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

β-hairpin-mediated nucleation of polyglutamine amyloid formation.

Journal of molecular biology - 12 Apr 2013

Kar Karunakar, Hoop Cody L, Drombosky Kenneth W, Baker Matthew A, Kodali Ravindra, Arduini Irene, van der Wel Patrick C A, Horne W Seth, Wetzel Ronald

Abstract excerpt

The conformational preferences of polyglutamine (polyQ) sequences are of major interest because of their central importance in the expanded CAG repeat diseases that include Huntington's disease. Here, we explore the response of various biophysical parameters to the introduction of β-hairpin motifs within polyQ sequences. These motifs (tryptophan zipper, disulfide, d-Pro-Gly, Coulombic attraction, l-Pro-Gly)...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Glutamine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Huntingtin Protein

Share to Magnetic Resonance Spectroscopy

Share to Microscopy, Confocal

Share to Microscopy, Electron

Share to PC12 Cells

Share to Spectroscopy, Fourier Transform Infrared

Source

Open in PubMed Open full text

Identifiers

PMID: 23353826
DOI: 10.1016/j.jmb.2013.01.016
PMCID: PMC3602386

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

β-hairpin-mediated nucleation of polyglutamine amyloid formation.PMID 23353826Read ↗

The polyglutamine amyloid nucleus in living cells is a monomer with competing dimensions of orderSemantic proximity Read ↗

Pathologic polyglutamine aggregation begins with a self-poisoning polymer crystalSemantic proximity Read ↗

Structure propensities in mutated polyglutamine peptides.Semantic proximity Read ↗

Normal-repeat-length polyglutamine peptides accelerate aggregation nucleation and cytotoxicity of expanded polyglutamine proteinsSemantic proximity Read ↗

Mutational analysis of the structural organization of polyglutamine aggregates.Semantic proximity Read ↗

The structural plasticity of polyglutamine repeatsSemantic proximity Read ↗

Investigating Mutations to Reduce Huntingtin Aggregation by Increasing Htt-N-Terminal Stability and Weakening Interactions with PolyQ Domain.Semantic proximity Read ↗

Polyglutamine expansion mutation yields a pathological epitope linked to nucleation of protein aggregate: determinant of Huntington's disease onset.Semantic proximity Read ↗

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

Stabilization of elongated polyglutamine tracts by a helical peptide derived from N-terminal huntingtin.Semantic proximity Read ↗

Exceptional aggregation propensity of amino acids in polyglutamine amino-acid-homopolymerSemantic proximity Read ↗

A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: evidence for a compact beta-sheet structure.Semantic proximity Read ↗

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