Technion Biology Faculty

Technion Biology Faculty

Biology provides the scientific basis for today's most vital areas, including biotechnology, medicine, biomedical and genetic engineering, and bioinformatics. With a finger on the pulse of different disciplines, The Technion Biology Faculty constantly tailor programs and courses to face the challenges of modern biology.

Detailed information can be found here.

Research Groups at the Faculty.


Technion Biology Faculty

Biology provides the scientific basis for today's most vital areas, including biotechnology, medicine, biomedical and genetic engineering, and bioinformatics. With a finger on the pulse of different disciplines, The Technion Biology Faculty constantly tailor programs and courses to face the challenges of modern biology.

Detailed information can be found here.

Research Groups at the Faculty.


Coordinator Prof. Michael Glickman

Professor Glickman hopes to gain insight into the cellular system that degrades proteins in a controlled manner. This system ensures that superfluous or defective proteins are marked with a molecular tag, the protein ubiquitin, and are disposed of in the cellular shredding machine, the proteasome. The ubiquitin-proteasome system is found in all eukaryotic cells and is – as its name indicates – ubiquitous. It is one of the organism’s most complex cellular systems and protects the body against serious diseases. For example, defective proteins that elude this system trigger serious diseases such as Alzheimer’s, Parkinson’s, Huntington’s, cystic fibrosis or diabetes. Our lab is interested in Proteasome structure and function, Mechanistic aspects of protein degradation by the ubiquitin-proteasome system and Charting the cellular ubiquitin-linkage profile using Mass spectrometry and proteomics. Towards this goal we are also analyzing the importance of proteolysis in homeostasis and regulation of the proteome and the specific recognition of ubiquitin and ubiquitin-like proteins. A separate yet related project looks at the biology of mitochondria membrane fusion and fission. More specifically, how does ubiquitination and proteasome-dependent-degradation participate in mitochondria function and dynamics.