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SUMMARY:Proteome homeostasis and protein aggregation in ALS - Dr. Justin Y
 erbury\, University of Wollongong
DTSTART:20151007T093000Z
DTEND:20151007T103000Z
UID:TALK61396@talks.cam.ac.uk
CONTACT:Jerome Charmet
DESCRIPTION:Motor Neurone Disease (MND) is a fatal\, incurable progressive
  neuromuscular paralysis. While many cases of MND are sporadic\, several g
 enes are implicated in familial forms of the disease. One of the major gen
 etic causes of MND is mutation in the superoxide dismutase 1 (SOD1) gene. 
 There are over 150 mutations spanning the entire protein sequence suggesti
 ng dysfunction arises from improper folding of the protein\, which is evid
 enced by the appearance of intracellular aggregates in motor neurons and o
 ther cell types at later stages of disease.  The disease is not caused by 
 loss of normal protein function and instead is a gain of a new inherent to
 xic attribute\, further indicative of SOD1 misfolding conferring new stres
 ses to cell functions. We propose that the proteostasis imbalance created 
 by expression of mutant SOD1 leads to a reduced operation of an extensive 
 network of housekeeping functions that are dependent on proteostasis machi
 nery such as ubiquitin proteasome system\, which we predict to cause a dec
 line in cell health and heighten sensitivity to further stresses that trig
 gers neurodegeneration.
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theater
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