Vinzenz Unger Professor

Research Summary: 

Using electron microscopy, digital image reconstruction, biophysics and a diversity of biochemical approaches, we study the structure and function of membrane proteins and membrane-associated scaffolds. Currently our efforts focus on the mechanisms by which cells acquire and distribute copper ions, and how cells change the shape of their membranes

Selected Publications:

Cellular distribution of copper to superoxide dismutase involves scaffolding by membranes. Pope CR, De Feo CJ, Unger VM. Proc Natl Acad Sci U S A. 2013 Dec 2. [Epub ahead of print]

Atox1 Contains Positive Residues that Mediate Membrane Association and Aid Subsequent Copper Loading.Flores AG, Unger VM. J Membr Biol. 2013 Dec;246(12):903-13.

Autoinhibition of Endophilin in Solution via Interdomain Interactions. Vásquez FX, Unger VM, and Voth GA. Biophysical Journal. 2013 January 22;104(2):396-403.

Structural basis of membrane bending by the N-BAR protein endophilin. Mim C, Cui H, Gawronski-Salerno JA, Frost A, Lyman E, Voth GA, Unger VM. Cell. 2012 Mar 30;149(1):137-45.

Three-dimensional structure of the human copper transporter hCTR1.De Feo CJ, Aller SG, Siluvai GS, Blackburn NJ, Unger VM. Proc Natl Acad Sci U S A. 2009 Mar 17;106(11):4237-42