Amyloid ion channels: a common structural link for protein-misfolding disease - Wikidata - awgldk - TriplyDB

Amyloid ion channels: a common structural link for protein-misfolding disease

Amyloid ion channels: a common structural link for protein-misfolding disease

http://www.wikidata.org/entity/Q33906626

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Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectin Molecular determinants of α-synuclein mutants' oligomerization and membrane interactions Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity Versatile Structures of α-Synuclein Overview of Alzheimer's Disease and Some Therapeutic Approaches Targeting Aβ by Using Several Synthetic and Herbal Compounds Insights into Mechanisms of Chronic Neurodegeneration Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Biophysical characterization of α-synuclein and its controversial structure The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPP Structural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studies Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives Dynamics of the formation of a hydrogel by a pathogenic amyloid peptide: islet amyloid polypeptide.Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR Spectroscopy Factors That Drive Peptide Assembly from Native to Amyloid Structures: Experimental and Theoretical Analysis of [Leu-5]-Enkephalin Mutants Role of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet Amyloidosis Structure and dynamics of parallel beta-sheets, hydrophobic core, and loops in Alzheimer's A beta fibrils Direct observation of single amyloid-β(1-40) oligomers on live cells: binding and growth at physiological concentrations Inter-species cross-seeding: stability and assembly of rat-human amylin aggregates Potential role of atomic force microscopy in systems biology Amyloid oligomer neurotoxicity, calcium dysregulation, and lipid rafts Synaptotoxicity of Alzheimer beta amyloid can be explained by its membrane perforating property Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide Familial Alzheimer's disease Osaka mutant (ΔE22) β-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment.All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.Effects of surface interactions on peptide aggregate morphology.Models of membrane-bound Alzheimer's Abeta peptide assemblies Beta-barrel models of soluble amyloid beta oligomers and annular protofibrils.Conversion of a porin-like peptide channel into a gramicidin-like channel by glycine to D-alanine substitutions.Specific chaperones and regulatory domains in control of amyloid formation.Biophysics of α-synuclein membrane interactions.Aggregation of Aß(25-35) on DOPC and DOPC/DHA bilayers: an atomic force microscopy study Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Aggregation and fibril morphology of the Arctic mutation of Alzheimer's Aβ peptide by CD, TEM, STEM and in situ AFM Role of endocytic inhibitory drugs on internalization of amyloidogenic light chains by cardiac fibroblasts.Neuroprotective natural antibodies to assemblies of amyloidogenic peptides decrease with normal aging and advancing Alzheimer's disease.Interaction of daptomycin with lipid bilayers: a lipid extracting effect Tyrosine Hydroxylase Binding to Phospholipid Membranes Prompts Its Amyloid Aggregation and Compromises Bilayer Integrity.

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Amyloid ion channels: a common structural link for protein-misfolding disease

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Amyloid ion channels: a common structural link for protein-misfolding disease

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Amyloid ion channels: a common structural link for protein-misfolding disease

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

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Amyloid ion channels: a common structural link for protein-misfolding disease

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Arjan Quist

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Blas Frangione

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Bruce Kagan

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Douglas Ng

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Hai Lin

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Ivo Doudevski

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Jorge Ghiso

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Ratnesh Lal

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Rushana Azimova

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P2860

Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo

Fresh and nonfibrillar amyloid beta protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for AbetaP-channel-mediated cellular toxicity

Protein folding and misfolding

Folding proteins in fatal ways

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Amyloid beta protein (1-40) forms calcium-permeable, Zn2+-sensitive channel in reconstituted lipid vesicles.

Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology.

Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: evidence for AbetaP channel-mediated cellular toxicity.

Amyloid beta protein-(1-42) forms calcium-permeable, Zn2+-sensitive channel.

Properties of cytotoxic peptide-formed ion channels.

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10427-10432

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102

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