How are aberrant proteins selected for elimination by the ubiquitin-proteasome system? – Biologisk Institut - Københavns Universitet

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How are aberrant proteins selected for elimination by the ubiquitin-proteasome system?

Speaker: Dr. Tommer Ravid, Principal Investigator, The Hebrew University of Jerusalem

Host: Professor Rasmus Hartmann-Petersen, Biomolecular Sciences, UCPH

Abstract
Research at the Ravid laboratory covers the disciplines of biochemistry, cell biology and genetics, taking advantage of the many research benefits offered by the Baker's yeast Saccharomyces cerevisiae as a model organism. Our area of interest is protein quality control, a universal protective cellular mechanism for ensuring that damaged or aberrant proteins are recognized and repaired or eliminated. Specifically, we are interested in understanding the role of the ubiquitin-proteasome degradation system and cellular chaperones in protein quality control, and the outcome of their deterioration during aging. Our research is driven by findings that link defective ubiquitin conjugation or proteasome function and the concomitant accumulation of cellular protein aggregates, to many human neurodegenerative diseases.