These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
278 related articles for article (PubMed ID: 24216111)
1. The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy. Ohta S; Kawai-Noma S; Kitamura A; Pack CG; Kinjo M; Taguchi H Biochem Biophys Res Commun; 2013 Dec; 442(1-2):28-32. PubMed ID: 24216111 [TBL] [Abstract][Full Text] [Related]
2. The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation. Aslam K; Tsai CJ; Hazbun TR Prion; 2016 Nov; 10(6):444-465. PubMed ID: 27690738 [TBL] [Abstract][Full Text] [Related]
3. A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ]. Helsen CW; Glover JR Prion; 2012 Jul; 6(3):234-9. PubMed ID: 22561166 [TBL] [Abstract][Full Text] [Related]
4. Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine-HCl-treated [PSI] cells. Kawai-Noma S; Pack CG; Tsuji T; Kinjo M; Taguchi H Genes Cells; 2009 Sep; 14(9):1045-54. PubMed ID: 19674118 [TBL] [Abstract][Full Text] [Related]
5. Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP-dependent manner. Inoue Y; Kawai-Noma S; Koike-Takeshita A; Taguchi H; Yoshida M Genes Cells; 2011 May; 16(5):545-56. PubMed ID: 21453424 [TBL] [Abstract][Full Text] [Related]
6. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Shorter J; Lindquist S Science; 2004 Jun; 304(5678):1793-7. PubMed ID: 15155912 [TBL] [Abstract][Full Text] [Related]
7. Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. Kryndushkin DS; Alexandrov IM; Ter-Avanesyan MD; Kushnirov VV J Biol Chem; 2003 Dec; 278(49):49636-43. PubMed ID: 14507919 [TBL] [Abstract][Full Text] [Related]
8. Over-expression of the molecular chaperone Hsp104 in Saccharomyces cerevisiae results in the malpartition of [PSI Ness F; Cox BS; Wongwigkarn J; Naeimi WR; Tuite MF Mol Microbiol; 2017 Apr; 104(1):125-143. PubMed ID: 28073182 [TBL] [Abstract][Full Text] [Related]
9. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Shorter J; Lindquist S Mol Cell; 2006 Aug; 23(3):425-38. PubMed ID: 16885031 [TBL] [Abstract][Full Text] [Related]
10. Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds. Park YN; Zhao X; Yim YI; Todor H; Ellerbrock R; Reidy M; Eisenberg E; Masison DC; Greene LE Eukaryot Cell; 2014 May; 13(5):635-47. PubMed ID: 24632242 [TBL] [Abstract][Full Text] [Related]
11. Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants. Dergalev AA; Alexandrov AI; Ivannikov RI; Ter-Avanesyan MD; Kushnirov VV Int J Mol Sci; 2019 May; 20(11):. PubMed ID: 31146333 [TBL] [Abstract][Full Text] [Related]
12. Prion variant maintained only at high levels of the Hsp104 disaggregase. Borchsenius AS; Müller S; Newnam GP; Inge-Vechtomov SG; Chernoff YO Curr Genet; 2006 Jan; 49(1):21-9. PubMed ID: 16307272 [TBL] [Abstract][Full Text] [Related]
13. Prion and nonprion amyloids: a comparison inspired by the yeast Sup35 protein. Kushnirov VV; Vishnevskaya AB; Alexandrov IM; Ter-Avanesyan MD Prion; 2007; 1(3):179-84. PubMed ID: 19164899 [TBL] [Abstract][Full Text] [Related]
14. Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP. Schirmer EC; Lindquist S Proc Natl Acad Sci U S A; 1997 Dec; 94(25):13932-7. PubMed ID: 9391130 [TBL] [Abstract][Full Text] [Related]
15. The life of [PSI]. Cox B; Tuite M Curr Genet; 2018 Feb; 64(1):1-8. PubMed ID: 28653109 [TBL] [Abstract][Full Text] [Related]