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

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

Scientific reports - 7 Jul 2014

Cui Xiaotian, Liang Qingnan, Liang Yijian, Lu Mingxing, Ding Yu, Lu Boxun

Abstract excerpt

Time-Resolved Fluorescence Resonance Energy Transfer (TR-FRET) technology is a widely used immunoassay that enables high-throughput quantitative measurements of proteins of interest. One of the well established examples is the TR-FRET assay for mutant huntingtin protein (HTT), which is the major cause of the neurodegenerative Huntington's disease (HD). To measure the mutant HTT protein, the published assays...

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 HEK293 Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Huntingtin Protein

Share to Peptide Fragments

Share to Peptides

Share to Protein Stability

Share to Solubility

Share to Transition Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 24998512
DOI: 10.1038/srep05601
PMCID: PMC4083280

Genes

HTT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

TR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes.PMID 24998512Read ↗

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

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

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

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

Identification of distinct conformations associated with monomers and fibril assemblies of mutant huntingtinSemantic proximity Read ↗

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

A precise and general FRET-based method for monitoring structural transitions in protein self-organizationSemantic proximity Read ↗

Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment.Semantic proximity Read ↗

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

The structural basis of huntingtin (Htt) fibril polymorphism, revealed by cryo-EM of exon 1 Htt fibrilsSemantic proximity Read ↗

The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain.Semantic proximity Read ↗

FibrilPaints for visualisation and ubiquitination of Huntingtin amyloid fibrilsSemantic proximity Read ↗

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