Techniques to study amyloid fibril formation in vitro.

By M. R. Nilsson. Methods, 2004

944 citations recorded by the source corpus.

Subfields: Food Science, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/2c13bbe4c9f2544f9cb41b75b009cd3c24055ad4

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Food Science

1. G. Núñez
2. Christopher M. Dobson
3. Fabrizio Chiti

In Molecular Biology

1. Fabrizio Chiti
2. Christopher M. Dobson
3. G. Núñez
4. L. Franchi
5. Luke A. O'Neill
6. S. Kahn
7. S. Masters
8. C. A. Dinarello

In Physiology

1. Christopher M. Dobson
2. Fabrizio Chiti
3. G. Núñez
4. L. Franchi
5. Luke A. O'Neill
6. Michele Vendruscolo
7. Tuomas P. J. Knowles
8. C. A. Dinarello

Citations in the corpus

• Activation of the Nlrp3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes (2010, methodology): “This was diluted to 10 μM in RPMI medium, and thioflavin T was added to a concentration of 20 μM, after which fluorescence was measured according to a published protoco”
• Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “The existence of such structure is characteristically monitored by the binding of dyes, such as thioflavin-T (ThT), Congo red (CR), or their derivatives, which are thought to form ordered arrays along the lengths of the fibrils that give rise to specific spectral responses (77, 78).”