Mechanism of thioflavin T binding to amyloid fibrils.

By R. Khurana, Chris W. Coleman, C. Ionescu-Zanetti, S. Carter, V. Krishna, R. Grover, R. Roy, Shashi Singh. Journal of Structural Biology, 2005

794 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/46830f1ecb30f82cd299fd7052e4afada31996ac

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Citations in the corpus

• Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils (2010, background): “[41] noted that most experiments employing ThT are performed at or above the critical micelle concentration (CMC) of the dye, estimated at ∼4 μM in water.”
• Extrinsic Fluorescent Dyes as Tools for Protein Characterization (2008, background): “increase in presence of amyloid fibrils to the formation of Thioflavin T micelles binding to the grooves of the twisted protofibrils or fibrils as analyzed by atomic force microscopy (69).”
• Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation (2017, neutral): “[29] show that ThT has a critical micelle concentration of approximately 4 μM, in good agreement with our observations that ThT becomes”