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

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

Protein engineering, design & selection : PEDS - 1 Sept 2013

Ikura Teikichi, Ito Nobutoshi

Abstract excerpt

The Alzheimer's disease-related protein, tau, aggregates into neurofibrillary tangles when it is hyperphosphorylated. The amino acid sequence included in the third repeat (R3) of the microtubule-binding region is suspected to be the main factor for tau aggregation. Here, we synthesized a 31-resid...

Read the complete abstract on PubMed

Topics

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

Share to Hydrophobic and Hydrophilic Interactions
Share to Peptides
Share to Peptidylprolyl Isomerase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Multimerization

Share to Solutions

Share to Spectrometry, Fluorescence

Share to Stereoisomerism

Share to tau Proteins

Source

Identifiers

PMID: 23832849
DOI: 10.1093/protein/gzt033

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-23832849-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Peptidyl-prolyl isomerase activity of FK506 binding protein 12 prevents tau peptide from aggregating.PMID 23832849Read ↗

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.Semantic proximity Read ↗

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

Saccharomyces cerevisiae Fpr1 functions as a chaperone to inhibit protein aggregation.Semantic proximity Read ↗

Functional interactions as a survival strategy against abnormal aggregation.Semantic proximity Read ↗

The β-turn-supporting motif in the polyglutamine binding peptide QBP1 is essential for inhibiting huntingtin aggregation.Semantic proximity Read ↗

Conformational switch of polyglutamine-expanded huntingtin into benign aggregates leads to neuroprotective effect.Semantic proximity Read ↗

Proline repeats, in cis- and trans-positions, confer protection against the toxicity of misfolded proteins in a mammalian cellular model.Semantic proximity Read ↗

FK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53T.Semantic proximity Read ↗

Multimer formation by FKBP-12: roles for cysteine 23 and phenylalanine 36.Semantic proximity Read ↗

Amyloid formation under physiological conditions proceeds via a native-like folding intermediate.Semantic proximity Read ↗

Amyloid fibrils from the viewpoint of protein folding.Semantic proximity Read ↗

Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro117 cis/trans isomerization.Semantic proximity Read ↗

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