Judith Frydman

Graduate & Fellowship Program Affiliations

• Biophysics
• Cancer Biology
• Cell Biology

Web Site Links

• Lab Website

Research Interests

The long term goal of our research is to understand how proteins fold in living cells. My lab uses a multidisciplinary approach to address fundamental questions about molecular chaperones, protein folding and degradation. In addition to basic mechanistic principles, we aim to define how impairment of cellular folding and quality control are linked to disease, including cancer and neurodegenerative diseases and examine whether reengineering chaperone networks can provide therapeutic strategies.

Publications

• The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation. Tam S, Spiess C, Auyeung W, Joachimiak L, Chen B, Poirier MA, Frydman J. Nat Struct Mol Biol. 2009
• Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Yam AY, Xia Y, Lin HT, Burlingame A, Gerstein M, Frydman J. Nat Struct Mol Biol. 2008; 15 (12): 1255-62
• Misfolded proteins partition between two distinct quality control compartments. Kaganovich D, Kopito R, Frydman J. Nature. 2008; 454 (7208): 1088-95
• Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT. Booth CR, Meyer AS, Cong Y, Topf M, Sali A, Ludtke SJ, Chiu W, Frydman J. Nat Struct Mol Biol. 2008; 15 (7): 746-53
• Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. McClellan AJ, Xia Y, Deutschbauer AM, Davis RW, Gerstein M, Frydman J. Cell. 2007; 131 (1): 121-35