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

The Nt17 Domain and its Helical Conformation Regulate the Aggregation, Cellular Properties and Neurotoxicity of Mutant Huntingtin Exon 1.

Journal of molecular biology - 15 Oct 2021

Vieweg Sophie, Mahul-Mellier Anne-Laure, Ruggeri Francesco S, Riguet Nathan, DeGuire Sean M, Chiki Anass, Cendrowska Urszula, Dietler Giovanni, Lashuel Hilal A

Abstract excerpt

Converging evidence points to the N-terminal domain comprising the first 17 amino acids of the Huntingtin protein (Nt17) as a key regulator of its aggregation, cellular properties and toxicity. In this study, we further investigated the interplay between Nt17 and the polyQ domain repeat length in regulating the aggregation and inclusion formation of exon 1 of the Huntingtin protein (Httex1). In addition, we...

Read the complete abstract on PubMed

Topics

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

Share to Corpus Striatum
Share to Cryoelectron Microscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Huntingtin Protein

Share to Microscopy, Atomic Force

Share to Primary Cell Culture

Share to Protein Aggregates

Share to Protein Conformation, alpha-Helical

Share to Protein Engineering

Source

Identifiers

PMID: 34492254
DOI: 10.1016/j.jmb.2021.167222

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

The Nt17 Domain and its Helical Conformation Regulate the Aggregation, Cellular Properties and Neurotoxicity of Mutant Huntingtin Exon 1.PMID 34492254Read ↗

N-terminal Huntingtin (Htt) phosphorylation is a molecular switch regulating Htt aggregation, helical conformation, internalization, and nuclear targeting.Semantic proximity Read ↗

Amplification of neurotoxic HTTex1 assemblies in human neurons.Semantic proximity Read ↗

Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6.Semantic proximity Read ↗

An N-terminal nuclear export signal regulates trafficking and aggregation of Huntingtin (Htt) protein exon 1.Semantic proximity Read ↗

Protofilament Structure and Supramolecular Polymorphism of Aggregated Mutant Huntingtin Exon 1.Semantic proximity Read ↗

Spontaneous self-assembly of pathogenic huntingtin exon 1 protein into amyloid structures.Semantic proximity Read ↗

The N17 domain mitigates nuclear toxicity in a novel zebrafish Huntington's disease model.Semantic proximity Read ↗

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

Site-Specific Phosphorylation of Huntingtin Exon 1 Recombinant Proteins Enabled by the Discovery of Novel Kinases.Semantic proximity Read ↗

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

Chaperone protein HYPK interacts with the first 17 amino acid region of Huntingtin and modulates mutant HTT-mediated aggregation and cytotoxicity.Semantic proximity Read ↗

Sonicated fibrils of huntingtin exon-1 preferentially seed neurons and produce toxic assembliesSemantic proximity Read ↗

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