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Ontario Tech acknowledges the lands and people of the Mississaugas of Scugog Island First Nation.

We are thankful to be welcome on these lands in friendship. The lands we are situated on are covered by the Williams Treaties and are the traditional territory of the Mississaugas, a branch of the greater Anishinaabeg Nation, including Algonquin, Ojibway, Odawa and Pottawatomi. These lands remain home to many Indigenous nations and peoples.

We acknowledge this land out of respect for the Indigenous nations who have cared for Turtle Island, also called North America, from before the arrival of settler peoples until this day. Most importantly, we acknowledge that the history of these lands has been tainted by poor treatment and a lack of friendship with the First Nations who call them home.

This history is something we are all affected by because we are all treaty people in Canada. We all have a shared history to reflect on, and each of us is affected by this history in different ways. Our past defines our present, but if we move forward as friends and allies, then it does not have to define our future.

Learn more about Indigenous Education and Cultural Services

March 12, 2012

Speaker: Dr. Steven Johnson, University of Washington, Seattle, Washington

Title: Medicinal chemistry strategies for modulating protein (mis)folding pathways associated with human diseases

Abstract: Proteins need to be properly folded in order to perform their functions. As such, cells have evolved biochemical pathways to help ensure that proteins either fold properly or are targeted for degradation. Nonetheless, there are instances where these systems fail, allowing misfolded proteins to accumulate, often with pathological consequences. Transthyretin, for example, can be prone to amyloidogenesis, the process of protein misfolding and subsequent aggregation, which is implicated in several human diseases. One therapeutic strategy for such maladies is to directly target the folded protein with a small molecule native state stabilizer, thereby inhibiting amyloidogenesis. Another, potentially far reaching strategy to address protein (mis)folding pathways, is to target molecular chaperones, cellular machines specialized in helping proteins fold properly. I will present my research on both avenues highlighting the application of structure activity relationships, medicinal chemistry, and high throughput screening for the discovery and development of novel small molecule probes and therapeutics for modulating protein (mis)folding pathways.