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

Self-assembly pathways of E22Δ-type amyloid β peptide mutants generated from non-aggregative O-acyl isopeptide precursors.

Bioorganic & medicinal chemistry - 15 Jun 2011

Sohma Youhei, Wang Hui, Taniguchi Atsuhiko, Hirayama Yuta, Kakizawa Taeko, Yamasaki Moe, Mukai Hidehito, Kiso Yoshiaki

Abstract excerpt

The recently identified E22Δ-type amyloid β peptide (Aβ) mutants are reported to favor oligomerization over fibrillization and to exhibit more-potent synaptotoxicity than does wild-type (WT) Aβ. Aβ(E22Δ) mutants can thus be expected to serve as tools for clarifying the impact of Aβ oligomers in Alzheimer's disease (or Alzheimer's-type dementia). However, the biochemical and biophysical properties of Aβ(E22Δ) have...

Read the complete abstract on PubMed

Topics

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

Share to Acylation
Share to Amyloid beta-Peptides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Blotting, Western

Share to Cell Survival

Share to Circular Dichroism

Share to PC12 Cells

Share to Peptide Fragments

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 21612934
DOI: 10.1016/j.bmc.2011.04.056

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Self-assembly pathways of E22Δ-type amyloid β peptide mutants generated from non-aggregative O-acyl isopeptide precursors.PMID 21612934Read ↗

The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseasesSemantic proximity Read ↗

The Structures of the E22Δ Mutant-Type Amyloid-β Alloforms and the Impact of E22Δ Mutation on the Structures of the Wild-Type Amyloid-β AlloformsSemantic proximity Read ↗

Molecular engineering of a secreted, highly homogeneous, and neurotoxic aβ dimer.Semantic proximity Read ↗

Synthetic and Biophysical Studies on the Toxic Conformer in Amyloid β with the E22Δ Mutation in Alzheimer Pathology.Semantic proximity Read ↗

Characterization of intermediate steps in amyloid beta (Aβ) production under near-native conditions.Semantic proximity Read ↗

Design of non-aggregating variants of Aβ peptide.Semantic proximity Read ↗

Amyloid β-Protein Assembly: Differential Effects of the Protective A2T Mutation and Recessive A2V Familial Alzheimer's Disease Mutation.Semantic proximity Read ↗

Direct evidence for self-propagation of different amyloid-β fibril conformations.Semantic proximity Read ↗

The Osaka FAD mutation E22Δ leads to the formation of a previously unknown type of amyloid β fibrils and modulates Aβ neurotoxicity.Semantic proximity Read ↗

'O-Acyl isopeptide method' for the efficient preparation of amyloid beta peptide 1-42 mutants.Semantic proximity Read ↗

The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly.Semantic proximity Read ↗

A turn for the worse: Aβ β-hairpins in Alzheimer’s diseaseSemantic proximity Read ↗

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