Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation - Wikidata - wikimedia - TriplyDB

Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

http://www.wikidata.org/entity/Q27670453

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NMR Meets Tau: Insights into Its Function and Pathology Self-propagation of pathogenic protein aggregates in neurodegenerative diseases The role of tau in neurodegenerative diseases and its potential as a therapeutic target Ubiquitous amyloids Aβ42-oligomer Interacting Peptide (AIP) neutralizes toxic amyloid-β42 species and protects synaptic structure and function.Computational design of a symmetric homodimer using -strand assembly Implications of aromatic-aromatic interactions: From protein structures to peptide models Inter-species cross-seeding: stability and assembly of rat-human amylin aggregates The stability of cylindrin β-barrel amyloid oligomer models-a molecular dynamics study.Protein modeling: what happened to the "protein structure gap"?Protein folding and de novo protein design for biotechnological applications Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen.Forcefield_NCAA: ab initio charge parameters to aid in the discovery and design of therapeutic proteins and peptides with unnatural amino acids and their application to complement inhibitors of the compstatin family.Learning To Fold Proteins Using Energy Landscape Theory.Amyloid: a multifaceted player in human health and disease.Human prion protein sequence elements impede cross-species chronic wasting disease transmission.The C-terminal amyloidogenic peptide contributes to self-assembly of Avibirnavirus viral protease Hydration water mobility is enhanced around tau amyloid fibers.The Surprising Role of Amyloid Fibrils in HIV Infection A resorcinarene for inhibition of Aβ fibrillation.Effect of semen and seminal amyloid on vaginal transmission of simian immunodeficiency virus Combined computational design of a zinc-binding site and a protein-protein interaction: one open zinc coordination site was not a robust hotspot for de novo ubiquitin binding Specific calpain inhibition by calpastatin prevents tauopathy and neurodegeneration and restores normal lifespan in tau P301L mice Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau.Strategies to control the binding mode of de novo designed protein interactions.Nature versus design: the conformational propensities of D-amino acids and the importance of side chain chirality.Curcumin Binding to Beta Amyloid: A Computational Study.An index for characterization of natural and non-natural amino acids for peptidomimetics De novo design and experimental characterization of ultrashort self-associating peptides Semen enhances HIV infectivity and impairs the antiviral efficacy of microbicides.Discovery of modulators of HIV-1 infection from the human peptidome.Aging and amyloid beta-induced oxidative DNA damage and mitochondrial dysfunction in Alzheimer's disease: implications for early intervention and therapeutics.Toxicity of eosinophil MBP is repressed by intracellular crystallization and promoted by extracellular aggregation.Binding cavities and druggability of intrinsically disordered proteins.Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation.Structure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity.Structure-Based Peptide Design to Modulate Amyloid Beta Aggregation and Reduce Cytotoxicity Naturally occurring fragments from two distinct regions of the prostatic acid phosphatase form amyloidogenic enhancers of HIV infection.

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Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

http://www.wikidata.org/entity/Q27670453

description

2011 nî lūn-bûn

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2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2011 թվականի հունիսին 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年论文

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name

Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

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Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

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Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

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type

label

Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

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Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

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Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

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prefLabel

Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

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Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

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Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

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Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

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Anni Zhao

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Howard W Chang

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Jan Münch

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Jason T Stevens

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John Karanicolas

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Lin Jiang

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Onofrio Zirafi

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Stuart A Sievers

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P2860

Design of a Novel Globular Protein Fold with Atomic-Level Accuracy

Semen-derived amyloid fibrils drastically enhance HIV infection

The 3D profile method for identifying fibril-forming segments of proteins

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

Atomic structures of amyloid cross-beta spines reveal varied steric zippers

Molecular mechanisms for protein-encoded inheritance

Computational Design of Proteins Targeting the Conserved Stem Region of Influenza Hemagglutinin

Coot: model-building tools for molecular graphics

Use of T7 RNA polymerase to direct expression of cloned genes

Phasercrystallographic software

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96-100

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scholarly article

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991797

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10.1038/NATURE10154

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7354

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475

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David Eisenberg

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2011-06-15T00:00:00Z

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1052435615

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21677644

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4073670

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