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SUMMARY:Special IMX Seminar - Cryo-EM structures of amyloid fibrils from A
 lzheimer's disease and systemic amyloidosis
DTSTART:20200127T170000
DTEND:20200127T183000
DTSTAMP:20260429T032125Z
UID:c164156b32d916423d9e490c523661144cad268294351b95e84a4b01
CATEGORIES:Conferences - Seminars
DESCRIPTION:Marcus Fändrich\, Institute of Protein Biochemistry\, Ulm Uni
 versity\, Ulm\, GERMANY\nAmyloid fibrils are associated with a range of d
 ebilitating diseases in humans and animals but the exact molecular structu
 res of these pathogenic agents have recently remained elusive. To determin
 e the structure of amyloid fibrils from patient tissue and to learn about 
 the mechanism of fibril formation. We obtained cryo-EM structure of amyloi
 d fibrils from three different forms of systemic amyloidosis: AA (Liberta 
 F\, Loerch S\, Rennegarbe M et al.\, Nature Comm. 10\, 1104\, 2019)\, AL (
 Radamaker et al.\, Nature Comm. 10\, 1103\, 2019) and ATTR (Schmidt M et a
 l. Nature Comm. 10\, 5008\, 2019). In addition\, we obtained the structure
  of Aβ amyloid fibrils from Alzheimer’s disease/cerebral amyloid angiop
 athy (Kollmer M et al. Nature Comm. 10\, 4760\, 2019). Our data reveal the
  present of right-hand twisted cross-β sheets and provide\, in specific c
 ases\, evidence about the order of events during fibril formation\, such a
 s whether proteolysis precedes fibril formation or vice versa. Amyloid fib
 rils from patient tissue are structurally different from known amyloid-lik
 e fibrils formed in vitro. Our findings illuminate the structural repertoi
 re of protein aggregates\, provide insights into the mechanism of fibril f
 ormation in vivo\, and inform about potential therapeutic strategies.
LOCATION:AI 1153 https://plan.epfl.ch/?room==AI%201153
STATUS:CONFIRMED
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