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

The trans isomer of Tau peptide is prone to aggregate, and the WW domain of Pin1 drastically decreases its aggregation.

FEBS letters - 1 Sept 2018

Ikura Teikichi, Tochio Naoya, Kawasaki Ryosuke, Matsuzaki Mizuki, Narita Akihiro, Kikumoto Mahito, Utsunomiya-Tate Naoko, Tate Shin-Ichi, Ito Nobutoshi

Abstract excerpt

In Alzheimer's, the disease-related protein Tau is hyperphosphorylated and aggregates into neurofibrillary tangles (NFT). The cis isomer of the phosphorylated Thr231-Pro232 has been proposed as a precursor of aggregation ('Cistauosis'), but this aggregation scheme is not yet completely accepted. Here, we synthesized peptides comprising a phosphorylated region including Thr231-Pro232 and an aggregation-core region...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to NIMA-Interacting Peptidylprolyl Isomerase

Share to Peptides

Share to Protein Aggregation, Pathological

Share to Protein Isoforms

Share to tau Proteins

Source

Identifiers

PMID: 30079475
DOI: 10.1002/1873-3468.13218

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The trans isomer of Tau peptide is prone to aggregate, and the WW domain of Pin1 drastically decreases its aggregation.PMID 30079475Read ↗

<b>Cis</b>phosphorylated tau as the earliest detectable pathogenic conformation in Alzheimer disease, offering novel diagnostic and therapeutic strategiesSemantic proximity Read ↗

Isomerase Pin1 stimulates dephosphorylation of tau protein at cyclin-dependent kinase (Cdk5)-dependent Alzheimer phosphorylation sites.Semantic proximity Read ↗

Pin1 has opposite effects on wild-type and P301L tau stability and tauopathy.Semantic proximity Read ↗

Pin1 Regulatory miRNAs as Novel Candidates for Alzheimer’s Disease TreatmentSemantic proximity Read ↗

Effects of naturally occurring charged mutations on the structure, stability, and binding of the Pin1 WW domain.Semantic proximity Read ↗

Peptidyl-prolyl isomerase activity of FK506 binding protein 12 prevents tau peptide from aggregating.Semantic proximity Read ↗

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

DNA sequence variations in the prolyl isomerase Pin1 gene and Alzheimer's disease.Semantic proximity Read ↗

Preclinical characterization and IND‐enabling safety studies for PNT001, an antibody that recognizes <i>cis</i>‐pT231 tauSemantic proximity Read ↗

Bending Tau into Shape: The Emerging Role of Peptidyl-Prolyl Isomerases in TauopathiesSemantic proximity Read ↗

Unusually Rapid Isomerization of Aspartic Acid in TauSemantic proximity Read ↗

Relation between serum amyloid A truncated peptides and their suprastructure chirality.Semantic proximity Read ↗

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