Publication | Closed Access
Thioflavin Derivatives as Markers for Amyloid‐β Fibrils: Insights into Structural Features Important for High‐Affinity Binding
69
Citations
19
References
2007
Year
Structural VariationsProteinlipid InteractionAmyloid‐β FibrilsProtein AssemblyMolecular BiologyPeptide ScienceAnalytical UltracentrifugationProtein FoldingAffinity VariationsProtein MisfoldingProtein ChemistryProtein FunctionBiochemistryHigh‐affinity BindingMolecular ModelingStructural Features ImportantStructural BiologyStructural RequirementsNatural SciencesMedicine
How do we go together? Structural variations have been used to obtain information regarding the interaction of thioflavin-derived markers and amyloid-β fibril targets. Affinity variations of up to three orders of magnitude were observed, revealing some structural requirements for these markers at the molecular level.
| Year | Citations | |
|---|---|---|
Page 1
Page 1