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

Disease-related modifications in tau affect the interaction between Fyn and Tau.

The Journal of biological chemistry - 21 Oct 2005

Bhaskar Kiran, Yen Shu-Hui, Lee Gloria

Abstract excerpt

Microtubule-associated protein tau is the major component of the neurofibrillary tangles of Alzheimer disease (AD) and is genetically linked to frontotemporal dementias (FTDP-17). We have recently shown that tau interacts with the SH3 domain of Fyn, an Src family non-receptor tyrosine kinase, and is tyrosine-phosphorylated by Fyn on Tyr-18. Also, tyrosine-phosphorylated tau is present in the neuropathology of AD....

Read the complete abstract on PubMed

Topics

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

Share to Glutathione Transferase
Share to Microtubules
Share to Neurodegenerative Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Proto-Oncogene Proteins c-fyn

Share to src Homology Domains

Share to Surface Plasmon Resonance

Share to tau Proteins

Share to Tyrosine

Source

Identifiers

PMID: 16115884
DOI: 10.1074/jbc.M505895200

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

Disease-related modifications in tau affect the interaction between Fyn and Tau.PMID 16115884Read ↗

Tyrosine phosphorylation of tau accompanies disease progression in transgenic mouse models of tauopathySemantic proximity Read ↗

Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of TauSemantic proximity Read ↗

Promotion of hyperphosphorylation by frontotemporal dementia tau mutations.Semantic proximity Read ↗

FTDP-17 Mutations Alter the Aggregation and Microtubule Stabilization Propensity of Tau in an Isoform-Specific FashionSemantic proximity Read ↗

Tau interacts with src-family non-receptor tyrosine kinasesSemantic proximity Read ↗

Phosphorylation in the amino terminus of tau prevents inhibition of anterograde axonal transport.Semantic proximity Read ↗

Tau proteins with frontotemporal dementia-17 mutations have both altered expression levels and phosphorylation profiles in differentiated neuroblastoma cells.Semantic proximity Read ↗

Regulatory region genetic variation is associated with FYN expression in Alzheimer's disease.Semantic 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 ↗

A peptide inhibitor of Tau-SH3 interactions ameliorates amyloid-β toxicitySemantic proximity Read ↗

[Molecular analysis of tau deposited in the FTDP-17 brain].Semantic proximity Read ↗

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