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SUMMARY:A little more than kin and less than kind: The origins of neurodeg
 enerative disease. - Prajwal Ciryam
DTSTART:20110224T190000Z
DTEND:20110224T210000Z
UID:TALK29956@talks.cam.ac.uk
CONTACT:Echo Ouyang
DESCRIPTION:A fundamental requirement for life is that proteins remain sol
 uble in the cell. When protein homeostasis fails to maintain solubility\, 
 toxic protein aggregates can form\, leading to the dozens of protein confo
 rmational disorders\, which include Alzheimer’s\, Parkinson’s\, and ot
 her diseases. These diseases\, especially Alzheimer's\, have an incredible
  impact on health care in the developed world. Four million people in the 
 United States currently suffer from Azheimer's disease\, a number expected
  to double by 2050. Because these diseases represent a dysfunction in a ce
 ntral process in biology—proteins folding into the correct shape—under
 standing them provides us insight into the foundations of living systems. 
 Similarly\, thinking about the basic principles that underlie life may yie
 ld important information about how the family of conformational disorders 
 occur. Relying on one of these principles—that proteins must remain diss
 olved to work—has led to our first generation predictor of the the most 
 dangerous proteins\, those most susceptible to disease. Using our danger p
 arameter\, ∂\, which relies on the gene expression of a given protein an
 d the protein's predicted tendency to form aggregates\, we are able to ide
 ntify groups of proteins in which the Alzheimer's disease\, Parkinson's di
 sease\, and Huntington's disease pathways are overrepresented. This provid
 es a first step at explaining the basis for human misfolding disease on a 
 proteomic level.
LOCATION:M3 Second Court\, St John's College (Dr. Sue Colwell's Office)
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