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

Substrate-specific reduction of PP2A activity exaggerates tau pathology.

Biochemical and biophysical research communications - 6 Feb 2009

Deters Natasha, Ittner Lars M, Götz Jürgen

Abstract excerpt

Phosphorylation of the microtubule-associated protein tau is regulated by the balanced interplay of kinases and phosphatases. Disturbance of this balance causes hyperphosphorylation of tau and neurofibrillary tangle formation in Alzheimer's disease brain. Here, we crossed Dom5 mice that express a substrate-specific dominant negative mutant form, L309A Calpha, of protein phosphatase 2A (PP2A) with...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer Disease
Share to Neurofibrillary Tangles
Share to Phosphorylation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Phosphatase 2

Share to Protein Subunits

Share to Solubility

Share to Substrate Specificity

Share to tau Proteins

Source

Identifiers

PMID: 19126401
DOI: 10.1016/j.bbrc.2008.12.140

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Substrate-specific reduction of PP2A activity exaggerates tau pathology.PMID 19126401Read ↗

Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice.Semantic proximity Read ↗

Altered phosphorylation of cytoskeletal proteins in mutant protein phosphatase 2A transgenic mice.Semantic proximity Read ↗

β-Amyloid Induces Pathology-Related Patterns of Tau Hyperphosphorylation at Synaptic Terminals.Semantic proximity Read ↗

Inhibition of Polo-like kinase 2 ameliorates pathogenesis in Alzheimer’s disease model miceSemantic proximity Read ↗

Mechanisms of tau-induced neurodegeneration.Semantic proximity Read ↗

Broad Kinase Inhibition Mitigates Early Neuronal Dysfunction in TauopathySemantic proximity Read ↗

EPAC2 knockout causes abnormal tau pathology through calpain-mediated CDK5 activationSemantic proximity Read ↗

Modulating Protein Phosphatase 2A Rescues Disease Phenotype in Neurodegenerative Tauopathies.Semantic proximity Read ↗

Pathological phosphorylation of tau and TDP-43 by TTBK1 and TTBK2 drives neurodegenerationSemantic proximity Read ↗

Neurofibrillary pathology in transgenic mice overexpressing V717F beta-amyloid precursor protein.Semantic proximity Read ↗

Tau-tubulin kinase 1 enhances prefibrillar tau aggregation and motor neuron degeneration in P301L FTDP-17 tau-mutant mice.Semantic proximity Read ↗

Phosphorylated PP2A (tyrosine 307) is associated with Alzheimer neurofibrillary pathology.Semantic proximity Read ↗

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