Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A DNA damage-activated checkpoint kinase phosphorylates tau and enhances tau-induced neurodegeneration.

Human molecular genetics - 15 May 2010

Iijima-Ando Kanae, Zhao LiJuan, Gatt Anthony, Shenton Christopher, Iijima Koichi

Abstract excerpt

Hyperphosphorylation of the microtubule associated protein tau is detected in the brains of individuals with a range of neurodegenerative diseases including Alzheimer's disease (AD). An imbalance in phosphorylation and/or dephosphorylation of tau at disease-related sites has been suggested to initiate the abnormal metabolism and toxicity of tau in disease pathogenesis. However, the mechanisms underlying abnormal...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Checkpoint Kinase 1
Share to Checkpoint Kinase 2

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Enzyme Activation

Share to Nerve Degeneration

Share to Phosphoserine

Share to Protein Kinases

Share to Retinal Degeneration

Share to tau Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 20159774
DOI: 10.1093/hmg/ddq068
PMCID: PMC2860892

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A DNA damage-activated checkpoint kinase phosphorylates tau and enhances tau-induced neurodegeneration.PMID 20159774Read ↗

Tau Ser262 phosphorylation is critical for A 42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's diseaseSemantic proximity Read ↗

DLK-MAPK Signaling Coupled with DNA Damage Promotes Intrinsic Neurotoxicity Associated with Non-Mutated Tau.Semantic proximity Read ↗

P301L tau mutation leads to alterations of cell cycle, DNA damage response and apoptosis: Evidence for a role of tau in cancer.Semantic proximity Read ↗

TTBK2: a tau protein kinase beyond tau phosphorylation.Semantic proximity Read ↗

Modeling Alzheimer’s disease in primary neurons reveals DNA damage response coupled with MAPK-DLK signaling in wild-type tau-induced neurodegenerationSemantic proximity Read ↗

Genetic Modifiers of Tauopathy in DrosophilaSemantic proximity Read ↗

MARK4 with an Alzheimer’s disease-related mutation promotes tau hyperphosphorylation directly and indirectly and exacerbates neurodegenerationSemantic proximity Read ↗

A neuroprotective role for the DNA damage checkpoint in tauopathySemantic proximity Read ↗

Pseudo-acetylation of multiple sites on human Tau proteins alters Tau phosphorylation and microtubule binding, and ameliorates amyloid beta toxicitySemantic proximity Read ↗

Failure of DNA double-strand break repair by tau mediates Alzheimer’s disease pathology in vitroSemantic proximity Read ↗

Mutations in TTBK2, encoding a kinase implicated in tau phosphorylation, segregate with spinocerebellar ataxia type 11Semantic proximity Read ↗

Protein Kinase CK2 and Its Potential Role as a Therapeutic Target in Huntington’s DiseaseSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.