371 related articles for article (PubMed ID: 20130680)
1. 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]
2. 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]
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. 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]
5. 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]
6. 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]
7. The molecular chaperone Hsp104--a molecular machine for protein disaggregation.
Bösl B; Grimminger V; Walter S
J Struct Biol; 2006 Oct; 156(1):139-48. PubMed ID: 16563798
[TBL] [Abstract][Full Text] [Related]
8. The ClpB/Hsp104 molecular chaperone-a protein disaggregating machine.
Lee S; Sowa ME; Choi JM; Tsai FT
J Struct Biol; 2004; 146(1-2):99-105. PubMed ID: 15037241
[TBL] [Abstract][Full Text] [Related]
9. M domains couple the ClpB threading motor with the DnaK chaperone activity.
Haslberger T; Weibezahn J; Zahn R; Lee S; Tsai FT; Bukau B; Mogk A
Mol Cell; 2007 Jan; 25(2):247-60. PubMed ID: 17244532
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. 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]
12. 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]
13. Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments.
Haslberger T; Zdanowicz A; Brand I; Kirstein J; Turgay K; Mogk A; Bukau B
Nat Struct Mol Biol; 2008 Jun; 15(6):641-50. PubMed ID: 18488042
[TBL] [Abstract][Full Text] [Related]
14. The N-terminal domain of Escherichia coli ClpB enhances chaperone function.
Chow IT; Barnett ME; Zolkiewski M; Baneyx F
FEBS Lett; 2005 Aug; 579(20):4242-8. PubMed ID: 16051221
[TBL] [Abstract][Full Text] [Related]
15. Structure and function of the molecular chaperone Hsp104 from yeast.
Grimminger-Marquardt V; Lashuel HA
Biopolymers; 2010 Mar; 93(3):252-76. PubMed ID: 19768774
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. Hsp104 and ClpB: protein disaggregating machines.
Doyle SM; Wickner S
Trends Biochem Sci; 2009 Jan; 34(1):40-8. PubMed ID: 19008106
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. Disaggregases, molecular chaperones that resolubilize protein aggregates.
Mokry DZ; Abrahão J; Ramos CH
An Acad Bras Cienc; 2015 Aug; 87(2 Suppl):1273-92. PubMed ID: 26312418
[TBL] [Abstract][Full Text] [Related]
20. Common and specific mechanisms of AAA+ proteins involved in protein quality control.
Mogk A; Haslberger T; Tessarz P; Bukau B
Biochem Soc Trans; 2008 Feb; 36(Pt 1):120-5. PubMed ID: 18208398
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
