294 related articles for article (PubMed ID: 12788951)
1. Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK.
Mogk A; Schlieker C; Friedrich KL; Schönfeld HJ; Vierling E; Bukau B
J Biol Chem; 2003 Aug; 278(33):31033-42. PubMed ID: 12788951
[TBL] [Abstract][Full Text] [Related]
2. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation.
Mogk A; Deuerling E; Vorderwülbecke S; Vierling E; Bukau B
Mol Microbiol; 2003 Oct; 50(2):585-95. PubMed ID: 14617181
[TBL] [Abstract][Full Text] [Related]
3. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.
Goloubinoff P; Mogk A; Zvi AP; Tomoyasu T; Bukau B
Proc Natl Acad Sci U S A; 1999 Nov; 96(24):13732-7. PubMed ID: 10570141
[TBL] [Abstract][Full Text] [Related]
4. A chaperone network for the resolubilization of protein aggregates: direct interaction of ClpB and DnaK.
Schlee S; Beinker P; Akhrymuk A; Reinstein J
J Mol Biol; 2004 Feb; 336(1):275-85. PubMed ID: 14741222
[TBL] [Abstract][Full Text] [Related]
5. Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses.
Diamant S; Eliahu N; Rosenthal D; Goloubinoff P
J Biol Chem; 2001 Oct; 276(43):39586-91. PubMed ID: 11517217
[TBL] [Abstract][Full Text] [Related]
6. Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation.
Zietkiewicz S; Krzewska J; Liberek K
J Biol Chem; 2004 Oct; 279(43):44376-83. PubMed ID: 15302880
[TBL] [Abstract][Full Text] [Related]
7. Role of Hsp70 (DnaK-DnaJ-GrpE) and Hsp100 (ClpA and ClpB) chaperones in refolding and increased thermal stability of bacterial luciferases in Escherichia coli cells.
Zavilgelsky GB; Kotova VY; Mazhul' MM; Manukhov IV
Biochemistry (Mosc); 2002 Sep; 67(9):986-92. PubMed ID: 12387711
[TBL] [Abstract][Full Text] [Related]
8. Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates.
Obuchowski I; Piróg A; Stolarska M; Tomiczek B; Liberek K
PLoS Genet; 2019 Oct; 15(10):e1008479. PubMed ID: 31652260
[TBL] [Abstract][Full Text] [Related]
9. Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides.
Schlieker C; Tews I; Bukau B; Mogk A
FEBS Lett; 2004 Dec; 578(3):351-6. PubMed ID: 15589844
[TBL] [Abstract][Full Text] [Related]
10. Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry.
Cheng G; Basha E; Wysocki VH; Vierling E
J Biol Chem; 2008 Sep; 283(39):26634-42. PubMed ID: 18621732
[TBL] [Abstract][Full Text] [Related]
11. Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System.
Zolkiewski M; Chesnokova LS; Witt SN
Curr Protoc Protein Sci; 2016 Feb; 83():28.10.1-28.10.18. PubMed ID: 26836408
[TBL] [Abstract][Full Text] [Related]
12. Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation.
Miot M; Reidy M; Doyle SM; Hoskins JR; Johnston DM; Genest O; Vitery MC; Masison DC; Wickner S
Proc Natl Acad Sci U S A; 2011 Apr; 108(17):6915-20. PubMed ID: 21474779
[TBL] [Abstract][Full Text] [Related]
13. Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.
Diamant S; Ben-Zvi AP; Bukau B; Goloubinoff P
J Biol Chem; 2000 Jul; 275(28):21107-13. PubMed ID: 10801805
[TBL] [Abstract][Full Text] [Related]
14. The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70.
Gonçalves CC; Sharon I; Schmeing TM; Ramos CHI; Young JC
Sci Rep; 2021 Aug; 11(1):17139. PubMed ID: 34429462
[TBL] [Abstract][Full Text] [Related]
15. Dicarboxylic amino acids and glycine-betaine regulate chaperone-mediated protein-disaggregation under stress.
Diamant S; Rosenthal D; Azem A; Eliahu N; Ben-Zvi AP; Goloubinoff P
Mol Microbiol; 2003 Jul; 49(2):401-10. PubMed ID: 12828638
[TBL] [Abstract][Full Text] [Related]
16. DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine.
Doyle SM; Hoskins JR; Wickner S
J Biol Chem; 2012 Aug; 287(34):28470-9. PubMed ID: 22745126
[TBL] [Abstract][Full Text] [Related]
17. Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli.
Kedzierska S; Chesnokova LS; Witt SN; Zolkiewski M
Arch Biochem Biophys; 2005 Dec; 444(1):61-5. PubMed ID: 16289019
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration.
Diamant S; Goloubinoff P
Biochemistry; 1998 Jul; 37(27):9688-94. PubMed ID: 9657681
[TBL] [Abstract][Full Text] [Related]
20. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.
Mogk A; Tomoyasu T; Goloubinoff P; Rüdiger S; Röder D; Langen H; Bukau B
EMBO J; 1999 Dec; 18(24):6934-49. PubMed ID: 10601016
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
