Scripps Research Joint Appointments

Department of Molecular and Experimental Medicine
Department of Chemical Physiology
Faculty, Kellogg School of Science and Technology

Research Focus

Protein misfolding and human disease

Conversion of genetic information into functional protein products requires the proper folding of polypeptide chains in the crowded intracellular environment. Disruption of these folding pathways through exposure to either environmental or genetic factors is associated with numerous human diseases – collectively referred to as protein misfolding diseases. Using proteomic, biophysical and cell biological approaches, work in the Wiseman lab is directed towards understanding the physical, chemical and biological factors that dictate intracellular protein folding as it relates to human disease. Currently, we have three ongoing projects focused on protein folding in vivo: 1) development of novel biosensors that report on protein folding in the complex intracellular environment; 2) characterization of mitochondrial folding efficiency in the context of neurodegenerative disease; and 3) elucidation of the impact of intracellular signaling pathways on protein folding and trafficking in the early secretory pathway.

Education

B.S., Chemistry, University of Virginia, 2001
Ph.D., Chemistry, The Scripps Research Institute, 2005

Selected References

Wiseman, RL; Powers, ET; Buxbaum, JN; Kelly, JW; Balch, WE (2007) An Adaptable Standard for Protein Export from the Endoplasmic Reticulum; Cell, 131, 809-821.

Sekijima, Y; Wiseman, RL; Matteson, J; Hammarstrom, P; Miller, SR; Balch, WE; Kelly, JW (2005) The Biological and Chemical Basis for Tissue-Selective Amyloid Disease, Cell, 121, 73-85.

Hammarstrom, P; Wiseman, RL; Powers, ET; Kelly, JW (2003) Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics, Science, 299, 713-716.