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polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction

polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction

http://www.wikidata.org/entity/Q34098314

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Fibrillogenesis of huntingtin and other glutamine containing proteins The structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice model Extended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein.Elongation kinetics of polyglutamine peptide fibrils: a quartz crystal microbalance with dissipation study.Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo.Dynamic imaging by fluorescence correlation spectroscopy identifies diverse populations of polyglutamine oligomers formed in vivo.Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies.Stable polyglutamine dimers can contain β-hairpins with interdigitated side chains-but not α-helices, β-nanotubes, β-pseudohelices, or steric zippers.Biophysical underpinnings of the repeat length dependence of polyglutamine amyloid formation Polyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences.The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence.A coarse-grained model for polyglutamine aggregation modulated by amphipathic flanking sequences Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides Normal-repeat-length polyglutamine peptides accelerate aggregation nucleation and cytotoxicity of expanded polyglutamine proteins Aggregation kinetics of interrupted polyglutamine peptides Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies.Polyglutamine expansion alters the dynamics and molecular architecture of aggregates in dentatorubropallidoluysian atrophy Structural transitions and oligomerization along polyalanine fibril formation pathways from computer simulations An Analysis of Biomolecular Force Fields for Simulations of Polyglutamine in Solution Nonnative protein polymers: structure, morphology, and relation to nucleation and growth.Kinetic mechanism of p53 oncogenic mutant aggregation and its inhibition.Quantitative connection between polyglutamine aggregation kinetics and neurodegenerative process in patients with Huntington's disease.A polymer physics perspective on driving forces and mechanisms for protein aggregation Slow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments.The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3.In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis.Nanoscale studies link amyloid maturity with polyglutamine diseases onset.Thermodynamics of beta-sheet formation in polyglutamine The impact of ataxin-1-like histidine insertions on polyglutamine aggregation Examining polyglutamine peptide length: a connection between collapsed conformations and increased aggregation.Mechanism of cis-inhibition of polyQ fibrillation by polyP: PPII oligomers and the hydrophobic effect.Structural motif of polyglutamine amyloid fibrils discerned with mixed-isotope infrared spectroscopy.Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.Inhibition of polyglutamine aggregation by SIMILAR huntingtin N-terminal sequences: Prospective molecules for preclinical evaluation in Huntington's disease.Backbone Engineering within a Latent β-Hairpin Structure to Design Inhibitors of Polyglutamine Amyloid Formation.Proteins Containing Expanded Polyglutamine Tracts and Neurodegenerative Disease.Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin.

P2860

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P2860

polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction

http://www.wikidata.org/entity/Q34098314

description

2005 nî lūn-bûn

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2005 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2005 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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name

polyglutamine aggregation nucl ...... rable protein folding reaction

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polyglutamine aggregation nucl ...... rable protein folding reaction

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polyglutamine aggregation nucl ...... rable protein folding reaction

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polyglutamine aggregation nucl ...... rable protein folding reaction

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polyglutamine aggregation nucl ...... rable protein folding reaction

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Proceedings of the National Academy of Sciences of the United States of America

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polyglutamine aggregation nucl ...... rable protein folding reaction

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P2093

Anusri M Bhattacharyya

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Ashwani K Thakur

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Ronald Wetzel

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P2860

Molecular origin of polyglutamine aggregation in neurodegenerative diseases.

Huntingtin aggregation and toxicity in Huntington's disease

Use of gene knockouts in cultured cells to study apoptosis.

A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.

Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.

Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells.

Absence of behavioral abnormalities and neurodegeneration in vivo despite widespread neuronal huntingtin inclusions.

A linear lattice model for polyglutamine in CAG-expansion diseases

Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.

Mutational analysis of the structural organization of polyglutamine aggregates.

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16230628

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protein folding

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1266079

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