Pages that link to "Q34546859"

The following pages link to The stability of monomeric intermediates controls amyloid formation: Abeta25-35 and its N27Q mutant (Q34546859):

Displaying 23 items.

• Structure and dynamics of parallel beta-sheets, hydrophobic core, and loops in Alzheimer's A beta fibrils (Q28395520) (← links)
• Induced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibition (Q30157126) (← links)
• Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates. (Q30352016) (← links)
• Structural determination of Abeta25-35 micelles by molecular dynamics simulations (Q33999447) (← links)
• Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape (Q34059772) (← links)
• Enzyme dynamics point to stepwise conformational selection in catalysis (Q34136545) (← links)
• Dynamics of metastable β-hairpin structures in the folding nucleus of amyloid β-protein. (Q36088283) (← links)
• Role of β-hairpin formation in aggregation: the self-assembly of the amyloid-β(25-35) peptide. (Q36150710) (← links)
• Hydration effects on the HET-s prion and amyloid-beta fibrillous aggregates, studied with three-dimensional molecular theory of solvation (Q36957378) (← links)
• Polymorphism of Alzheimer's Abeta17-42 (p3) oligomers: the importance of the turn location and its conformation (Q37303941) (← links)
• Tauroursodeoxycholic acid prevents E22Q Alzheimer's Abeta toxicity in human cerebral endothelial cells. (Q37384925) (← links)
• Human Neuronal Calcium Sensor-1 Protein Avoids Histidine Residues To Decrease pH Sensitivity (Q46439263) (← links)
• Lipid-induced conformational transition of the amyloid core fragment Abeta(28-35) and its A30G and A30I mutants (Q46636201) (← links)
• Modulating protein amyloid aggregation with nanomaterials. (Q47259639) (← links)
• Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology (Q48175839) (← links)
• Hierarchy and the mechanism of fibril formation in ADan peptides. (Q48400882) (← links)
• Conformational features of the Aβ42 peptide monomer and its interaction with the surrounding solvent (Q48446186) (← links)
• Dynamics of the conformational transitions during the dimerization of an intrinsically disordered peptide: a case study on the human islet amyloid polypeptide fragment. (Q51112827) (← links)
• Structural and Material Properties of Amyloid Aβ40/42 Fibrils (Q51345356) (← links)
• Single molecule study of initial structural features on the amyloidosis process (Q51411240) (← links)
• Global fitting without a global model: regularization based on the continuity of the evolution of parameter distributions (Q51890052) (← links)
• Disordered versus Fibril-like Amyloid β (25−35) Dimers in Water: Structure and Thermodynamics (Q85235252) (← links)
• Location and conformation of amyloid β(25-35) peptide and its sequence-shuffled peptides within membranes: implications for aggregation and toxicity in PC12 cells (Q87676281) (← links)