Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism.

By L. Nielsen, R. Khurana, Alisa C. Coats, S. Frokjaer, J. Brange, S. Vyas, Vladimir N Uversky, A. Fink. Biochemistry, 2001

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Conformational constraints for amyloid fibrillation: the importance of being unfolded. (2004, background): “The fibrillation of insulin is accelerated in the presence of denaturants such as urea, whereas stabilizers, such as trimethylamine N-oxide (TMAO) and sucrose, decrease the fibrillation rate [25].”
Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature. (2009, methodology): “Fink's empirical equation has been used to analyze numerous data sets thus allowing for comparisons to be made between related data sets [34,35,37,142]; an example is shown in Fig.”
Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation (2017, background): “[20] reported that ThT did not affect the kinetics of insulin fibril formation at 60°C, but Manno et al.”
Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation (2003, background): “Examples include recombinant factor VIII SQ (41), low-molecular-weight urokinase (42), relaxin (43), rhGCSF (17,20), deoxyhemoglobin (44), interlukin-1 (45), ribonuclease A (46), and insulin ( 47 ).”