575 related articles for article (PubMed ID: 22580344)
1. Chaperone networks in protein disaggregation and prion propagation.
Winkler J; Tyedmers J; Bukau B; Mogk A
J Struct Biol; 2012 Aug; 179(2):152-60. PubMed ID: 22580344
[TBL] [Abstract][Full Text] [Related]
2. Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation.
Haslberger T; Bukau B; Mogk A
Biochem Cell Biol; 2010 Feb; 88(1):63-75. PubMed ID: 20130680
[TBL] [Abstract][Full Text] [Related]
3. Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation.
Tessarz P; Mogk A; Bukau B
Mol Microbiol; 2008 Apr; 68(1):87-97. PubMed ID: 18312264
[TBL] [Abstract][Full Text] [Related]
4. Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions.
Reidy M; Miot M; Masison DC
Genetics; 2012 Sep; 192(1):185-93. PubMed ID: 22732191
[TBL] [Abstract][Full Text] [Related]
5. Mechanism of Hsp104/ClpB inhibition by prion curing Guanidinium hydrochloride.
Kummer E; Oguchi Y; Seyffer F; Bukau B; Mogk A
FEBS Lett; 2013 Mar; 587(6):810-7. PubMed ID: 23416293
[TBL] [Abstract][Full Text] [Related]
6. Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.
Reidy M; Sharma R; Shastry S; Roberts BL; Albino-Flores I; Wickner S; Masison DC
PLoS Genet; 2014 Oct; 10(10):e1004720. PubMed ID: 25329162
[TBL] [Abstract][Full Text] [Related]
7. Bacterial and Yeast AAA+ Disaggregases ClpB and Hsp104 Operate through Conserved Mechanism Involving Cooperation with Hsp70.
Kummer E; Szlachcic A; Franke KB; Ungelenk S; Bukau B; Mogk A
J Mol Biol; 2016 Oct; 428(21):4378-4391. PubMed ID: 27616763
[TBL] [Abstract][Full Text] [Related]
8. Functions of yeast Hsp40 chaperone Sis1p dispensable for prion propagation but important for prion curing and protection from prion toxicity.
Kirkland PA; Reidy M; Masison DC
Genetics; 2011 Jul; 188(3):565-77. PubMed ID: 21555396
[TBL] [Abstract][Full Text] [Related]
9. Molecular chaperone Hsp104 can promote yeast prion generation.
Kryndushkin DS; Engel A; Edskes H; Wickner RB
Genetics; 2011 Jun; 188(2):339-48. PubMed ID: 21467567
[TBL] [Abstract][Full Text] [Related]
10. [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.
Moriyama H; Edskes HK; Wickner RB
Mol Cell Biol; 2000 Dec; 20(23):8916-22. PubMed ID: 11073991
[TBL] [Abstract][Full Text] [Related]
11. Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation.
Winkler J; Tyedmers J; Bukau B; Mogk A
J Cell Biol; 2012 Aug; 198(3):387-404. PubMed ID: 22869599
[TBL] [Abstract][Full Text] [Related]
12. Chaperone functional specificity promotes yeast prion diversity.
Killian AN; Hines JK
PLoS Pathog; 2018 Jan; 14(1):e1006695. PubMed ID: 29300791
[No Abstract] [Full Text] [Related]
13. N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression.
Hung GC; Masison DC
Genetics; 2006 Jun; 173(2):611-20. PubMed ID: 16582428
[TBL] [Abstract][Full Text] [Related]
14. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.
Shorter J; Lindquist S
EMBO J; 2008 Oct; 27(20):2712-24. PubMed ID: 18833196
[TBL] [Abstract][Full Text] [Related]
15. Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.
Weibezahn J; Tessarz P; Schlieker C; Zahn R; Maglica Z; Lee S; Zentgraf H; Weber-Ban EU; Dougan DA; Tsai FT; Mogk A; Bukau B
Cell; 2004 Nov; 119(5):653-65. PubMed ID: 15550247
[TBL] [Abstract][Full Text] [Related]
16. Novel insights into the mechanism of chaperone-assisted protein disaggregation.
Weibezahn J; Schlieker C; Tessarz P; Mogk A; Bukau B
Biol Chem; 2005 Aug; 386(8):739-44. PubMed ID: 16201868
[TBL] [Abstract][Full Text] [Related]
17. In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104.
Tipton KA; Verges KJ; Weissman JS
Mol Cell; 2008 Nov; 32(4):584-91. PubMed ID: 19026788
[TBL] [Abstract][Full Text] [Related]
18. DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface.
Acebrón SP; Martín I; del Castillo U; Moro F; Muga A
FEBS Lett; 2009 Sep; 583(18):2991-6. PubMed ID: 19698713
[TBL] [Abstract][Full Text] [Related]
19. The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions.
Kimura Y; Koitabashi S; Kakizuka A; Fujita T
Genes Cells; 2004 Aug; 9(8):685-96. PubMed ID: 15298677
[TBL] [Abstract][Full Text] [Related]
20. Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation.
Dulle JE; Stein KC; True HL
PLoS One; 2014; 9(1):e87521. PubMed ID: 24466354
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
