Andisheh Abedini

发表

Role of aromatic interactions in amyloid formation by peptides derived from human Amylin.

D. Raleigh, Miles Driscoll, Daniel P Raleigh, 2004, Biochemistry.

The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity.

Fanling Meng, D. Raleigh, C. Verchere, 2010, Biochemistry.

A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor.

Fanling Meng, D. Raleigh, Daniel P Raleigh, 2007, Journal of the American Chemical Society.

A role for helical intermediates in amyloid formation by natively unfolded polypeptides?

D. Raleigh, Daniel P Raleigh, Andisheh Abedini, 2009, Physical biology.

The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors.

Fanling Meng, D. Raleigh, P. Cao, 2010, Biochemistry.

Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology.

D. Raleigh, P. Cao, Daniel P Raleigh, 2013, Current opinion in structural biology.

Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20.

Ann Marie Schmidt, Olesya Levsh, D. Raleigh, 2012, Journal of molecular biology.

Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity

Peter Marek, D. Raleigh, P. Marek, 2012, FEBS letters.

Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation.

Fanling Meng, D. Raleigh, Daniel P Raleigh, 2010, Journal of the American Chemical Society.