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

Time-resolved FRET screening identifies small molecular modifiers of mutant Huntingtin conformational inflexibility in patient-derived cells.

SLAS discovery : advancing life sciences R & D - 1 Jun 2022

Wilbertz Johannes H, Frappier Julia, Muller Sandra, Gratzer Sabine, Englaro Walter, Stanek Lisa M, Calamini Barbara

Abstract excerpt

Huntington's disease (HD) is the most common monogenic neurodegenerative disease and is fatal. CAG repeat expansions in mutant Huntingtin (mHTT) exon 1 encode for polyglutamine (polyQ) stretches and influence age of onset and disease severity, depending on their length. mHTT is more structured compared to wild-type (wt) HTT, resulting in a decreased N-terminal conformational flexibility. mHTT inflexibility may...

Read the complete abstract on PubMed

Topics

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

Share to Fluorescence Resonance Energy Transfer
Share to Huntingtin Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Huntington Disease

Share to Mutation

Share to Nerve Tissue Proteins

Share to Neurodegenerative Diseases

Source

Identifiers

PMID: 35058188
DOI: 10.1016/j.slasd.2021.10.005

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

Time-resolved FRET screening identifies small molecular modifiers of mutant Huntingtin conformational inflexibility in patient-derived cells.PMID 35058188Read ↗

Time-resolved FRET screening identifies small molecular modifiers of mutant Huntingtin conformational inflexibility in patient-derived cellsSemantic proximity Read ↗

Discovery of Small Molecule Inhibitors of Huntingtin Exon 1 Aggregation by FRET-Based High-Throughput Screening in Living Cells.Semantic proximity Read ↗

Polyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopy.Semantic proximity Read ↗

High-Affinity, Structure-Validated and Selective Macrocyclic Peptide Tools for Chemical Biology Studies of HuntingtinSemantic proximity Read ↗

PET Ligands for Imaging Mutant Huntingtin Aggregates: A Case Study in Non-For-Profit Scientific Management.Semantic proximity Read ↗

TR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes.Semantic proximity Read ↗

Highly Potent Peptide Therapeutics To Prevent Protein Aggregation In Huntington’s DiseaseSemantic proximity Read ↗

Mutant huntingtin fragmentation in immune cells tracks Huntington's disease progression.Semantic proximity Read ↗

Macrocyclic Peptide Tools for Huntingtin-bound HAP40Semantic proximity Read ↗

Conformational dynamics of Tau in the cell quantified by an intramolecular FRET biosensor in physiological and pathological contextSemantic proximity Read ↗

Expanding the Huntington’s disease research toolbox; validated subdomain protein constructs for biochemical and structural investigation of huntingtinSemantic proximity Read ↗

Immuno-based detection assays to quantify distinct mutant huntingtin conformations in biological samples.Semantic proximity Read ↗

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