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

Effects of endogenous beta-amyloid overproduction on tau phosphorylation in cell culture.

Journal of neurochemistry - 1 Aug 2006

Wang Ze-Fen, Li Hong-Lian, Li Xia-Chun, Zhang Qi, Tian Qing, Wang Qun, Xu Huaxi, Wang Jian-Zhi

Abstract excerpt

Alzheimer's disease is characterized by beta-amyloid (Abeta) overproduction and tau hyperphosphorylation. Recent studies have shown that synthetic Abeta promotes tau phosphorylation in vitro. However, whether endogenously overproduced Abeta promotes tau phosphorylation and the underlying mechanisms remain unknown. Here, we used mouse neuroblastoma N2a stably expressing wild-type amyloid precursor protein (APPwt)...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid beta-Protein Precursor
Share to Culture Media

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclin-Dependent Kinase 5

Share to Enzyme Inhibitors

Share to Glycogen Synthase Kinase 3

Share to Neuroblastoma

Share to Protein Kinase C

Share to tau Proteins

Source

Identifiers

PMID: 16762022
DOI: 10.1111/j.1471-4159.2006.03956.x

Genes

APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effects of endogenous beta-amyloid overproduction on tau phosphorylation in cell culture.PMID 16762022Read ↗

Glycogen synthase kinase-3 beta phosphorylates tau protein at multiple sites in intact cells.Semantic proximity Read ↗

Alzheimer's disease genetic mutation evokes ultrastructural alterations: correlation to an intracellular Abeta deposition and the level of GSK-3beta-P(Y216) phosphorylated form.Semantic proximity Read ↗

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

Dual effects of PKNalpha and protein kinase C on phosphorylation of tau protein by glycogen synthase kinase-3beta.Semantic proximity Read ↗

Functional Implications of Glycogen Synthase Kinase‐3‐Mediated Tau PhosphorylationSemantic proximity Read ↗

Current Advances on Different Kinases Involved in Tau Phosphorylation, and Implications in Alzheimers Disease and TauopathiesSemantic proximity Read ↗

Transgenic mouse and cell culture models demonstrate a lack of mechanistic connection between endoplasmic reticulum stress and tau dysfunction.Semantic proximity Read ↗

Different tau epitopes define Abeta42-mediated tau insolubility.Semantic proximity Read ↗

Abnormally phosphorylated tau in SY5Y human neuroblastoma cellsSemantic proximity Read ↗

Deposition of Phosphorylated α-Synuclein and Activation of GSK-3β and PP2A in the PS19 Mouse Model of Tauopathy.Semantic proximity Read ↗

Differential phosphorylation of human tau isoforms containing three repeats by several protein kinases.Semantic proximity Read ↗

Quantitative and combinatory determination of in situ phosphorylation of tau and its FTDP-17 mutants.Semantic proximity Read ↗

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