Aβ(39-42) modulates Aβ oligomerization but not fibril formation
about
Modulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanismsAmyloid β-Protein Assembly: The Effect of Molecular Tweezers CLR01 and CLR03Novel insights into protein misfolding diseases revealed by ion mobility-mass spectrometry.A resorcinarene for inhibition of Aβ fibrillation.Modulation of Amyloid β-Protein (Aβ) Assembly by Homologous C-Terminal Fragments as a Strategy for Inhibiting Aβ Toxicity.Analysis of the Amyloidogenic Potential of Pufferfish (Takifugu rubripes) Islet Amyloid Polypeptide Highlights the Limitations of Thioflavin-T Assays and the Difficulties in Defining AmyloidogenicityRational design of a structural framework with potential use to develop chemical reagents that target and modulate multiple facets of Alzheimer's disease.Ion mobility spectrometry: A personal view of its development at UCSBDisordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Defining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions.Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Di-tyrosine cross-link decreases the collisional cross-section of aβ peptide dimers and trimers in the gas phase: an ion mobility study.Effects of secondary metabolite extract from Phomopsis occulta on β-amyloid aggregationSDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MSHuntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues.Amyloid β-Protein Assembly: Differential Effects of the Protective A2T Mutation and Recessive A2V Familial Alzheimer's Disease Mutation.Opposing Effects of Cucurbit[7]uril and 1,2,3,4,6-Penta-O-galloyl-β-d-glucopyranose on Amyloid β25-35 Assembly.Mechanism of C-Terminal Fragments of Amyloid β-Protein as Aβ Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?Amyloid-β-neuropeptide interactions assessed by ion mobility-mass spectrometry.Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.Pulsed hydrogen-deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation.Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Assembling the pieces of macromolecular complexes: Hybrid structural biology approaches.Antibody-Based Drugs and Approaches Against Amyloid-β Species for Alzheimer's Disease Immunotherapy.Role of Species-Specific Primary Structure Differences in Aβ42 Assembly and NeurotoxicityConformational dynamics of α-synuclein: insights from mass spectrometry.Identification of the primary peptide contaminant that inhibits fibrillation and toxicity in synthetic amyloid-β42.Identification of key regions and residues controlling Aβ folding and assembly.Design of a Molecular Hybrid of Dual Peptide Inhibitors Coupled on AuNPs for Enhanced Inhibition of Amyloid β-Protein Aggregation and Cytotoxicity.Ion Mobility-Mass Spectrometry Reveals a Dipeptide That Acts as a Molecular Chaperone for Amyloid β.Conformational features of the Aβ42 peptide monomer and its interaction with the surrounding solvent.
P2860
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P2860
Aβ(39-42) modulates Aβ oligomerization but not fibril formation
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Aβ(39-42) modulates Aβ oligomerization but not fibril formation
@ast
Aβ(39-42) modulates Aβ oligomerization but not fibril formation
@en
type
label
Aβ(39-42) modulates Aβ oligomerization but not fibril formation
@ast
Aβ(39-42) modulates Aβ oligomerization but not fibril formation
@en
prefLabel
Aβ(39-42) modulates Aβ oligomerization but not fibril formation
@ast
Aβ(39-42) modulates Aβ oligomerization but not fibril formation
@en
P2093
P2860
P356
P1433
P1476
Aβ(39-42) modulates Aβ oligomerization but not fibril formation
@en
P2093
Huiyuan Li
Joan-Emma Shea
Michael T Bowers
P2860
P304
P356
10.1021/BI201520B
P407
P577
2011-12-23T00:00:00Z