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Daniel Segal - Research 'Conformational diseases' are diseases caused by misfolding of a protein, often as a result of a missense mutation that does not necessarily disrupt the active site of the protein. As a result, the protein may lose its function, and often the misfolded monomers self-assemble to form cytotoxic aggregates. We study the structural causes of such protein misfolding in conditions ranging from neurodegenerative diseases to certain cancers. In various cases such misfolding can be reversible under experimental conditions. Thus, drugs that will cause refolding of the misfolded protein may restore its function and prevent its harmful aggregation. Research methods: In vitro and bacterial assays of protein folding and aggregation (in collaboration with Prof. Ehud Gazit, Dept. Biotechnology), cytotoxcisity assays in cell culture, genetics and molecular biology of transgenics (Drosophila, mice), immunohistochemistry, behavioral and cognitive assays (mouse work - in collaboration with Dr. Dan Frenkel, Dept. Neurobiology). Main projects in the lab include: Develop and screen in vivo novel small molecules as amyloid-beta and tau inhibitors in Alzheimer’s disease. Develop and screen natural plant compounds as amyloid-beta and tau inhibitors in Alzheimer’s disease. Develop and screen in vivo novel small molecules as alpha-synuclein inhibitors in Parkinson’s disease Develop and screen in vivo novel small molecules as TDP-43 inhibitors in ALS. Examine the mechanism of spreading of TDP-43 in ALS. Examine the role of protein glycosylation in the aging and neurodegenerative brain. Study misfolding of the tumor suppressor proteins p53 and VHL and develop small molecules for restoring their folding and function.