Pages that link to "Q47110086"

The following pages link to The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation. (Q47110086):

Displaying 38 items.

• Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils (Q27714742) (← links)
• Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance (Q28066391) (← links)
• Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM. (Q30316195) (← links)
• N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42 (Q33626314) (← links)
• SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MS (Q36138981) (← links)
• High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR. (Q36217985) (← links)
• Monomeric Aβ(1-40) and Aβ(1-42) Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil (Q36569893) (← links)
• In silico investigation on the inhibition of Aβ42 aggregation by Aβ40 peptide by potential of mean force study (Q38917669) (← links)
• Dynamics of heteromolecular filament formation (Q39204296) (← links)
• Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines (Q41540882) (← links)
• Monomer-dependent secondary nucleation in amyloid formation (Q41579457) (← links)
• Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms (Q41954285) (← links)
• Pyroglutamate-modified Aβ(3-42) affects aggregation kinetics of Aβ(1-42) by accelerating primary and secondary pathways (Q42363417) (← links)
• Cross-seeding between Aβ40 and Aβ42 in Alzheimer's disease (Q44369500) (← links)
• Comparing the Aggregation Free Energy Landscapes of Amyloid Beta(1-42) and Amyloid Beta(1-40). (Q46277930) (← links)
• Effect of metal chelators on the aggregation of beta-amyloid peptides in the presence of copper and iron. (Q46405967) (← links)
• Crystallographic insights into the self-assembly of KLVFF amyloid-beta peptides (Q47311832) (← links)
• Imaging Aβ(1-42) fibril elongation reveals strongly polarised growth and growth incompetent states (Q47449222) (← links)
• Biophysical Aspects of Alzheimer's Disease: Implications for Pharmaceutical Sciences : Theme: Drug Discovery, Development and Delivery in Alzheimer's Disease Guest Editor: Davide Brambilla (Q47722422) (← links)
• Theory of amyloid fibril nucleation from folded proteins (Q47764012) (← links)
• Stereochemistry and amyloid inhibition: Asymmetric triplex metallohelices enantioselectively bind to Aβ peptide. (Q48161785) (← links)
• N-Terminally Truncated Amyloid-β(11-40/42) Cofibrillizes with its Full-Length Counterpart: Implications for Alzheimer's Disease. (Q48284125) (← links)
• E22G Pathogenic Mutation of β-Amyloid (Aβ) Enhances Misfolding of Aβ40 by Unexpected Prion-like Cross Talk between Aβ42 and Aβ40. (Q50100231) (← links)
• Depletion of amyloid-β peptides from solution by sequestration within fibril-seeded hydrogels (Q50125047) (← links)
• Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide. (Q52340980) (← links)
• Amyloid β-peptides 1-40 and 1-42 form oligomers with mixed β-sheets. (Q54959267) (← links)
• Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface. (Q55233780) (← links)
• Directing curli polymerization with DNA origami nucleators (Q64114173) (← links)
• Modular genetic design of multi-domain functional amyloids: insights into self-assembly and functional properties (Q64228589) (← links)
• Molecular insights into the surface-catalyzed secondary nucleation of amyloid-β40 (Aβ40) by the peptide fragment Aβ16–22. (Q64882394) (← links)
• Metallotexaphyrins as MRI-Active Catalytic Antioxidants for Neurodegenerative Disease: A Study on Alzheimer's Disease (Q90579247) (← links)
• Self-Assembly and Neurotoxicity of β-Amyloid (21-40) Peptide Fragment: The Regulatory Role of GxxxG Motifs (Q91424644) (← links)
• Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide (Q91874866) (← links)
• Functional Amyloids and their Possible Influence on Alzheimer Disease (Q92070015) (← links)
• α-Helical Motif as Inhibitors of Toxic Amyloid-β Oligomer Generation via Highly Specific Recognition of Amyloid Surface (Q93131408) (← links)
• Should the Treatment of Amyloidosis Be Personified? Molecular Mechanism of Amyloid Formation by Aβ Peptide and Its Fragments (Q93332924) (← links)
• Biophysical studies of protein misfolding and aggregation in in vivo models of Alzheimer's and Parkinson's diseases (Q96129239) (← links)
• A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease (Q99564822) (← links)