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dc.contributor.authorMontano, Ximena
dc.identifier.citationMontano , X 2001 , ' Common amino acid sequence motifs in p53, 14-3-3 and Akt protein families ' , FEBS Letters , vol. 507 , no. 2 , pp. 237-240 .
dc.identifier.otherPURE: 952362
dc.identifier.otherPURE UUID: fbec1821-333f-418f-bf19-ba910e82c67e
dc.identifier.otherScopus: 0035955437
dc.description.abstractThe tumour suppressor p53 is a multifunctional phosphoprotein able to induce apoptosis, differentiation or growth arrest, by acting as a transcription factor (capable of recognising DNA specific sequences) and targeting expression of genes involved in cell cycle control. p53 is a member of a family of related proteins (p63/CUSP/KET/p51/p40 and p73) characterised by multiple isoforms which share similar biological functions. Recently, we have shown that p53 binds to trk A (the receptor for nerve growth factor (NGF)) in the presence of the non-receptor tyrosine kinase c-abl. Importantly, p53 induces trk A hyperphosphorylation and stimulation of signalling cascades in the absence of NGF stimulation. Therefore, because of its role in trk A signalling, the aim has been to determine whether p53 has sequence homology to proteins involved in signal transduction pathwaysen
dc.relation.ispartofFEBS Letters
dc.titleCommon amino acid sequence motifs in p53, 14-3-3 and Akt protein familiesen
dc.contributor.institutionParamedic Science
dc.contributor.institutionSchool of Health and Social Work
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionAllied Health Professions
dc.contributor.institutionDepartment of Allied Health Professions and Midwifery
dc.description.statusPeer reviewed
rioxxterms.typeJournal Article/Review

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