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Andrew Miranker

 

Molecular Biophysics & Biochemistry; Pharmacology & Molecular Medicine; Computational Biology & Bioinformatics

Associate Professor of Molecular Biophysics & Biochemistry

Education

B.S. Carnegie Mellon University 1986
Ph.D. Harvard University 1992

Research Interests

Research in our laboratory is focused on conformational changes in proteins which give rise to a special class of protein complex known as amyloid fibrils. Depending on the protein involved, fibril formation gives rise or contributes to the pathogenesis of more than 20 clinical conditions. This includes Alzheimer’s, Parkinson’s, Mad Cow disease, type II diabetes, to name a few. This folding problem is particularly fascinating as proteins which are seemingly unrelated in primary sequence and in their native 3 dimensional structure form aggregates which share common structural and cytotoxic features. Projects currently underway in the laboratory include the islet amyloid polypeptide system which forms cytotoxic fibrils in type II diabetics, and beta-2 microglobulin which forms deposits on the connective tissues of renal failure patients. We study protein folding, fiber formation and cytotoxicity in these systems. Our approaches range from the cellular to the physical chemical with interests ranging from rational drug design to kinetic pathway analysis to molecular structure determination.

Links

• Miranker Homepage

Recent Publications

• Hebda, JA and Miranker, AD (2009) The Interplay of Catalysis and Toxicity by Amyloid Intermediates on Lipid Bilayers: Insights from Type II Diabetes, Annual Reviews in Biophysics 38:125–152.
• Calabrese, MF and Miranker, AD (2009) Metal binding sheds light on mechanisms of amyloid assembly, Prion 3:1-4.

Contact

E-mail
andrew.miranker@yale.edu