A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity.
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Overnutrition Determines LPS Regulation of Mycotoxin Induced Neurotoxicity in Neurodegenerative DiseasesDisrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal modelsMolecular Tweezers Targeting Transthyretin AmyloidosisSite-specific inhibitory mechanism for amyloid β42 aggregation by catechol-type flavonoids targeting the Lys residues.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Safety and pharmacological characterization of the molecular tweezer CLR01 - a broad-spectrum inhibitor of amyloid proteins' toxicity.Polyphenols as therapeutic molecules in Alzheimer's disease through modulating amyloid pathways.Comparison of three amyloid assembly inhibitors: the sugar scyllo-inositol, the polyphenol epigallocatechin gallate, and the molecular tweezer CLR01Elucidating the Aβ42 Anti-Aggregation Mechanism of Action of Tramiprosate in Alzheimer's Disease: Integrating Molecular Analytical Methods, Pharmacokinetic and Clinical DataProtection of primary neurons and mouse brain from Alzheimer's pathology by molecular tweezers.Amino acid substitutions [K16A] and [K28A] distinctly affect amyloid β-protein oligomerization.Perspectives on Inhibiting β-Amyloid Aggregation through Structure-Based Drug Design.The flavonoid derivative 2-(4' Benzyloxyphenyl)-3-hydroxy-chromen-4-one protects against Aβ42-induced neurodegeneration in transgenic Drosophila: insights from in silico and in vivo studies.Characteristics of C-terminal, β-amyloid peptide binding fragment of neuroprotective protease inhibitor, cystatin C.Inhibition of Mutant αB Crystallin-Induced Protein Aggregation by a Molecular Tweezer.Lipid insertion domain unfolding regulates protein orientational transition behavior in a lipid bilayer.A Toxic Conformer of Aβ42 with a Turn at 22-23 is a Novel Therapeutic Target for Alzheimer's DiseaseAtomic and dynamic insights into the beneficial effect of the 1,4-naphthoquinon-2-yl-L-tryptophan inhibitor on Alzheimer's Aβ1-42 dimer in terms of aggregation and toxicity.Identification of key regions and residues controlling Aβ folding and assembly.Molecular tweezers for lysine and arginine - powerful inhibitors of pathologic protein aggregationEffect of the Tottori familial disease mutation (D7N) on the monomers and dimers of Aβ40 and Aβ42.Multicomponent, fragment-based synthesis of polyphenol-containing peptidomimetics and their inhibiting activity on beta-amyloid oligomerization.Characterizing Structural Stability of Amyloid Motif Fibrils Mediated by Water Molecules.Bioactive polyphenol interactions with β amyloid: a comparison of binding modelling, effects on fibril and aggregate formation and neuroprotective capacity.Dual effects of familial Alzheimer's disease mutations (D7H, D7N, and H6R) on amyloid β peptide: correlation dynamics and zinc binding.Colorimetric and fluorescence probe for the detection of nano-molar lysine in aqueous medium.Discovery and Identification of an Endogenous Metabolite of Tramiprosate and Its Prodrug ALZ-801 that Inhibits Beta Amyloid Oligomer Formation in the Human Brain
P2860
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P2860
A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity.
@en
type
label
A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity.
@en
prefLabel
A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity.
@en
P2860
P356
P1476
A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity
@en
P2093
Dahabada H J Lopes
P2860
P304
P356
10.1021/CN3000247
P577
2012-03-16T00:00:00Z