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

Development of new fusion proteins for visualizing amyloid-β oligomers in vivo

16 Mar 2016

Abstract excerpt

The intracellular accumulation of amyloid-β (Aβ) oligomers critically contributes to disease progression in Alzheimer's disease (AD) and can be the potential target of AD therapy. Direct observation of molecular dynamics of Aβ oligomers in vivo is key for drug discovery research, however, it has been challenging because Aβ aggregation inhibits the fluorescence from fusion proteins. Here, we developed Aβ1-42-GFP...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer's disease research and treatments
Share to Prion Diseases and Protein Misfolding
Share to Protein Structure and Dynamics

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 26982553
DOI: 10.1038/srep22712

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Development of new fusion proteins for visualizing amyloid-β oligomers in vivoPMID 26982553Read ↗

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

Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by SequestrationSemantic proximity Read ↗

Rational design of amyloid beta peptide-binding proteins: pseudo-Abeta beta-sheet surface presented in green fluorescent protein binds tightly and preferentially to structured Abeta.Semantic proximity Read ↗

Mitigating protein aggregation to reduce the toxicity inherent to Parkinson's and Alzheimer's diseasesSemantic proximity Read ↗

Misfolded amyloid β-42 induced impairment of the endosomal-lysosomal pathway revealed by real-time optical monitoringSemantic proximity Read ↗

Extracellular Monomeric Tau Protein Is Sufficient to Initiate the Spread of Tau Protein PathologySemantic proximity Read ↗

Efficient imaging of amyloid deposits in Drosophila models of human amyloidoses.Semantic proximity Read ↗

Significant structural differences between transient amyloid-β oligomers and less-toxic fibrils in regions known to harbor familial Alzheimer's mutations.Semantic proximity Read ↗

A genetically encoded selection for amyloid-β oligomer bindersSemantic proximity Read ↗

Self-assembly of FUS through its low-complexity domain contributes to neurodegeneration.Semantic proximity Read ↗

A commonly used Drosophila model of Alzheimer's disease generates an aberrant species of amyloid-β with an additional N-terminal glutamine residue.Semantic proximity Read ↗

Aβ43 is neurotoxic and primes aggregation of Aβ40 in vivoSemantic proximity Read ↗

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