IMP, Vienna | Austria
EMBO 2010 | MemC 14–17
The misfolding and aggregation of protein molecules is a severe danger for cell viability. All living organisms therefore evolved a sophisticated network of molecular chaperones and proteases to reduce the amount of aberrant proteins, a process that is regulated by multiple stress response pathways. My group performs a structure-function analysis of several of these factors in order to better understand how cells deal with stress situations.
Keywords: Macromolecular machines / protein quality control / chaperone networks / regulatory proteolysis / stress response
Subject area(s): Proteins & Biochemistry | Signal Transduction | Structural Biology & Biophysics