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SUMMARY:New insights into protein misfolding in Alzheimer's and Parkinson'
 s diseases using in vivo systems - Professor Dennis Selkoe\, Harvard Medic
 al School\, Center for Neurologic Diseases\, Brigham & Women’s Hospital
DTSTART:20171213T110000Z
DTEND:20171213T120000Z
UID:TALK94075@talks.cam.ac.uk
CONTACT:Patrick Flagmeier
DESCRIPTION:Misfolding and progressive aggregation of specific proteins ma
 y be etiologic in several human neurodegenerative diseases. Many studies h
 ave examined the process in vitro\, resulting in valuable insights\, but t
 o what extent findings in relatively pure in vitro systems reflect the sit
 uation in the patient’s brain is unclear. Here\, we have focused on livi
 ng cells\, mice\, and human brain tissue to learn more about the character
 istics and bioactivities of various endogenous forms of amyloid beta-prote
 in (Abeta) and alpha-synculein (alphaSyn). We will describe recent work on
  the effects of natural oligomers of Abeta isolated from AD cortex on iPSC
 -derived human neurons\, including protection by certain antibodies. We wi
 ll then provide further evidence that alphaSyn occurs normally as helical 
 tetramers in intact cells\, but these rapidly disassemble upon cell lysis\
 , yielding the unfolded monomers that have been the focus of in vitro stud
 ies. Mice expressing tetramer-abrogating alphaSyn mutations develop nigros
 triatal and cortical lesions\, decreased tyrosine hydroxylase\, and a prog
 ressive motor phenotype that includes tremor and gait defects which respon
 d in part to L-DOPA. These new findings have implications for the initiati
 on of PD and other human synucleinopathies and their potential prevention 
 by compounds which stabilize the physiological tetramers. 
LOCATION:Department of Chemistry\, Cambridge\, Pfizer lecture theatre
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