical applications.en_US
dc.format.extent22264 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.rightsclosedAccessen_US
dc.titletRnase Zen_US
dc.typeartículoen_US
dc.description.peerreviewedPeer revieweden_US
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeartículo-
item.cerifentitytypePublications-
item.grantfulltextnone-
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