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SUMMARY:Protein misfolding and amyloid fibril formation: role in aging\, n
 eurodegeneration\, non-neuropathic diseases and cancer
DTSTART:20260325T130000Z
DTEND:20260325T140000Z
DTSTAMP:20260506T231900Z
UID:indico-event-50788@agenda.infn.it
DESCRIPTION:Speakers: Fabrizio Chiti (Unifi)\n\nAbstract\nAn increasing nu
 mber of human diseases\, that are typically associated with aging\, often 
 originate from misfolding and aggregation of well-defined proteins. These 
 include neurodegenerative conditions\, such as Alzheimer\, Parkinson and p
 rion diseases\, frontotemporal dementia\, amyotrophic lateral sclerosis\, 
 as well as non-neuropathic diseases\, such as systemic amyloidosis\, type 
 II diabetes and many others. It is also increasingly recognized that prote
 in aggregation is a key process in some types of cancer\, such as those as
 sociated with p53 mutations. In this Seminar\, the main pathways leading 
 a protein to misfold\, oligomerize aberrantly and then form large and inso
 luble aggregates will be shown\, along with the mechanisms of protection u
 sed by cells to prevent these deleterious events. The main mechanisms thro
 ugh which aging and mutations promote protein aggregation will be discusse
 d. It will then show the recent progress in the field brought by solid-sta
 te nuclear magnetic resonance and cryogenic electron microscopy to elucida
 te the structure of the main protein aggregates that accumulate in patholo
 gy\, namely amyloid fibrils\, and how our community has progressed substan
 tially to the elucidation of their structure and polymorphism\, with a res
 olution down to <3.0 Å. I will finally show the main contributions of ou
 r lab to elucidate the effect of mutations on amyloid fibril formation\, t
 he regions of the sequence determining fibril structure and their associat
 ed polymorphism. We will also show how aberrant protein oligomers forming 
 during aggregation or released from mature fibrils cause cell dysfunction 
 and prospective therapeutic strategies to neutralise them.\n \n\nhttps://
 agenda.infn.it/event/50788/
LOCATION:aula magna
URL:https://agenda.infn.it/event/50788/
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