The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils. - Wikidata - awgldk - TriplyDB

The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.

The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.

http://www.wikidata.org/entity/Q33838789

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Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residues Atomic structure and hierarchical assembly of a cross- amyloid fibril Structure and Topology of the Huntingtin 1–17 Membrane Anchor by a Combined Solution and Solid-State NMR Approach Mechanistic insight into the relationship between N-terminal acetylation of α-synuclein and fibril formation rates by NMR and fluorescence Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity Scalable production in human cells and biochemical characterization of full-length normal and mutant huntingtin Glutamine and Asparagine Side Chain Hyperconjugation-Induced Structurally Sensitive Vibrations.Super-resolution fluorescence of huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregates Elucidation of the Aggregation Pathways of Helix-Turn-Helix Peptides: Stabilization at the Turn Region Is Critical for Fibril Formation.Free-Energy Landscape of the Amino-Terminal Fragment of Huntingtin in Aqueous Solution Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansion Investigating the structural impact of the glutamine repeat in huntingtin assembly.Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.Molecular interaction between the chaperone Hsc70 and the N-terminal flank of huntingtin exon 1 modulates aggregation Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions.Kinetically competing huntingtin aggregation pathways control amyloid polymorphism and properties 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.Fibrillar structure and charge determine the interaction of polyglutamine protein aggregates with the cell surface.Structural features and domain organization of huntingtin fibrils.CAMELOT: A machine learning approach for coarse-grained simulations of aggregation of block-copolymeric protein sequences.α-Synuclein and huntingtin exon 1 amyloid fibrils bind laterally to the cellular membrane.Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core Slow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments.Solid-State Nuclear Magnetic Resonance on the Static and Dynamic Domains of Huntingtin Exon-1 Fibrils.Efficient resonance assignment of proteins in MAS NMR by simultaneous intra- and inter-residue 3D correlation spectroscopy.Levels of supramolecular chirality of polyglutamine aggregates revealed by vibrational circular dichroism.Acetylation within the First 17 Residues of Huntingtin Exon 1 Alters Aggregation and Lipid Binding.Nanoscale studies link amyloid maturity with polyglutamine diseases onset.Identification and Structural Characterization of the N-terminal Amyloid Core of Orb2 isoform A.Investigating Mutations to Reduce Huntingtin Aggregation by Increasing Htt-N-Terminal Stability and Weakening Interactions with PolyQ Domain.SUMO-2 and PIAS1 modulate insoluble mutant huntingtin protein accumulation.Chaperones in Polyglutamine Aggregation: Beyond the Q-Stretch.Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.A serendipitous survey of prediction algorithms for amyloidogenicity.Advances in huntington disease drug discovery: novel approaches to model disease phenotypes.Polyglutamine Aggregation in Huntington Disease: Does Structure Determine Toxicity?

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P2860

The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.

http://www.wikidata.org/entity/Q33838789

description

2011 nî lūn-bûn

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2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.

@ast

The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.

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type

label

The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.

@ast

The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.

@en

prefLabel

The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.

@ast

The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.

@en

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P1433

Journal of the American Chemical Society

P1476

The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.

@en

P2093

Cody L Hoop

http://www.w3.org/2001/XMLSchema#string

Murali Jayaraman

http://www.w3.org/2001/XMLSchema#string

Patrick C A van der Wel

http://www.w3.org/2001/XMLSchema#string

Ravindra Kodali

http://www.w3.org/2001/XMLSchema#string

Ronald Wetzel

http://www.w3.org/2001/XMLSchema#string

V N Sivanandam

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P2860

Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity

Structure of the cross-beta spine of amyloid-like fibrils

The predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregation

Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy

Secondary Structure of Huntingtin Amino-Terminal Region

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

The CCPN data model for NMR spectroscopy: development of a software pipeline

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Protein misfolding, functional amyloid, and human disease

The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans

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4558-4566

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10.1021/JA110715F

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21381744

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3109494

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