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dc.contributor.authorPulido, R.
dc.contributor.authorBaker, S. J.
dc.contributor.authorBarata, J. T.
dc.contributor.authorCarracedo Álvarez, Ángel
dc.contributor.authorCid, V. J.
dc.contributor.authorChin-Sang, I. D.
dc.contributor.authorDavé, V.
dc.contributor.authorden Hertog, J.
dc.contributor.authorDevreotes, P.
dc.contributor.authorEickholt, B. J.
dc.contributor.authorEng, C.
dc.contributor.authorFurnari, F. B.
dc.contributor.authorGeorgescu, M. M.
dc.contributor.authorGericke, A.
dc.contributor.authorHopkins, B.
dc.contributor.authorJiang, X.
dc.contributor.authorLee, S. R.
dc.contributor.authorLösche, M.
dc.contributor.authorMalaney, P.
dc.contributor.authorMatias-Guiu, X.
dc.contributor.authorMolina, M.
dc.contributor.authorPandolfi, P. P.
dc.contributor.authorParsons, R.
dc.contributor.authorPinton, P.
dc.contributor.authorRivas ?, Carmen
dc.contributor.authorRocha, R. M.
dc.contributor.authorRodríguez, M. S.
dc.contributor.authorRoss, A. H.
dc.contributor.authorSerrano, M.
dc.contributor.authorStambolic, V.
dc.contributor.authorStiles, B.
dc.contributor.authorSuzuki, A.
dc.contributor.authorTan, S. S.
dc.contributor.authorTonks, N. K.
dc.contributor.authorTrotman, L. C.
dc.contributor.authorWolff, N.
dc.contributor.authorWoscholski, R.
dc.contributor.authorWu, H.
dc.contributor.authorLeslie, N. R.
dc.date.accessioned2017-06-07T07:23:43Z
dc.date.available2017-06-07T07:23:43Z
dc.date.issued2014
dc.identifier.issn1937-9145
dc.identifier.urihttp://hdl.handle.net/20.500.11940/5911
dc.description.abstractThe tumor suppressor PTEN is a major brake for cell transformation, mainly due to its phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] phosphatase activity that directly counteracts the oncogenicity of phosphoinositide 3-kinase (PI3K). PTEN mutations are frequent in tumors and in the germ line of patients with tumor predisposition or with neurological or cognitive disorders, which makes the PTEN gene and protein a major focus of interest in current biomedical research. After almost two decades of intense investigation on the 403-residue-long PTEN protein, a previously uncharacterized form of PTEN has been discovered that contains 173 amino-terminal extra amino acids, as a result of an alternate translation initiation site. To facilitate research in the field and to avoid ambiguities in the naming and identification of PTEN amino acids from publications and databases, we propose here a unifying nomenclature and amino acid numbering for this longer form of PTEN.
dc.language.isoeng
dc.subject.meshAmino Acid Sequence
dc.subject.meshAmino Acids
dc.subject.meshCodon, Initiator
dc.subject.meshDatabases, Protein
dc.subject.meshHumans
dc.subject.meshPTEN Phosphohydrolase
dc.subject.meshTerminology as Topic
dc.titleA unified nomenclature and amino acid numbering for human PTEN
dc.typeArtigoes
dc.authorsophosPulido, R.
dc.authorsophosBaker, S. J.
dc.authorsophosBarata, J. T.
dc.authorsophosCarracedo, A.
dc.authorsophosCid, V. J.
dc.authorsophosChin-Sang, I. D.
dc.authorsophosDavé, V.
dc.authorsophosden Hertog, J.
dc.authorsophosDevreotes, P.
dc.authorsophosEickholt, B. J.
dc.authorsophosEng, C.
dc.authorsophosFurnari, F. B.
dc.authorsophosGeorgescu, M. M.
dc.authorsophosGericke, A.
dc.authorsophosHopkins, B.
dc.authorsophosJiang, X.
dc.authorsophosLee, S. R.
dc.authorsophosLösche, M.
dc.authorsophosMalaney, P.
dc.authorsophosMatias-Guiu, X.
dc.authorsophosMolina, M.
dc.authorsophosPandolfi, P. P.
dc.authorsophosParsons, R.
dc.authorsophosPinton, P.
dc.authorsophosRivas, C.
dc.authorsophosRocha, R. M.
dc.authorsophosRodríguez, M. S.
dc.authorsophosRoss, A. H.
dc.authorsophosSerrano, M.
dc.authorsophosStambolic, V.
dc.authorsophosStiles, B.
dc.authorsophosSuzuki, A.
dc.authorsophosTan, S. S.
dc.authorsophosTonks, N. K.
dc.authorsophosTrotman, L. C.
dc.authorsophosWolff, N.
dc.authorsophosWoscholski, R.
dc.authorsophosWu, H.
dc.authorsophosLeslie, N. R.
dc.identifier.doi10.1126/scisignal.2005560
dc.identifier.isi338511700001
dc.identifier.pmid24985344
dc.identifier.sophos14930
dc.issue.number332
dc.journal.titleScience Signaling
dc.organizationServizo Galego de Saúde::Estrutura de Xestión Integrada (EOXI)::EOXI de Santiago::IDIS.- Instituto de investigaciones sanitarias de Santiago
dc.page.initialpe15
dc.rights.accessRightsopenAccess
dc.typesophosArtículo Original
dc.volume.number7


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