thioflavin

These substitutions also result in a dramatic enhancement of both thioflavin-T positive fibril formation and binding to preformed Aβ fibrils while maintaining its plaque-binding ability in AD transgenic mice.

Elites TV 2010

These substitutions also result in a dramatic enhancement of both thioflavin-T positive fibril formation and binding to preformed Aβ fibrils while maintaining its plaque-binding ability in AD transgenic mice.

Elites TV 2010

When MstnPP-containing Escherichia coli inclusion bodies are refolded and purified, a proportion of MstnPP spontaneously misfolds into amyloid-like aggregates as characterised by electron microscopy and binding of the amyloid-specific dye thioflavin T.

PLoS ONE Alerts: New Articles Carlene S. Starck et al. 2010

These substitutions also result in a dramatic enhancement of both thioflavin-T positive fibril formation and binding to preformed Aβ fibrils while maintaining its plaque-binding ability in AD transgenic mice.

Elites TV 2010

When MstnPP-containing Escherichia coli inclusion bodies are refolded and purified, a proportion of MstnPP spontaneously misfolds into amyloid-like aggregates as characterised by electron microscopy and binding of the amyloid-specific dye thioflavin T.

PLoS ONE Alerts: New Articles Carlene S. Starck et al. 2010

We now show that a human MstnPP misfolded species shares the morphological characteristics of amyloid protofibrils and the ability to bind the amyloid-specific dye thioflavin T.

PLoS ONE Alerts: New Articles Carlene S. Starck et al. 2010

A defining characteristic of amyloid fibrils and protofibrils is their ability to bind the fluorescent dye thioflavin T (ThT) [63] - [65]

PLoS ONE Alerts: New Articles Carlene S. Starck et al. 2010

When MstnPP-containing Escherichia coli inclusion bodies are refolded and purified, a proportion of MstnPP spontaneously misfolds into amyloid-like aggregates as characterised by electron microscopy and binding of the amyloid-specific dye thioflavin T.

Elites TV PLoS ONE 2010

E. coli inclusion bodies, a population of MstnPP spontaneously misfolds into amyloid protofibril-like aggregates that can be visualised using electron microscopy and bind the amyloid-specific dye thioflavin T.

PLoS ONE Alerts: New Articles Carlene S. Starck et al. 2010

Fibril formation was achieved using a continuous in vitro fibrillization assay, with amyloid fibril formation monitored by the dye, thioflavin T (ThT).

PLoS ONE Alerts: New Articles Diane Latawiec et al. 2010