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Autordc.contributor.authorContreras Vallejos, Erick 
Autordc.contributor.authorUtreras Puratich, Elías 
Autordc.contributor.authorBórquez, Daniel A. 
Autordc.contributor.authorProchazkova, Michaela 
Autordc.contributor.authorTerse, Anita 
Autordc.contributor.authorJaffe, Howard 
Autordc.contributor.authorToledo, Andrea 
Autordc.contributor.authorArruti, Cristina 
Autordc.contributor.authorPant, Harish C. 
Autordc.contributor.authorKulkarni, Ashok B. 
Autordc.contributor.authorGonzález Billault, Christian 
Fecha ingresodc.date.accessioned2019-03-15T16:06:29Z
Fecha disponibledc.date.available2019-03-15T16:06:29Z
Fecha de publicacióndc.date.issued2014
Cita de ítemdc.identifier.citationPLoS ONE, Volumen 9, Issue 3, 2018,
Identificadordc.identifier.issn19326203
Identificadordc.identifier.other10.1371/journal.pone.0090363
Identificadordc.identifier.urihttps://repositorio.uchile.cl/handle/2250/166144
Resumendc.description.abstractProtein phosphorylation is the most common post-translational modification that regulates several pivotal functions in cells. Cyclin-dependent kinase 5 (Cdk5) is a proline-directed serine/threonine kinase which is mostly active in the nervous system. It regulates several biological processes such as neuronal migration, cytoskeletal dynamics, axonal guidance and synaptic plasticity among others. In search for novel substrates of Cdk5 in the brain we performed quantitative phosphoproteomics analysis, isolating phosphoproteins from whole brain derived from E18.5 Cdk5+/+ and Cdk5-/- embryos, using an Immobilized Metal-Ion Affinity Chromatography (IMAC), which specifically binds to phosphorylated proteins. The isolated phosphoproteins were eluted and isotopically labeled for relative and absolute quantitation (iTRAQ) and mass spectrometry identification. We found 40 proteins that showed decreased phosphorylation at Cdk5-/- brains. In addition, out of these 40 hypophosphorylated proteins we
Idiomadc.language.isoen
Publicadordc.publisherPublic Library of Science
Tipo de licenciadc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link a Licenciadc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
Fuentedc.sourcePLoS ONE
Palabras clavesdc.subjectBiochemistry, Genetics and Molecular Biology (all)
Palabras clavesdc.subjectAgricultural and Biological Sciences (all)
Títulodc.titleSearching for novel Cdk5 substrates in brain by comparative phosphoproteomics of wild type and Cdk5-/- mice
Tipo de documentodc.typeArtículo de revista
dcterms.accessRightsdcterms.accessRightsAcceso Abierto
Catalogadoruchile.catalogadorSCOPUS
Indizaciónuchile.indexArtículo de publicación SCOPUS
uchile.cosechauchile.cosechaSI


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Attribution-NonCommercial-NoDerivs 3.0 Chile
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