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SUMMARY:Special LMNN Seminar - Optical superresolution microscopy of molec
 ular mechanisms of disease
DTSTART:20190205T100000
DTEND:20190205T110000
DTSTAMP:20260509T211715Z
UID:bb079f192ab358c24a8cfaafff4d737dcd33aa41c84acc830b155c95
CATEGORIES:Conferences - Seminars
DESCRIPTION:Clemens F. Kaminski\, Department of Chemical Engineering and B
 iotechnology\,  University of Cambridge\, UK. url: http://laser.ceb.cam.
 ac.uk\nThe self-assembly of proteins into ordered macromolecular units is 
 fundamental to a variety of diseases. For example\, in Alzheimer’s Disea
 se (AD) and Parkinson’s Disease (PD)\, proteins that are usually harmles
 s are found to adopt aberrant shapes\, a process referred to as protein mi
 sfolding.  In the misfolded state the proteins are prone to aggregate int
 o highly ordered\, toxic structures\, called protein amyloids and these ma
 ke up the insoluble deposits found in the brains of patients suffering fro
 m these devastating disorders. A key requirement to gain insights into mol
 ecular mechanisms of disease and to progress in the search for therapeutic
  intervention is a capability to image the protein assembly process in sit
 u i.e. in cellular models of disease. \nIn this talk I will give an overv
 iew of research techniques that allow us to gain insights into the aggrega
 tion of neurotoxic proteins in vitro (1\, 2)\, in cells (3) and in live mo
 del organisms (4). In particular\, we wish to understand how these and sim
 ilar proteins nucleate to form toxic structures and to correlate such info
 rmation with phenotypes of disease (3). I will show how direct stochastic 
 optical reconstruction microscopy\, dSTORM\, and developments of high spee
 d structured illumination microscopy\, SIM\, are capable of tracking amylo
 idogenesis in vitro\, and in vivo\, and how we can correlate the appearanc
 e of certain aggregate species with toxic phenotypes of relevance to neuro
 degeneration (6-13).\n(1) Pinotsi et al\, Nano Letters (2013)\n(2) Kaminsk
 i Schierle\, et al\, JACS (2011)\n(3) Esbjörner\, et al\, ChemBiol (2014)
 \n(4) Kaminski Schierle\, et al\, ChemPhysChem (2011)\n(5) Stroehl and Kam
 inski\, Optica (2016)\n(6) Fantham and Kaminski\, Nature Phot. (2017)\n(7)
  Michel\, et al\, JBC (2014)\n(8) Pinotsi\, et al\, PNAS (2016)\n(9) Murak
 ami\, et al\, Neuron (2015)\n(10) Wong\, et al\, Neuron (2017)\n(11) Fusco
 \, et al\, Nature Comms. (2016)\n(12) Qamear\, et al\, Cell (2018)\n(13) L
 autenschlaeger et al.\, Nature Comms. (2018)
LOCATION:SV 1717 https://plan.epfl.ch/?room==SV%201717
STATUS:CONFIRMED
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