Chaperone effects on prion and nonprion aggregates

Eugene G. Rikhvanov, Nina V. Romanova, Yury O. Chernoff

Результат исследований: Публикации в книгах, отчётах, сборниках, трудах конференцийглава/разделрецензирование

12 Цитирования (Scopus)


Exposure to high temperature or other stresses induces a synthesis of heat shock proteins. Many of these proteins are molecular chaperones, and some of them help cells to cope with heat-induced denaturation and aggregation of other proteins. In the last decade, chaperones have received increased attention in connection with their role in maintenance and propagation of the Saccharomyces cerevisiae prions, infectious or heritable agents transmitted at the protein level. Recent data suggest that functioning of the chaperones in reactivation of heat-damaged proteins and in propagation of prions is based on the same molecular mechanisms but may lead to different consequences depending on the type of aggregate. In both cases the conceited and balanced action of “chaperones’ team”, including Hsp 104, Hsp70, Hsp40 and possibly other proteins, determines whether a misfolded protein is to be incorporated into an aggregate, rescued to the native state or targeted for degradation.

Язык оригиналаанглийский
Название основной публикацииProtein-Based Inheritance
ИздательTaylor & Francis
Число страниц10
ISBN (электронное издание)9781498712507
ISBN (печатное издание)9781587061387
СостояниеОпубликовано - 1 янв 2007

Предметные области Scopus

  • Земледелие и биологические науки (все)
  • Биохимия, генетика и молекулярная биология (все)


Подробные сведения о темах исследования «Chaperone effects on prion and nonprion aggregates». Вместе они формируют уникальный семантический отпечаток (fingerprint).