Chile | Article
dc.creatorTramutola A.
dc.creatorSharma N.
dc.creatorBarone E.
dc.creatorLanzillotta C.
dc.creatorCastellani A.
dc.creatorIavarone F.
dc.creatorVincenzoni F.
dc.creatorCastagnola M.
dc.creatorButterfield D.A.
dc.creatorGaetani S.
dc.creatorCassano T.
dc.creatorPerluigi M.
dc.creatorDi Domenico F.
dc.date.accessioned2020-09-02T22:29:23Z
dc.date.accessioned2022-11-08T20:22:04Z
dc.date.available2020-09-02T22:29:23Z
dc.date.available2022-11-08T20:22:04Z
dc.date.created2020-09-02T22:29:23Z
dc.date.issued2018
dc.identifier1864, 10, 3309-3321
dc.identifier09254439
dc.identifierhttps://hdl.handle.net/20.500.12728/6438
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/5144277
dc.languageen
dc.publisherElsevier B.V.
dc.subjectAlzheimer disease
dc.subjectGlucose metabolism
dc.subjectInsulin signaling
dc.subjectO-GlcNAcylation
dc.subjectPhosphorylation
dc.subjectglucose
dc.subjectglucose transporter 3
dc.subjectinsulin
dc.subjectproteome
dc.subjectserine
dc.subjecttau protein
dc.subjectthreonine
dc.subjectbeta n acetylhexosaminidase
dc.subjecthexosaminidase C
dc.subjectinsulin receptor substrate
dc.subjectIRS1 protein, human
dc.subjectn acetylglucosamine
dc.subjectn acetylglucosaminyltransferase
dc.subjectOGT protein, human
dc.subjectprotein
dc.subjectprotein kinase B
dc.subjectacylation
dc.subjectAlzheimer disease
dc.subjectanimal experiment
dc.subjectanimal model
dc.subjectanimal tissue
dc.subjectArticle
dc.subjectcerebellum
dc.subjectcontrolled study
dc.subjectenzyme activity
dc.subjectglucose metabolism
dc.subjectglucose transport
dc.subjecthippocampus
dc.subjecthomogenate
dc.subjectimmunofluorescence
dc.subjectinsulin resistance
dc.subjectinsulin signaling
dc.subjectmale
dc.subjectmass spectrometry
dc.subjectmolecular pathology
dc.subjectmouse
dc.subjectmouse model
dc.subjectneuropathology
dc.subjectnon insulin dependent diabetes mellitus
dc.subjectnonhuman
dc.subjectpriority journal
dc.subjectprotein degradation
dc.subjectprotein phosphorylation
dc.subjectprotein targeting
dc.subjectproteomics
dc.subjecttransgenic mouse
dc.subjecttwo dimensional electrophoresis
dc.subjectWestern blotting
dc.subjectAlzheimer disease
dc.subjectanimal
dc.subjectbrain
dc.subjectdisease model
dc.subjectfemale
dc.subjectgenetics
dc.subjecthuman
dc.subjectmetabolism
dc.subjectphosphorylation
dc.subjectprocedures
dc.subjectproteomics
dc.subjectAcetylglucosamine
dc.subjectAlzheimer Disease
dc.subjectAnimals
dc.subjectbeta-N-Acetylhexosaminidases
dc.subjectBrain
dc.subjectDisease Models, Animal
dc.subjectFemale
dc.subjectHumans
dc.subjectInsulin Receptor Substrate Proteins
dc.subjectMale
dc.subjectMice
dc.subjectMice, Transgenic
dc.subjectN-Acetylglucosaminyltransferases
dc.subjectPhosphorylation
dc.subjectProteins
dc.subjectProteomics
dc.subjectProto-Oncogene Proteins c-akt
dc.titleProteomic identification of altered protein O-GlcNAcylation in a triple transgenic mouse model of Alzheimer's disease
dc.typeArticle


Este ítem pertenece a la siguiente institución