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Article

Phosphorylation of FTDP-17 mutant tau by cyclin-dependent kinase 5 complexed with p35, p25, or p39.

The Journal of biological chemistry - 9 Sept 2005

Sakaue Fumika, Saito Taro, Sato Yutaka, Asada Akiko, Ishiguro Koichi, Hasegawa Masato, Hisanaga Shin-ichi

Abstract excerpt

One of the major pathological hallmarks of Alzheimer disease is neurofibrillary tangles. Neurofibrillary tangles are bundles of paired helical filaments composed of hyperphosphorylated tau. Cyclin-dependent kinase 5 (Cdk5) is one of the tau protein kinases that increase paired helical filament epitopes in tau by phosphorylation. Recently, various mutations of tau have been identified in frontotemporal dementia...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 15994305
DOI: 10.1074/jbc.M504792200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Phosphorylation of FTDP-17 mutant tau by cyclin-dependent kinase 5 complexed with p35, p25, or p39.PMID 15994305Read ↗

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Effect of Pin1 or microtubule binding on dephosphorylation of FTDP-17 mutant Tau.Semantic proximity Read ↗

Cdk5 Is a Key Factor in Tau Aggregation and Tangle Formation In VivoSemantic proximity Read ↗

Sites of phosphorylation in tau and factors affecting their regulation.Semantic proximity Read ↗

Distinct FTDP-17 missense mutations in tau produce tau aggregates and other pathological phenotypes in transfected CHO cells.Semantic proximity Read ↗

The FTDP‐17‐Linked Mutation R406W Abolishes the Interaction of Phosphorylated Tau with MicrotubulesSemantic proximity Read ↗

Accelerated filament formation from tau protein with specific FTDP‐17 missense mutationsSemantic proximity Read ↗

Physiological and Pathological Roles of Cdk5: Potential Directions for Therapeutic Targeting in Neurodegenerative DiseaseSemantic proximity Read ↗

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