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The role of post-translational modifications on STAT3 interactions

dc.contributor.authorFerreira, Joana Grand-Guillaume Perrenoud Silvestre
dc.date.accessioned2019-08-26T14:59:19Z
dc.date.available2019-09-30T00:30:39Z
dc.date.issued2017
dc.description.abstract"The JAK/STAT3 pathway is involved in multiple biological phenomena, mostly related to stress or tissue damage, but also development and cancer. A rate-limiting step of the pathway involves STAT3 dimerization, phosphorylation and translocation to the nucleus. Originally, it was thought that STAT3 dimerized upon phosphorylation by JAKs on Y705. However, current evidence indicates that STAT3 exists as a dimer prior to phosphorylation and activation, and that phosphorylation only induces a change in the conformation of the dimer.(...)"pt_PT
dc.description.versionN/Apt_PT
dc.identifier.urihttp://hdl.handle.net/10362/79296
dc.language.isoengpt_PT
dc.publisherUniversidade Nova de Lisboa. Instituto de Tecnologia Química e Biológica António Xavierpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectJAK/STAT3 pathwaypt_PT
dc.subjectSTAT3pt_PT
dc.subjectpost-translational modificationspt_PT
dc.subjectBiFC systempt_PT
dc.titleThe role of post-translational modifications on STAT3 interactionspt_PT
dc.typemaster thesis
dspace.entity.typePublication
oaire.citation.conferencePlaceOeiras, Portugalpt_PT
rcaap.embargofctArtigos por publicarpt_PT
rcaap.rightsembargoedAccesspt_PT
rcaap.typemasterThesispt_PT

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