The role of post-translational modifications on STAT3 interactions

Detalhes bibliográficos
Autor(a) principal: Ferreira, Joana Grand-Guillaume Perrenoud Silvestre
Data de Publicação: 2017
Tipo de documento: Dissertação
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/79296
Resumo: "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.(...)"
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spelling The role of post-translational modifications on STAT3 interactionsJAK/STAT3 pathwaySTAT3post-translational modificationsBiFC system"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.(...)"Universidade Nova de Lisboa. Instituto de Tecnologia Química e Biológica António XavierRUNFerreira, Joana Grand-Guillaume Perrenoud Silvestre2019-09-30T00:30:39Z20172017-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttp://hdl.handle.net/10362/79296enginfo:eu-repo/semantics/embargoedAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T04:35:15Zoai:run.unl.pt:10362/79296Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:35:47.900921Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv The role of post-translational modifications on STAT3 interactions
title The role of post-translational modifications on STAT3 interactions
spellingShingle The role of post-translational modifications on STAT3 interactions
Ferreira, Joana Grand-Guillaume Perrenoud Silvestre
JAK/STAT3 pathway
STAT3
post-translational modifications
BiFC system
title_short The role of post-translational modifications on STAT3 interactions
title_full The role of post-translational modifications on STAT3 interactions
title_fullStr The role of post-translational modifications on STAT3 interactions
title_full_unstemmed The role of post-translational modifications on STAT3 interactions
title_sort The role of post-translational modifications on STAT3 interactions
author Ferreira, Joana Grand-Guillaume Perrenoud Silvestre
author_facet Ferreira, Joana Grand-Guillaume Perrenoud Silvestre
author_role author
dc.contributor.none.fl_str_mv RUN
dc.contributor.author.fl_str_mv Ferreira, Joana Grand-Guillaume Perrenoud Silvestre
dc.subject.por.fl_str_mv JAK/STAT3 pathway
STAT3
post-translational modifications
BiFC system
topic JAK/STAT3 pathway
STAT3
post-translational modifications
BiFC system
description "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.(...)"
publishDate 2017
dc.date.none.fl_str_mv 2017
2017-01-01T00:00:00Z
2019-09-30T00:30:39Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/masterThesis
format masterThesis
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/79296
url http://hdl.handle.net/10362/79296
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/embargoedAccess
eu_rights_str_mv embargoedAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade Nova de Lisboa. Instituto de Tecnologia Química e Biológica António Xavier
publisher.none.fl_str_mv Universidade Nova de Lisboa. Instituto de Tecnologia Química e Biológica António Xavier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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