dc.creatorChamorro, María Eugenia
dc.creatorMaltaneri, Romina Eugenia
dc.creatorVittori, Daniela Cecilia
dc.creatorNesse, Alcira Beatriz
dc.date.accessioned2018-03-07T18:17:31Z
dc.date.accessioned2018-11-06T15:34:32Z
dc.date.available2018-03-07T18:17:31Z
dc.date.available2018-11-06T15:34:32Z
dc.date.created2018-03-07T18:17:31Z
dc.date.issued2015-02
dc.identifierChamorro, María Eugenia; Maltaneri, Romina Eugenia; Vittori, Daniela Cecilia; Nesse, Alcira Beatriz; Protein tyrosine phosphatase 1B (PTP1B) is involved in the defective erythropoietic function of carbamylated erythropoietin; Pergamon-Elsevier Science Ltd; International Journal Of Biochemistry And Cellular Biology; 61; 2-2015; 63-71
dc.identifier1357-2725
dc.identifierhttp://hdl.handle.net/11336/38152
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1898680
dc.description.abstract• Epo induced prolonged phosphorylation of proliferation signals in UT-7 cells. • cEpo induced only transient phosphorylation of proliferative pathways. • PTP1B activity was significantly increased in cultures with cEpo. • PTP1B colocalized with both subunits of the heterodimeric receptor used by cEpo. • Phosphatases are involved in the inability of cEpo to act as an erythroid growth factor.
dc.languageeng
dc.publisherPergamon-Elsevier Science Ltd
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.biocel.2015.01.019
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1357272515000291
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectCARBAMYLATED ERYTHROPOIETIN
dc.subjectCELL PROLIFERATION
dc.subjectERYTHROPOIETIN
dc.subjectPTP1B
dc.subjectTYROSINE PHOSPHATASES
dc.titleProtein tyrosine phosphatase 1B (PTP1B) is involved in the defective erythropoietic function of carbamylated erythropoietin
dc.typeArtículos de revistas
dc.typeArtículos de revistas
dc.typeArtículos de revistas


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