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DTSTART:20230312T100000
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DTSTART;TZID=America/Los_Angeles:20230518T120000
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DTSTAMP:20260614T015605
CREATED:20230320T172456Z
LAST-MODIFIED:20230320T172456Z
UID:28648-1684411200-1684414800@www.chemistry.ucla.edu
SUMMARY:Chem 218 Student Exit Seminar: Natalie Kashanchi
DESCRIPTION:
URL:https://www.chemistry.ucla.edu/events/chem-218-student-exit-seminar-natalie-kashanchi/
LOCATION:Mani L. Bhaumik Centennial Collaboratory\, 607 Charles E. Young Dr.\, East\, Los Angeles\, CA\, 90095\, United States
CATEGORIES:Chem 218 Student Exit Seminar
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DTSTART;TZID=America/Los_Angeles:20230518T160000
DTEND;TZID=America/Los_Angeles:20230518T170000
DTSTAMP:20260614T015605
CREATED:20230309T213700Z
LAST-MODIFIED:20230309T214156Z
UID:28540-1684425600-1684429200@www.chemistry.ucla.edu
SUMMARY:Houk-Jung Organic Colloquium 247: Joshua Kritzer
DESCRIPTION:Kritzer Flyer \nDesigning Stapled Peptides that Control Autophagy \nAbstract: Autophagy is a cellular recycling process important for health and disease\, and a major focus for new types of targeted protein degradation. The Kritzer Lab has used structure-based design to develop stapled peptides that bind the critical autophagy proteins LC3B and GABARAP with nanomolar affinities. Small changes in staple structure produced ligands with very different binding modes\, leading to differences in paralog selectivity. The stapled peptides exhibited considerable cytosolic penetration and resistance to biological degradation. They also reduced autophagic flux in cultured ovarian cancer cells and sensitized ovarian cancer cells to cisplatin. These small\, potent stapled peptides represent promising autophagy-modulating compounds that can be developed as novel cancer therapeutics and novel mediators of targeted protein degradation.
URL:https://www.chemistry.ucla.edu/events/houk-jung-organic-colloquium-247-joshua-kritzer/
LOCATION:Mani L. Bhaumik Centennial Collaboratory\, 607 Charles E. Young Dr.\, East\, Los Angeles\, CA\, 90095\, United States
CATEGORIES:Organic Colloquium
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