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</o:shapelayout></xml><![endif]--></head><body lang=SL link="#0563C1" vlink="#954F72"><div class=WordSection1><p class=MsoNormal>Vabimo vas na 6. predavanje iz sklopa "Kolokviji na IJS" v letu 2018/19, ki bo <strong><span style='color:red'>v sredo, 9. januarja 2019, ob 13. uri </span></strong><span style='color:red'>v Veliki predavalnici Instituta »Jožef Stefan«</span> na Jamovi cesti 39 v Ljubljani. Napovednik predavanja najdete tudi na naslovu <a href="http://www.ijs.si/ijsw/Koledar_prireditev">http://www.ijs.si/ijsw/Koledar_prireditev</a>, posnetke preteklih predavanj<span style='color:blue'> </span>pa na <a href="http://videolectures.net/kolokviji_ijs">http://videolectures.net/kolokviji_ijs</a>. <o:p></o:p></p><p class=MsoNormal style='margin-bottom:12.0pt'>~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~<strong><span style='color:red'><o:p></o:p></span></strong></p><p class=MsoNormal><b><span lang=EN-US>prof. dr. Eva Žerovnik</span></b><span lang=EN-US><o:p></o:p></span></p><p class=MsoNormal><i><span lang=EN-US>Institut Jožef Stefan, Ljubljana<o:p></o:p></span></i></p><p class=MsoNormal><i><span lang=EN-US><o:p> </o:p></span></i></p><p class=MsoNormal align=center style='mso-margin-top-alt:auto;margin-bottom:12.0pt;text-align:center'><b><span style='font-size:14.0pt'>Človeški stefin B kot modelni protein za študij zvijanja in agregacije proteinov<o:p></o:p></span></b></p><p class=MsoNormal style='mso-margin-top-alt:auto;margin-bottom:12.0pt;text-align:justify'>Mehanizmi zvijanja in agregacije proteinov so skupni večini proteinov. Proteini se razlikujejo glede na to, ali so zviti ali intrinzično odviti, a vsi agregirajo preko delno odvitih intermediatov in mehanizem večinoma poteka kot nukleacija in rast. Da bi se naučili več o teh mehanizmih, smo preučevali proteinsko zvijanje in agregacijo do amiloidnih fibril dveh homolognih proteinov stefina A in B ter njunih himernih variant. Zatem smo razširili študije zvitja in agregacije nekaterih EPM1 mutant stefina B tudi na sesalske celice. Nenazadnje smo del raziskav posvetili splošnemu mehanizmu, kako oligomeri amiloidogenih proteinov preluknjajo membrane. Doslej smo preverili modelne membrane in pokazali, da oligomeri in protofibrili stefina B sprožijo prehajanje kalceina preko membrane, povečajo površinsko napetost, se vežejo na lipidno površino in sprožijo stopničaste tokove. Kapaciteta oligomerov za vezavo membrane korelira s povečanjem reaktivnih kisikovih zvrsti (ROS) v celicah, kar nazadnje pripelje do celične smrti. Predstavili bomo nove raziskave, ki podpirajo hipotezo o amiloidnih porah, ki predpostavlja, da se oligomeri amiloidogenih proteinov obnašajo podobno kot peptidi, ki tvorijo pore. Ti oligomeri se verjetno vežejo na različne celične membrane in jih celo preluknjajo. S sodobnimi visoko ločljivimi mikroskopskimi metodami slikanja bi bilo najbrž mogoče te oligomere (velikost od 20 do 200 nm) tudi videti ter tako ugotoviti, kje natanko se nahajajo in katere celične procese sprožijo.<o:p></o:p></p><p class=MsoNormal style='mso-margin-top-alt:auto;margin-bottom:12.0pt;text-align:justify'>Predavanje bo v angleščini.<o:p></o:p></p><p class=MsoNormal style='mso-margin-top-alt:auto;margin-bottom:12.0pt'><strong><span style='color:red'>Lepo vabljeni!<o:p></o:p></span></strong></p><p class=MsoNormal style='mso-margin-top-alt:auto;margin-bottom:12.0pt'><strong><span style='color:red'><o:p> </o:p></span></strong></p><p class=MsoNormal style='mso-margin-top-alt:auto;margin-bottom:12.0pt;margin-left:212.4pt;text-indent:35.4pt'><span style='color:black'>*****</span><o:p></o:p></p><span style='font-size:12.0pt;font-family:"Times New Roman",serif;mso-fareast-language:SL'><br clear=all style='page-break-before:always'></span><p class=MsoNormal><span lang=EN-US style='color:black'>We invite you to the 6th Institute colloquium in the academic year 2018/19. The colloquium will be held </span><b><span lang=EN-US style='color:red'>on Wednesday, January </span><span style='color:red'>9, 2019 at 1 PM</span></b><span style='color:red'> in <b>the main Institute lecture hall</b></span><span style='color:black'>, Jamova 39, Ljubljana. To read the abstract click </span><span style='color:#1F497D'><a href="http://www.ijs.si/ijsw/Koledar_prireditev">http://www.ijs.si/ijsw/Koledar_prireditev</a>. <o:p></o:p></span></p><p class=MsoNormal><span style='color:black'>Past colloquia are posted on</span><span style='color:#1F497D'> <a href="http://videolectures.net/kolokviji_ijs">http://videolectures.net/kolokviji_ijs</a>.<o:p></o:p></span></p><p class=MsoNormal style='margin-bottom:12.0pt'>********************************************<b><o:p></o:p></b></p><p class=MsoNormal><b><span lang=EN-US>prof. dr. Eva Žerovnik<o:p></o:p></span></b></p><p class=MsoNormal><i><span lang=EN-US>Institut Jožef Stefan, Ljubljana<o:p></o:p></span></i></p><p class=MsoNormal><i><span lang=EN-US><o:p> </o:p></span></i></p><p class=Default align=center style='text-align:center'><b><span style='font-size:14.0pt;font-family:"Times New Roman",serif;color:#202020;mso-fareast-language:SL'>Human stefin B as a model protein to study protein folding and aggregation<o:p></o:p></span></b></p><p class=Default><span lang=EN-US style='font-family:"Times New Roman",serif'><o:p> </o:p></span></p><p class=MsoNormal style='text-align:justify'><span lang=EN-US>Folding and aggregation mechanisms are in common to most proteins. Proteins differ whether they are folded or intrinsically unfolded/disordered, however, all aggregate over partially unfolded intermediates and the mechanism in most cases conforms to nucleation and growth. In order to get to know more of the mechanism, we studied folding and aggregation to amyloid fibrils of two homologous proteins, stefins A and B and their chimeric variants. Further, we performed cellular studies of certain EPM1 stefin B mutants. Part of our studies was devoted to the possible common mechanism of how amyloid proteins form pores within membranes. Thus far we checked model membranes and it was shown that oligomers and protofibrils of stefin B release calcein from lipid vesicles, increase pressure on the lipid surface, and finally lead to step-wise currents. The capacity of the oligomers to bind to cellular membranes correlates with an increase of reactive oxygen species (ROS) and leads ultimately to cell death. We will present novel studies supporting the “amyloid pore” hypothesis, which assumes that the oligomers of amyloidogenic proteins behave similarly to pore forming peptides. The oligomers likely bind various cellular membranes and even perforate them. With modern high–resolution microscopic methods it should be possible to image these oligomers (of the size between 20 and 200 nm) and in such a way determine their detailed localization and down-stream processes.<o:p></o:p></span></p><p class=MsoNormal><o:p> </o:p></p><p class=MsoNormal>Cordially invited!<o:p></o:p></p><p class=MsoNormal><span style='font-size:11.0pt;font-family:"Calibri",sans-serif;mso-fareast-language:EN-US'><o:p> </o:p></span></p></div></body></html>