Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42. - Wikidata - awgldk - TriplyDB

Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.

Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.

http://www.wikidata.org/entity/Q36996040

about

BRI2 (ITM2b) inhibits Abeta deposition in vivo Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils Aβ42-oligomer Interacting Peptide (AIP) neutralizes toxic amyloid-β42 species and protects synaptic structure and function.Molecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-Assemblies Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation Molecular mechanism of Thioflavin-T binding to amyloid fibrils Structure and dynamics of parallel beta-sheets, hydrophobic core, and loops in Alzheimer's A beta fibrils Computational design of new Peptide inhibitors for amyloid Beta (aβ) aggregation in Alzheimer's disease: application of a novel methodology Models of membrane-bound Alzheimer's Abeta peptide assemblies Interprotofilament interactions between Alzheimer's Abeta1-42 peptides in amyloid fibrils revealed by cryoEM A new structural model of Alzheimer's Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modeling Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavities Inhibition of Abeta42 aggregation using peptides selected from combinatorial libraries.Molecular structures of quiescently grown and brain-derived polymorphic fibrils of the Alzheimer amyloid abeta9-40 peptide: a comparison to agitated fibrils.Beta-amyloid precursor protein mutants respond to gamma-secretase modulators Polymorphic structures of Alzheimer's β-amyloid globulomers.What is the role of amyloid precursor protein dimerization?Mapping the specific cytoprotective interaction of humanin with the pro-apoptotic protein bid.Peptides for therapy and diagnosis of Alzheimer's disease.Polymorphic C-terminal beta-sheet interactions determine the formation of fibril or amyloid beta-derived diffusible ligand-like globulomer for the Alzheimer Abeta42 dodecamer.Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process.Lowering of amyloid beta peptide production with a small molecule inhibitor of amyloid-β precursor protein dimerization Comparative analysis of the Shadoo gene between cattle and buffalo reveals significant differences.Critique of the use of fluorescence-based reporters in Escherichia coli as a screening tool for the identification of peptide inhibitors of Aβ42 aggregation.Hydralazine modifies Aβ fibril formation and prevents modification by lipids in vitro.The unique Alzheimer's β-amyloid triangular fibril has a cavity along the fibril axis under physiological conditions.Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species.Conformational stability of fibrillar amyloid-beta oligomers via protofilament pair formation - a systematic computational study Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Polymorphic triple beta-sheet structures contribute to amide hydrogen/deuterium (H/D) exchange protection in the Alzheimer amyloid beta42 peptide Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulations Amyloid polymorphism: structural basis and neurobiological relevance.Structural differences of amyloid-β fibrils revealed by antibodies from phage display Self-Assembly of Aβ40, Aβ42 and Aβ43 Peptides in Aqueous Mixtures of Fluorinated Alcohols.Effects of peptides derived from terminal modifications of the aβ central hydrophobic core on aβ fibrillization.Cross-linking of cell surface amyloid precursor protein leads to increased β-amyloid peptide production in hippocampal neurons: implications for Alzheimer's disease.Role of the familial Dutch mutation E22Q in the folding and aggregation of the 15-28 fragment of the Alzheimer amyloid-beta protein.Physiological temperature has a crucial role in amyloid β in the absence and presence of hydrophobic and hydrophilic nanoparticles.Novel therapeutic strategies for the treatment of protein-misfolding diseases.Glycines from the APP GXXXG/GXXXA Transmembrane Motifs Promote Formation of Pathogenic Aβ Oligomers in Cells

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Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.

http://www.wikidata.org/entity/Q36996040

description

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Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.

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Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.

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Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.

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Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.

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Huilin Li

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

James I Elliott

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Jean-Noel Octave

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Mahiuddin Ahmed

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Saburo Aimoto

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Steven O Smith

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Takeshi Sato

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Wei Liu

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P2860

Efficient reversal of Alzheimer's disease fibril formation and elimination of neurotoxicity by a small molecule

High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy

The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

In vitro studies of amyloid beta-protein fibril assembly and toxicity provide clues to the aetiology of Flemish variant (Ala692-->Gly) Alzheimer's disease

Site-specific identification of non-beta-strand conformations in Alzheimer's beta-amyloid fibrils by solid-state NMR

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils

Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils

3D structure of Alzheimer's amyloid-beta(1-42) fibrils

Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

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5503-5516

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10.1021/BI052485F

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17

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45

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Stefan N Constantinescu

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2006-05-01T00:00:00Z

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7145496

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16634632

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2593882

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