BEGIN:VCALENDAR

VERSION:2.0

PRODID:-//wp-events-plugin.com//7.2.2.1//EN

TZID:Asia/Jerusalem

X-WR-TIMEZONE:Asia/Jerusalem
BEGIN:VEVENT

UID:919@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20200914T130000

DTEND;TZID=Asia/Jerusalem:20200914T140000

DTSTAMP:20210802T125902Z

URL:https://biology.technion.ac.il/en/seminars/m-sc-graduate-seminar-roni-
 monin-2/

SUMMARY:M.Sc. Graduate Seminar- Roni Monin [No Categories]
DESCRIPTION:Location:   \n Affiliation: \n Host:\n Roni MoninFrom the Lab o
 f  Professor Michael GlickmanResearch Topic: 20S Proteasome gain-of-func
 tionduring stress conditionsThe Proteasome is a large Protein complexrespo
 nsible for protein degradation in cells. The 26S Proteasome is composed of
 two main parts – the 19S is the regulatory particle and the 20S which is
  thecatalytic core particle. Under normal conditions\, proteins are ubiqui
 tinated andthen recognized as a substrates for degradation by the 19S\, wh
 ich prepares themfor proteolysis within the 20S subcomplex.However\, durin
 g stress condition as more proteins are damaged they couldoverload the ubi
 quitin-proteasome system. Also\, during stress\, the proteasomeitself coul
 d be modified or damaged. We found preliminary evidence that hypoxiaor oxi
 dative stress conditions promote separation of the 19S from the 20S.Recent
  studies have shown the ability of the 20S to degrade non-ubiquitinatedpro
 teins. We propose a gain-of-function of the 20S during stress conditionsth
 at could help clearing damaged or partially unfolded proteins. In our work
  weshow the effect of hypoxia on proteasome composition in the cell and th
 eability of purified human proteasome to degrade a partially unfolded mode
 lsubstrate. 

END:VEVENT

BEGIN:VTIMEZONE

TZID:Asia/Jerusalem

X-LIC-LOCATION:Asia/Jerusalem

BEGIN:DAYLIGHT

DTSTART:20200327T030000

TZOFFSETFROM:+0200

TZOFFSETTO:+0300

TZNAME:IDT

END:DAYLIGHT

END:VTIMEZONE
END:VCALENDAR