{"id":19,"date":"2020-05-15T09:25:03","date_gmt":"2020-05-15T09:25:03","guid":{"rendered":"http:\/\/www.amyloid.bti.vu.lt\/?page_id=19"},"modified":"2026-11-14T18:05:13","modified_gmt":"2026-11-14T16:05:13","slug":"apie","status":"publish","type":"page","link":"http:\/\/www.amyloid.bti.vu.lt\/lt\/","title":{"rendered":""},"content":{"rendered":"
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Understanding how proteins misfold, aggregate and self-replicate<\/strong><\/p>\n\n\n\n

We study the mechanisms of amyloid fibril formation and liquid-liquid phase seperation \u2014 the processes behind neurodegenerative and other amyloid-related diseases<\/p>\n<\/div>

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Baltymai – vienos svarbiausi\u0173 biomolekuli\u0173, kurios dalyvauja beveik visuose biologiniuose procesuose. Tam, kad atlikt\u0173 savo funkcij\u0105, \u0161ios biomolekul\u0117s turi \u012fgauti natyvi\u0105 funkcionali\u0105 konformacij\u0105. Tam tikrais atvejais baltymai nesugeba \u012fgauti ar likti natyvioje konformacijoje ir yra link\u0119 agreguoti \u012f netirpius fibrilinius agregatus, dar \u017einomus kaip amiloidai. Daugiau nei penkiasde\u0161imties \u017emogaus lig\u0173 \u012fskaitant Alzheimerio lig\u0105, Parkinsono lig\u0105, II tipo diabet\u0105, bei prion\u0173 ligas, atsiradimas ir progresija yra siejama su specifini\u0173 peptid\u0173 ir baltym\u0173 nesugeb\u0117jimu \u012fgauti natyvi\u0105 konformacj\u0105 ar i\u0161likti joje, bei toliau sekan\u010dia \u0161i\u0173 monomerini\u0173 peptid\u0173 ar baltym\u0173 konversija \u012f amiloidinius agregatus. Pastaraisiais metais amiloid\u0173 susidarymo tyrimai tapo ypa\u010d aktual\u016bs, kadangi buvo pripa\u017einta, jog daugelis su amiloidais siejam\u0173 lig\u0173 neb\u0117ra retos ir yra vienos i\u0161 da\u017eniausiai pasirei\u0161kian\u010di\u0173 lig\u0173 senstan\u010dioje visuomen\u0117je. Milijonai \u017emoni\u0173 visame pasaulyje ken\u010dia nuo \u0161i\u0173 lig\u0173, vien Alzheimerio ar Parkinsono ligomis sergan\u010di\u0173 \u017emoni\u0173 yra daugiau nei 50 milijon\u0173. Nepaisant reik\u0161ming\u0173 mokslinink\u0173 pastang\u0173, molekuliniai ir mechanistiniai ry\u0161iai tarp baltym\u0173 agregacijos ir agregat\u0173 toksi\u0161kumo i\u0161lieka neai\u0161k\u016bs ir sunkiai charakterizuojami. Taip pat \u0161iai dienai, deja, n\u0117ra nei vieno veiksmingo vaistinio preparato ar gydymo metodo skirto lig\u0173 siejam\u0173 su amiloidais prevencijai ar gydymui. Vienos i\u0161 pagrindini\u0173 to prie\u017eas\u010di\u0173 yra be galo sud\u0117tingi amiloidini\u0173 agregat\u0173 susidarymo ir savireplikacijos mechanizmai, bei s\u0105lyginiai skurdus \u0161i\u0173 mechanizm\u0173 supratimas. S\u0117kminga bet kokios ligos prevencija ar gydymas yra galimi tik tuomet jei dauguma proces\u0173 susijusi\u0173 su ligos atsiradimu bei progresija yra \u017einomi ir yra pakankamai gerai suprasti. <\/p>\n\n\n\n

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Mokslini\u0173 darb\u0173 kryptys<\/p>\n\n\n\n

M\u016bs\u0173 tikslas <\/h2>\n\n\n\n

Savo tyrimais mes siekiame prisid\u0117ti prie gilesnio amiloidin\u0117s agregacijos proceso supratimo. Naudodami \u012fvairius biofizikinius, biocheminius, molekulin\u0117s biologijos bei bioinformatikos metodus mes bandome i\u0161siai\u0161kinti baltym\u0173 amiloidin\u0117s agregacijos mechanizmus, tikriname \u012fvairi\u0173 aplinkos faktori\u0173 poveik\u012f agregacijos procesui ir amiloidini\u0173 fibrili\u0173 strukt\u016brai, taip pat ie\u0161kome jungini\u0173, galin\u010di\u0173 sul\u0117tinti ar sustabdyti amiloidini\u0173 baltym\u0173 agregacij\u0105. <\/p>\n\n\n\n

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Jei esi studentas ir labai nor\u0117tum padirb\u0117ti su amiloidiniais baltymais – para\u0161yk ar u\u017esuk \u012f sve\u010dius<\/a>.<\/h4>","protected":false},"excerpt":{"rendered":"

Understanding how proteins misfold, aggregate and self-replicate We study the mechanisms of amyloid fibril formation and liquid-liquid phase seperation \u2014 the processes behind neurodegenerative and other amyloid-related diseases Baltymai – vienos svarbiausi\u0173 biomolekuli\u0173, kurios dalyvauja beveik visuose biologiniuose procesuose. Tam, kad atlikt\u0173 savo funkcij\u0105, \u0161ios biomolekul\u0117s turi \u012fgauti natyvi\u0105 funkcionali\u0105 konformacij\u0105. Tam tikrais atvejais baltymai […]<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-19","page","type-page","status-publish","hentry"],"rise-blocks_excerpt":"Understanding how proteins misfold, aggregate and self-replicate We study the mechanisms of amyloid fibril formation and liquid-liquid phase seperation \u2014 the processes behind neurodegenerative and other amyloid-related diseases Baltymai – vienos svarbiausi\u0173 biomolekuli\u0173, kurios dalyvauja beveik visuose biologiniuose procesuose. Tam, kad atlikt\u0173 savo funkcij\u0105, \u0161ios biomolekul\u0117s turi \u012fgauti natyvi\u0105 funkcionali\u0105 konformacij\u0105. Tam tikrais atvejais baltymai nesugeba \u012fgauti ar likti natyvioje..","yoast_head":"\n- Amiloid\u0173 tyrimo sektorius<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"http:\/\/www.amyloid.bti.vu.lt\/lt\/\" \/>\n<meta property=\"og:locale\" content=\"lt_LT\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"- Amiloid\u0173 tyrimo sektorius\" \/>\n<meta property=\"og:description\" content=\"Understanding how proteins misfold, aggregate and self-replicate We study the mechanisms of amyloid fibril formation and liquid-liquid phase seperation \u2014 the processes behind neurodegenerative and other amyloid-related diseases Baltymai – vienos svarbiausi\u0173 biomolekuli\u0173, kurios dalyvauja beveik visuose biologiniuose procesuose. Tam, kad atlikt\u0173 savo funkcij\u0105, \u0161ios biomolekul\u0117s turi \u012fgauti natyvi\u0105 funkcionali\u0105 konformacij\u0105. 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