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000141416 0247_ $$2doi$$a10.3233/JAD-2011-110320
000141416 0247_ $$2pmid$$apmid:21628793
000141416 0247_ $$2ISSN$$a1387-2877
000141416 0247_ $$2ISSN$$a1875-8908
000141416 037__ $$aDZNE-2020-07738
000141416 041__ $$aEnglish
000141416 082__ $$a610
000141416 1001_ $$aPloia, Cristina$$b0
000141416 245__ $$aJNK plays a key role in tau hyperphosphorylation in Alzheimer's disease models.
000141416 260__ $$aAmsterdam$$bIOS Press$$c2011
000141416 264_1 $$2Crossref$$3print$$bIOS Press$$c2011-09-09
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000141416 520__ $$aAlzheimer's disease (AD) is a major clinical concern, and the search for new molecules to combat disease progression remains important. One of the major hallmarks in AD pathogenesis is the hyperphosphorylation of tau and subsequent formation of neurofibrillary tangles. Several kinases are involved in this process. Amongst them, c-Jun N-terminal kinases (JNKs) are activated in AD brains and are also associated with the development of amyloid plaques. This study was designed to investigate the contribution of JNK in tau hyperphosphorylation and whether it may represent a potential therapeutic target for the fight against AD. The specific inhibition of JNK by the cell permeable peptide D-JNKI-1 led to a reduction of p-tau at S202/T205 and S422, two established target sites of JNK, in rat neuronal cultures and in human fibroblasts cultures. Similarly, D-JNKI-1 reduced p-tau at S202/T205 in an in vivo model of AD (TgCRND8 mice). Our findings support the fundamental role of JNK in the regulation of tau hyperphosphorylation and subsequently in AD pathogenesis.
000141416 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
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000141416 650_7 $$2NLM Chemicals$$atau Proteins
000141416 650_7 $$0EC 2.7.11.24$$2NLM Chemicals$$aJNK Mitogen-Activated Protein Kinases
000141416 650_7 $$0EC 2.7.11.24$$2NLM Chemicals$$aMitogen-Activated Protein Kinases
000141416 650_2 $$2MeSH$$aAged
000141416 650_2 $$2MeSH$$aAged, 80 and over
000141416 650_2 $$2MeSH$$aAlzheimer Disease: metabolism
000141416 650_2 $$2MeSH$$aAlzheimer Disease: pathology
000141416 650_2 $$2MeSH$$aAnimals
000141416 650_2 $$2MeSH$$aCells, Cultured
000141416 650_2 $$2MeSH$$aCerebral Cortex: drug effects
000141416 650_2 $$2MeSH$$aCerebral Cortex: metabolism
000141416 650_2 $$2MeSH$$aCerebral Cortex: pathology
000141416 650_2 $$2MeSH$$aFemale
000141416 650_2 $$2MeSH$$aHumans
000141416 650_2 $$2MeSH$$aJNK Mitogen-Activated Protein Kinases: metabolism
000141416 650_2 $$2MeSH$$aJNK Mitogen-Activated Protein Kinases: pharmacology
000141416 650_2 $$2MeSH$$aMale
000141416 650_2 $$2MeSH$$aMiddle Aged
000141416 650_2 $$2MeSH$$aMitogen-Activated Protein Kinases: metabolism
000141416 650_2 $$2MeSH$$aNeurofibrillary Tangles: drug effects
000141416 650_2 $$2MeSH$$aNeurofibrillary Tangles: metabolism
000141416 650_2 $$2MeSH$$aNeurofibrillary Tangles: pathology
000141416 650_2 $$2MeSH$$aNeurons: drug effects
000141416 650_2 $$2MeSH$$aNeurons: metabolism
000141416 650_2 $$2MeSH$$aNeurons: pathology
000141416 650_2 $$2MeSH$$aPhosphorylation
000141416 650_2 $$2MeSH$$aRats
000141416 650_2 $$2MeSH$$atau Proteins: metabolism
000141416 7001_ $$aAntoniou, Xanthi$$b1
000141416 7001_ $$aSclip, Alessandra$$b2
000141416 7001_ $$aGrande, Valentina$$b3
000141416 7001_ $$aCardinetti, Daniele$$b4
000141416 7001_ $$0P:(DE-2719)2340744$$aColombo, Alessio$$b5$$udzne
000141416 7001_ $$aCanu, Nadia$$b6
000141416 7001_ $$aBenussi, Luisa$$b7
000141416 7001_ $$aGhidoni, Roberta$$b8
000141416 7001_ $$aForloni, Gianluigi$$b9
000141416 7001_ $$0P:(DE-HGF)0$$aBorsello, Tiziana$$b10$$eCorresponding author
000141416 77318 $$2Crossref$$3journal-article$$a10.3233/jad-2011-110320$$b : IOS Press, 2011-09-09$$n2$$p315-329$$tJournal of Alzheimer's Disease$$v26$$x1875-8908$$y2011
000141416 773__ $$0PERI:(DE-600)2070772-1$$a10.3233/JAD-2011-110320$$gVol. 26, no. 2, p. 315 - 329$$n2$$p315-329$$q26:2<315 - 329$$tJournal of Alzheimer's disease$$v26$$x1875-8908$$y2011
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