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Kinases, tails and more: regulation of PTEN function by phosphorylation

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dc.contributor.authorFragoso, Rita
dc.contributor.authorBarata, João T.
dc.date.accessioned2022-03-08T16:58:25Z
dc.date.available2022-03-08T16:58:25Z
dc.date.issued2015
dc.description© 2014 Elsevier Inc. All rights reserved.pt_PT
dc.description.abstractPhosphorylation regulates the conformation, stability, homo- and heterotypic protein interactions, localization, and activity of the tumor suppressor PTEN. From a simple picture, at the beginning of this millennium, recognizing that CK2 phosphorylated PTEN at the C-terminus and thereby impacted on PTEN stability and activity, research has led to a significantly more complex scenario today, where for instance GSK3, Plk3, ATM, ROCK or Src-family kinases are also gaining the spotlight in this evolving play. Here, we review the current knowledge on the kinases that phosphorylate PTEN, and on the impact that specific phosphorylation events have on PTEN function.pt_PT
dc.description.sponsorshipResearch work in JTB’s lab that relates to the current article was supported by grants, PTDC/SAU-ONC/113202/2009 and PTDC/SAU-ONC/122428/2010 from Fundação para a Ciência e a Tecnologia (FCT), Portugal. RF and JTB were awarded FCT Starting and Consolidator Investigator grants, respectively.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationMethods. 2015 May;77-78:75-81pt_PT
dc.identifier.doi10.1016/j.ymeth.2014.10.015pt_PT
dc.identifier.eissn1095-9130
dc.identifier.issn1046-2023
dc.identifier.urihttp://hdl.handle.net/10451/51652
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relation.publisherversionhttps://www.sciencedirect.com/journal/methodspt_PT
dc.subjectC-terminal tailpt_PT
dc.subjectC2 domainpt_PT
dc.subjectCK2pt_PT
dc.subjectGSK3pt_PT
dc.subjectKinasespt_PT
dc.subjectPLK3pt_PT
dc.subjectPTENpt_PT
dc.subjectPhosphorylationpt_PT
dc.subjectPosttranslational modificationpt_PT
dc.subjectSrcpt_PT
dc.titleKinases, tails and more: regulation of PTEN function by phosphorylationpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardNumberPTDC/SAU-ONC/113202/2009
oaire.awardNumberPTDC/SAU-ONC/122428/2010
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FSAU-ONC%2F113202%2F2009/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FSAU-ONC%2F122428%2F2010/PT
oaire.citation.endPage81pt_PT
oaire.citation.startPage75pt_PT
oaire.citation.titleMethodspt_PT
oaire.citation.volume77-78pt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
person.familyNameFragoso
person.familyNameBarata
person.givenNameRita
person.givenNameJoão
person.identifier.ciencia-id261B-665F-73EE
person.identifier.orcid0000-0002-9206-1964
person.identifier.orcid0000-0002-4826-8976
person.identifier.ridD-9181-2015
person.identifier.scopus-author-id57210655467
person.identifier.scopus-author-id7006937224
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsrestrictedAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication45ef496f-867f-4009-b688-3cb1f7395df4
relation.isAuthorOfPublication06f27f7f-1c6c-4c03-a70d-52f8a388bd3b
relation.isAuthorOfPublication.latestForDiscovery45ef496f-867f-4009-b688-3cb1f7395df4
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