@prefix activity: .
@prefix address: .
@prefix agency: .
@prefix assay: .
@prefix assayCategory: .
@prefix assayTargetLink: .
@prefix biopax3: .
@prefix calbc: .
@prefix calbc-group: .
@prefix carrierLink: .
@prefix certainAgreement: .
@prefix chebi: .
@prefix chembl: .
@prefix chemicalCompound: .
@prefix chemicalCompoundRecord: .
@prefix clan: .
@prefix clinicalResult: .
@prefix clinicalStudy: .
@prefix clinicaltrials: .
@prefix company: .
@prefix confidenceScore: .
@prefix contact: .
@prefix country: .
@prefix cpath: .
@prefix curationLookup: .
@prefix dailymed: .
@prefix dailymed-drugs: .
@prefix dailymed-ingredient: .
@prefix dailymed-instance: .
@prefix databaseReference: .
@prefix dc: .
@prefix dc-term: .
@prefix diseaseontology: .
@prefix diseasome: .
@prefix diseasome-diseases: .
@prefix diseasome-gene: .
@prefix diseasome-instance: .
@prefix documentType: .
@prefix dosageForm: .
@prefix drug: .
@prefix drugbank: .
@prefix drugbank-proteinSequence: .
@prefix drugCategory: .
@prefix drugInteraction: .
@prefix drugTarget: .
@prefix eligibility: .
@prefix entrez-gene: .
@prefix entrez-goterm: .
@prefix entrezgene: .
@prefix enzymeLink: .
@prefix externalIdentifier: .
@prefix externalLink: .
@prefix factforge: .
@prefix family: .
@prefix foaf: .
@prefix formulation: .
@prefix freebase: .
@prefix gene-rif: .
@prefix geneontology: .
@prefix geneSequence: .
@prefix hapmap: .
@prefix indication: .
@prefix intervention: .
@prefix investigator: .
@prefix label: .
@prefix lhgdn: .
@prefix lifeskim: .
@prefix linkedct: .
@prefix linkedct-condition: .
@prefix linkedct-intervention: .
@prefix literatureCitation: .
@prefix lld: .
@prefix location: .
@prefix measurement: .
@prefix meddraSideEffect: .
@prefix mixture: .
@prefix molecularSpecies: .
@prefix molecule: .
@prefix moleculeType: .
@prefix ontotext: .
@prefix organismSpecies: .
@prefix outcomeAnalysis: .
@prefix outcomeMeasure: .
@prefix overallOfficial: .
@prefix owl: .
@prefix owlim: .
@prefix packager: .
@prefix participantFlow: .
@prefix patent: .
@prefix pfam: .
@prefix phenotype: .
@prefix pointOfContact: .
@prefix price: .
@prefix primaryOutcome: .
@prefix product: .
@prefix property: .
@prefix proteinSequence: .
@prefix pubmed: .
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@prefix reportingGroup: .
@prefix researchStem: .
@prefix responsibleParty: .
@prefix result: .
@prefix resultsBaseline: .
@prefix resultsMeasure: .
@prefix resultsOutcome: .
@prefix secondaryOutcome: .
@prefix sideEffect: .
@prefix sideEffectFrequency: .
@prefix sider: .
@prefix sider-drug: .
@prefix skos: .
@prefix skos-xl: .
@prefix snp: .
@prefix structureType: .
@prefix studyMilestone: .
@prefix studyParticipants: .
@prefix studyPeriod: .
@prefix substructure: .
@prefix symptom: .
@prefix synonym: .
@prefix targetLink: .
@prefix targetType: .
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@prefix transporterLink: .
@prefix umls: .
@prefix umls-concept: .
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@prefix uniprot-unstable: .
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pubmed-article:21432781 a pubmed:Citation ;
lifeskim:mentions umls-concept:C0812230 , umls-concept:C0812228 ;
pubmed:issue "5" ;
pubmed:dateCreated "2011-3-24" ;
pubmed:abstractText "Kinases of the Akt family are integral and essential components in growth factor signaling pathways activated downstream of the membrane bound phospho-inositol-3 kinase. In light of strong homologies in the primary amino acid sequence, the three Akt kinases were long surmised to play redundant and overlapping roles in insulin signaling across the spectra of cell and tissue types. Over the last 10 years, work using mouse knockout models, cell specific inactivation, and more recently targeted gene inactivation, has brought into question the redundancy within Akt kinase isoforms and instead pointed to isoform specific functions in different cellular events and diseases. Here we concentrate on the differential roles played by Akt1 and Akt2 in a variety of cellular processes and in particular during cancer biogenesis. In this overview, we illustrate that while Akt1 and 2 are often implicated in many aspects of cellular transformation, the two isoforms frequently act in a complementary opposing manner. Furthermore, Akt1 and Akt2 kinases interact differentially with modulating proteins and are necessary in relaying roles during the evolution of cancers from deregulated growth into malignant metastatic killers. These different actions of the two isoforms point to the importance of treatments targeting isoform specific events in the development of effective approaches involving Akt kinases in human disease." ;
pubmed:language "eng" ;
pubmed:journal ;
pubmed:citationSubset "IM" ;
pubmed:chemical , , ;
pubmed:status "MEDLINE" ;
pubmed:month "May" ;
pubmed:issn "1699-5848" ;
pubmed:author pubmed-author:FernandezAnneA , , pubmed-author:Heron-MilhavetLisaL , pubmed-author:KhouyaNabilN ;
pubmed:issnType "Electronic" ;
pubmed:volume "26" ;
pubmed:owner "NLM" ;
pubmed:authorsComplete "Y" ;
pubmed:pagination "651-62" ;
pubmed:dateRevised "2011-11-17" ;
pubmed:meshHeading pubmed-meshheading:21432781-Humans , pubmed-meshheading:21432781-Animals , pubmed-meshheading:21432781-Mice , pubmed-meshheading:21432781-Neoplasms , pubmed-meshheading:21432781-Insulin , , , , , , , , , , , , ;
pubmed:year "2011" ;
pubmed:articleTitle "Akt1 and Akt2: differentiating the aktion." ;
pubmed:affiliation "Cell Cycle and Myogenesis, Institut de Génétique Humaine, CNRS UPR1142, Montpellier, France. lisa.heron-milhavet@igh.cnrs.fr" ;
pubmed:publicationType "Journal Article" , "Review" .