|
ИСТИНА |
Войти в систему Регистрация |
ИСТИНА ИНХС РАН |
||
Ubiquitin recruiting chimera: more than just a PROTACстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 2 апреля 2025 г.
- Авторы: Grigoreva Tatyana A., Novikova Daria S., Melino Gerry, Barlev Nick A., Tribulovich Vyacheslav G.
- Журнал: Biology Direct
- Том: 19
- Номер: 1
- Год издания: 2024
- Издательство: BioMed Central
- Местоположение издательства: London
- Номер статьи: 55
- DOI: 10.1186/s13062-024-00497-8
- Аннотация: Ubiquitinylation of protein substrates results in various but distinct biological consequences, among which ubiquitin-mediated degradation is most well studied for its therapeutic application. Accordingly, artificially targeted ubiquitin-dependent degradation of various proteins has evolved into the therapeutically relevant PROTAC technology. This tethered ubiquitinylation of various targets coupled with a broad assortment of modifying E3 ubiquitin ligases has been made possible by rational design of bi-specific chimeric molecules that bring these proteins in proximity. However, forced ubiquitinylation inflicted by the binary warheads of a chimeric PROTAC molecule should not necessarily result in protein degradation but can be used to modulate other cellular functions. In this respect it should be noted that the ubiquitinylation of a diverse set of proteins is known to control their transport, transcriptional activity, and protein-protein interactions. This review provides examples of potential PROTAC usage based on non-degradable ubiquitinylation.
- Добавил в систему: Новикова Дарья Сергеевна