Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid. - Wikidata - wikimedia - TriplyDB

Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid.

Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid.

http://www.wikidata.org/entity/Q44219224

about

Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer's disease Metals and amyloid-beta in Alzheimer's disease Oxidized cholesterol as the driving force behind the development of Alzheimer's disease The turn formation at positions 22 and 23 in the 42-mer amyloid beta peptide: the emerging role in the pathogenesis of Alzheimer's disease.Effect of metals on kinetic pathways of amyloid-β aggregation The effect of Aβ on IAPP aggregation in the presence of an isolated β-cell membrane.Amyloid ion channels: a common structural link for protein-misfolding disease Alzheimer disease beta-amyloid activity mimics cholesterol oxidase.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Surface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide Copper and iron in Alzheimer's disease: a systematic review and its dietary implications.Membrane cholesterol modulates {beta}-amyloid-dependent tau cleavage by inducing changes in the membrane content and localization of N-methyl-D-aspartic acid receptors Cu(2+) affects amyloid-β (1-42) aggregation by increasing peptide-peptide binding forces.Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species.Copper, beta-amyloid, and Alzheimer's disease: tapping a sensitive connection Current concepts in therapeutic strategies targeting cognitive decline and disease modification in Alzheimer's disease.Promotion of oxidative lipid membrane damage by amyloid beta proteins Effects of amyloid beta-peptides on the lysis tension of lipid bilayer vesicles containing oxysterols.Amyloid-beta aggregation.Amyloid beta ion channel: 3D structure and relevance to amyloid channel paradigm.Links between copper and cholesterol in Alzheimer's disease.The modulation of metal bio-availability as a therapeutic strategy for the treatment of Alzheimer's disease.The structure of the amyloid-beta peptide high-affinity copper II binding site in Alzheimer disease.Clinical field-strength MRI of amyloid plaques induced by low-level cholesterol feeding in rabbits Therapeutics for Alzheimer's disease based on the metal hypothesis Liberation of GPI-anchored prion from phospholipids accelerates amyloidogenic conversion.Pharmacotherapeutic targets in Alzheimer's disease Membrane-targeted strategies for modulating APP and Abeta-mediated toxicity.Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide.Oxidative stress and cell membranes in the pathogenesis of Alzheimer's disease.The role of metallobiology and amyloid-β peptides in Alzheimer's disease.Formation of the 42-mer Amyloid β Radical and the Therapeutic Role of Superoxide Dismutase in Alzheimer's Disease.Cellular membrane fluidity in amyloid precursor protein processing.CHOLESTEROL AND NEURONAL SUSCEPTIBILITY TO BETA-AMYLOID TOXICITY.Effect of trehalose on amyloid beta (29-40)-membrane interaction.Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes.Glucose directs amyloid-beta into membrane-active oligomers.Amyloid-β(1-42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity.Redox reactions of copper complexes formed with different beta-amyloid peptides and their neuropathological [correction of neuropathalogical] relevance.Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.

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P2860

Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid.

http://www.wikidata.org/entity/Q44219224

description

2002 nî lūn-bûn

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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2002年學術文章

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name

Metal ions, pH, and cholestero ...... a peptide with membrane lipid.

@en

Metal ions, pH, and cholestero ...... a peptide with membrane lipid.

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type

label

Metal ions, pH, and cholestero ...... a peptide with membrane lipid.

@en

Metal ions, pH, and cholestero ...... a peptide with membrane lipid.

@nl

prefLabel

Metal ions, pH, and cholestero ...... a peptide with membrane lipid.

@en

Metal ions, pH, and cholestero ...... a peptide with membrane lipid.

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P1433

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P1433

Journal of Biological Chemistry

P1476

Metal ions, pH, and cholestero ...... a peptide with membrane lipid.

@en

P2093

Danielle G Smith

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

Fedá E Ali

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

Kevin J Barnham

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P2860

Inhibition of Bax channel-forming activity by Bcl-2

Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice

Amyloid plaque core protein in Alzheimer disease and Down syndrome

Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?

Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1

Apolipoprotein E and cholesterol affect neuronal calcium signalling: the possible relationship to beta-amyloid neurotoxicity

Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

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

Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease.

Theoretical models of the ion channel structure of amyloid beta-protein.

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2977-2982

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scholarly article

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10.1074/JBC.M205455200

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P407

P433

5

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P478

278

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Colin L. Masters

Cyril C. Curtain

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2002-11-14T00:00:00Z

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12435742

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P921

Alzheimer's disease