Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation. - Test2 - elhamkhani - TriplyDB

Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation.

Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation.

http://www.wikidata.org/entity/Q34388290

about

Relating sequence encoded information to form and function of intrinsically disordered proteins Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation An Intein-based Strategy for the Production of Tag-free Huntingtin Exon 1 Proteins Enables New Insights into the Polyglutamine Dependence of Httex1 Aggregation and Fibril Formation Dynamics of protein aggregation and oligomer formation governed by secondary nucleation.Data for ion and seed dependent fibril assembly of a spidroin core domain.Free-Energy Landscape of the Amino-Terminal Fragment of Huntingtin in Aqueous Solution TR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes.Solubility and aggregation of Gly(5) in water.Assemblages: functional units formed by cellular phase separation A coarse-grained model for polyglutamine aggregation modulated by amphipathic flanking sequences Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome.Polyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopy The emerging role of the first 17 amino acids of huntingtin in Huntington's disease Huntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues.Sequence heuristics to encode phase behaviour in intrinsically disordered protein polymers.Conformational dynamics and self-association of intrinsically disordered Huntingtin exon 1 in cells.CAMELOT: A machine learning approach for coarse-grained simulations of aggregation of block-copolymeric protein sequences.Solid-State Nuclear Magnetic Resonance on the Static and Dynamic Domains of Huntingtin Exon-1 Fibrils.The Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules.Acetylation within the First 17 Residues of Huntingtin Exon 1 Alters Aggregation and Lipid Binding.Nanoscale studies link amyloid maturity with polyglutamine diseases onset.An Intrabody Drug (rAAV6-INT41) Reduces the Binding of N-Terminal Huntingtin Fragment(s) to DNA to Basal Levels in PC12 Cells and Delays Cognitive Loss in the R6/2 Animal Model Investigating Mutations to Reduce Huntingtin Aggregation by Increasing Htt-N-Terminal Stability and Weakening Interactions with PolyQ Domain.Chaperones in Polyglutamine Aggregation: Beyond the Q-Stretch.Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases.Ubiquitin-dependent proteolysis in yeast cells expressing neurotoxic proteins.An Amyloidogenic Sequence at the N-Terminus of the Androgen Receptor Impacts Polyglutamine Aggregation.Proteins Containing Expanded Polyglutamine Tracts and Neurodegenerative Disease.Aggregation behavior of chemically synthesized, full-length huntingtin exon1."Wet" Versus "Dry" Folding of Polyproline.Altered Co-Translational Processing Plays a Role in Huntington's Pathogenesis-A Hypothesis.Staying Together: Protein Molecules in Mesoscopic Clusters.Protein Polymerization into Fibrils from the Viewpoint of Nucleation Theory.Control of the structural landscape and neuronal proteotoxicity of mutant Huntingtin by domains flanking the polyQ tract.Frozen in beta.Amyloid oligomers and protofibrils, but not filaments, self-replicate from native lysozyme.Aggregation landscapes of Huntingtin exon 1 protein fragments and the critical repeat length for the onset of Huntington's disease.Nucleation: The Birth of a New Protein Phase.Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6.

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Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation.

http://www.wikidata.org/entity/Q34388290

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2013 nî lūn-bûn

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2013 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2013 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2013年の論文

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年學術文章

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Unmasking the roles of N- and ...... of polyglutamine aggregation.

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Unmasking the roles of N- and ...... of polyglutamine aggregation.

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Unmasking the roles of N- and ...... of polyglutamine aggregation.

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Unmasking the roles of N- and ...... of polyglutamine aggregation.

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Unmasking the roles of N- and ...... of polyglutamine aggregation.

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PNAS.1320626110

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

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Unmasking the roles of N- and ...... of polyglutamine aggregation.

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Carl Frieden

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Kanchan Garai

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Kiersten M Ruff

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Rohit V Pappu

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Scott L Crick

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P2860

Measurement of protein using bicinchoninic acid

PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone.

Huntington's disease

Solubilization and disaggregation of polyglutamine peptides

Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions

Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease.

Nucleated conformational conversion and the replication of conformational information by a prion determinant.

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

Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides

Flanking sequences profoundly alter polyglutamine toxicity in yeast.

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3864320

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