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DTSTART:20110801T120000
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URL:https://murmitoyen.com/events/vanille/udem/detail/58456
LOCATION:Université de Montréal - Pavillon Roger-Gaudry\, 2900\, chemin d
 e la Tour\, Montréal\, QC\, Canada\, H3T 1J6
SUMMARY:Structural folds of amyloid and prion fibrils
DESCRIPTION:À l'invitation du Dr Serguei Chteinberg\, le Département de b
 iochimie de l'Université de Montréal reçoit le Dr Andrey Kajava\, le lu
 ndi 1er août prochain.Vous trouverez l’affiche de cette conférence :ww
 w.biochimie.umontreal.ca/doc/Conferences/1aout11.pdfDr Andrey KajavaCentre
  de Recherches de Biochimie Macromoléculaire (CRBM)Université Montpellie
 r 1 et 2Résumé de la conférence (en anglais)Structural details of the a
 myloid and prion fibrils are keys to developing new therapeutics for neuro
 degenerative disease such as Alzheimer's disease\, Huntington's disease\, 
 Parkinson's disease\, human prion diseases.Over the past decade\, substant
 ial progress has been made inunderstanding the structural arrangements in 
 amyloid fibrils.Although these specimens remain refractory to the classica
 l approach of X-ray crystallography\, progress has stemmed largely from th
 e application of new experimental techniques such as solid state NMR\, sca
 nning transmission electron microscopy mass measurements and electron para
 magnetic resonance spectroscopy of spin-labelled derivatives. Based on the
 se and other experimental data\, several new structural models for amyloid
  and prion fibrils have been formulated including A-beta amyloid\, tau\, a
 lpha-synuclein\, human amylin\, and the fungal prions\, Ure2p\, Sup35 prio
 ns and HET-s. The number of structural data is now large enough to support
  a systematic analysis. The analysis is making it possible to categorize t
 hese structures\, yielding an enhanced understanding of their 'pathogenic 
 fold' determinants\, and is shedding light on how they form and function. 
 The status of this generalization\, and its implications\, will be central
  themes of this talk.
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