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SUMMARY:Observing Oligomerization Kinetics of p53 Via Fluorescence Correlat
 ion Spectroscopy
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20181001T000000
UID:2026-04-24-16-27-14@natsci.colostate.edu
DTSTAMP:20260424T162714
Description:Literature Seminar Abstract\n\nTumor growth is regulated by the
  tumor suppressing protein p53. Nearly half of all cancers contain a mutat
 ion in tp53\, the gene that codes for p53.[i] Therefore\, understanding ho
 w p53 functions is a key component in understanding cancer. Previous studi
 es have shown that in healthy cells\, p53 tetramerizes and binds to DNA to
  regulate abnormal cell growth.[ii] In cancerous cells\, p53 function can 
 be inhibited by overexpression of proteins regulating the tetramerization 
 (s100 family proteins) and p53 degradation (mdm2).1.[iii] Understanding th
 e kinetics of p53 in cancer cells could lead to new treatment methods. Pre
 sented here is the analysis of the kinetics of p53 in healthy cells by Flu
 orescence Correlation Spectroscopy (FCS)\, as well as a mathematical model
  to analyze FCS results to determine oligomerization kinetics.[iv]\,[v] Th
 is provides a method for determining p53 oligomerization kinetics in cance
 rous cells.\n\n[i] Gaglia\, G.\; Guan\, Y.\; Shah\, J. V.\; Lahav\, G. Pro
 ceedings of the National Academy of Sciences 2013\, 110 (38)\, 15497.\n\n[
 ii] Mclure\, K. G. The EMBO Journal 1998\, 17 (12)\, 3342.\n\n[iii] Urso\,
  L.\; Calabrese\, F.\; Favaretto\, A.\; Conte\, P.\; Pasello\, G. Critical
  Reviews in Oncology/Hematology 2016\, 97\, 220\n\n[iv] Gaglia\, G.\; Guan
 \, Y.\; Shah\, J. V.\; Lahav\, G. Proceedings of the National Academy of 
 Sciences 2013\, 110 (38)\, 15497\n\n[v] Kanno\, D. M.\; Levitus\, M. T
 he Journal of Physical Chemistry B 2014\, 118 (43)\, 12404 4:00 pm
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