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DTSTART:20070311T020000
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DTSTAMP:20251117T080145
DTSTART;TZID=America/Detroit:20260113T160000
DTEND;TZID=America/Detroit:20260113T170000
SUMMARY:Lecture / Discussion:CPOD Winter 2026 Seminar Series: \"Uncovering defect mechanisms and apical polarity cues in neural tube organoids\"
DESCRIPTION:Andrew Tidball\, Ph.D.\nResearch Assistant Professor\nNeurology\nUniversity of Michigan
UID:141937-21889654@events.umich.edu
URL:https://events.umich.edu/event/141937
CLASS:PUBLIC
STATUS:CONFIRMED
CATEGORIES:Free,Undergraduate Students,seminar,Science,Research,Rackham,Public Health,Postdoctoral Research Fellows,Medicine,Life Science,Lecture,Interdisciplinary,In Person,human genetics,Graduate Students,Graduate School,Engineering,Education,Ecology,Biosciences,biomedical engineering,biomedical,Biology,Biointerfaces,Basic Science,AEM Featured
LOCATION:Taubman Biomedical Science Research Building - ABC Seminar Rooms
CONTACT:
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BEGIN:VEVENT
DTSTAMP:20251211T102025
DTSTART;TZID=America/Detroit:20260113T160000
DTEND;TZID=America/Detroit:20260113T171500
SUMMARY:Workshop / Seminar:Exploring the structural biology of enteroviral genome replication
DESCRIPTION:The Enterovirus genus comprises RNA viruses associated with various illnesses\, including the common cold\, poliomyelitis\, acute flaccid paralysis\, and myocarditis. These viruses have conserved cloverleaf-shaped RNA secondary structures at the extreme 5′ end of their genomes\, which are crucial for assembling viral and host proteins\, such as 3CD and PCBP2\, into functional ribonucleoprotein (RNP) complexes required for genome replication. However\, the high-resolution structures and mechanisms of these cloverleaf RNAs have largely remained unknown. Recently\, we determined the crystal structures of five cloverleaf RNAs from different enteroviral species\, revealing a highly conserved H-type four-way junction fold that positions the 3CD and PCBP2 binding sites far apart. The conserved features observed in these structures\, including a long-range A•C•U base triple\, enabled us to predict structural models for other enteroviruses via homology modeling\, yielding models similar to the experimental structures. Our structure-guided binding analyses\, using recombinantly purified full-length human PCBP2 and viral 3C proteins\, along with the crystal structures of the cloverleaf-3C complexes\, offered further insights into how these viruses assemble RNP complexes for their genome replication within host cells. Moreover\, we demonstrated that antisense oligonucleotides could block high-affinity PCBP2-binding sites\, highlighting the potential to develop therapeutics targeting this replication platform for enteroviral infections. The notable structural conservation among enteroviral cloverleafs observed in our studies underscores opportunities to develop universal therapeutics that target this viral RNP platform across multiple enterovirus infections.
UID:138424-21882929@events.umich.edu
URL:https://events.umich.edu/event/138424
CLASS:PUBLIC
STATUS:CONFIRMED
CATEGORIES:Chemical Biology,Science,Chemistry
LOCATION:Chemistry Dow Lab - 1640
CONTACT:
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