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

Glassy dynamics in mutant huntingtin proteins.

The Journal of chemical physics - 21 Aug 2018

Kang Hongsuk, Luan Binquan, Zhou Ruhong

Abstract excerpt

Causative to the neurodegenerative Huntington's disease (HD), a mutational huntingtin (HTT) protein consists of an unusual expansion on the poly-glutamine (polyQ) region in the first exon (exon-1) domain. Despite its significance on HD progression, the structural role of the exon-1 with the polyQ region is still elusive. As HTT is an intrinsically disordered protein (IDP), a large ensemble of various...

Read the complete abstract on PubMed

Topics

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

Share to Huntingtin Protein
Share to Intrinsically Disordered Proteins
Share to Isomerism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Proline

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Domains

Source

Identifiers

PMID: 30134683
DOI: 10.1063/1.5029369

Genes

HTT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Glassy dynamics in mutant huntingtin proteins.PMID 30134683Read ↗

Emerging β-Sheet Rich Conformations in Supercompact Huntingtin Exon-1 Mutant Structures.Semantic proximity Read ↗

Mutation effects on structural stability of polyglutamine peptides by molecular dynamics simulation.Semantic proximity Read ↗

The structure of pathogenic huntingtin exon-1 defines the bases of its aggregation propensitySemantic 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 ↗

Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.Semantic proximity Read ↗

Integrative determination of the atomic structure of mutant huntingtin exon 1 fibrils implicated in Huntington’s diseaseSemantic proximity Read ↗

Integrative determination of atomic structure of mutant huntingtin exon 1 fibrils implicated in Huntington disease.Semantic proximity Read ↗

Dissecting how ALS-associated D290V mutation enhances pathogenic aggregation of hnRNPA2286-291 peptides: Dynamics and conformational ensembles.Semantic proximity Read ↗

Kinetic network models of tryptophan mutations in β-hairpins reveal the importance of non-native interactions.Semantic proximity Read ↗

The physics of liquid-to-solid transitions in multi-domain protein condensatesSemantic proximity Read ↗

Aggregation landscapes of Huntingtin exon 1 protein fragments and the critical repeat length for the onset of Huntington’s diseaseSemantic proximity Read ↗

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

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