295 related articles for article (PubMed ID: 31953415)
1. Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein.
Imamoglu R; Balchin D; Hayer-Hartl M; Hartl FU
Nat Commun; 2020 Jan; 11(1):365. PubMed ID: 31953415
[TBL] [Abstract][Full Text] [Related]
2. Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate.
Sharma SK; De Los Rios P; Goloubinoff P
Proteins; 2011 Jun; 79(6):1991-8. PubMed ID: 21488102
[TBL] [Abstract][Full Text] [Related]
3. Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE.
Groemping Y; Klostermeier D; Herrmann C; Veit T; Seidel R; Reinstein J
J Mol Biol; 2001 Feb; 305(5):1173-83. PubMed ID: 11162122
[TBL] [Abstract][Full Text] [Related]
4. Action of the Hsp70 chaperone system observed with single proteins.
Nunes JM; Mayer-Hartl M; Hartl FU; Müller DJ
Nat Commun; 2015 Feb; 6():6307. PubMed ID: 25686738
[TBL] [Abstract][Full Text] [Related]
5. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.
Szabo A; Langer T; Schröder H; Flanagan J; Bukau B; Hartl FU
Proc Natl Acad Sci U S A; 1994 Oct; 91(22):10345-9. PubMed ID: 7937953
[TBL] [Abstract][Full Text] [Related]
6. Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ.
Suh WC; Lu CZ; Gross CA
J Biol Chem; 1999 Oct; 274(43):30534-9. PubMed ID: 10521435
[TBL] [Abstract][Full Text] [Related]
7. Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery.
Sekhar A; Santiago M; Lam HN; Lee JH; Cavagnero S
Protein Sci; 2012 Jul; 21(7):1042-55. PubMed ID: 22549943
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. Recognizability of heterologous co-chaperones with Streptococcus intermedius DnaK and Escherichia coli DnaK.
Tomoyasu T; Tsuruno K; Tanatsugu R; Miyazaki A; Kondo H; Tabata A; Whiley RA; Sonomoto K; Nagamune H
Microbiol Immunol; 2018 Nov; 62(11):681-693. PubMed ID: 30239035
[TBL] [Abstract][Full Text] [Related]
10. Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.
Gässler CS; Buchberger A; Laufen T; Mayer MP; Schröder H; Valencia A; Bukau B
Proc Natl Acad Sci U S A; 1998 Dec; 95(26):15229-34. PubMed ID: 9860951
[TBL] [Abstract][Full Text] [Related]
11. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli.
Zolkiewski M
J Biol Chem; 1999 Oct; 274(40):28083-6. PubMed ID: 10497158
[TBL] [Abstract][Full Text] [Related]
12. Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.
Rodriguez F; Arsène-Ploetze F; Rist W; Rüdiger S; Schneider-Mergener J; Mayer MP; Bukau B
Mol Cell; 2008 Nov; 32(3):347-58. PubMed ID: 18995833
[TBL] [Abstract][Full Text] [Related]
13. Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE.
Melero R; Moro F; Pérez-Calvo MÁ; Perales-Calvo J; Quintana-Gallardo L; Llorca O; Muga A; Valpuesta JM
J Biol Chem; 2015 Apr; 290(16):10083-92. PubMed ID: 25739641
[TBL] [Abstract][Full Text] [Related]
14. Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response.
Zhang H; Yang J; Wu S; Gong W; Chen C; Perrett S
J Biol Chem; 2016 Mar; 291(13):6967-81. PubMed ID: 26823468
[TBL] [Abstract][Full Text] [Related]
15. A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.
Gamer J; Multhaup G; Tomoyasu T; McCarty JS; Rüdiger S; Schönfeld HJ; Schirra C; Bujard H; Bukau B
EMBO J; 1996 Feb; 15(3):607-17. PubMed ID: 8599944
[TBL] [Abstract][Full Text] [Related]
16. Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response.
Groemping Y; Reinstein J
J Mol Biol; 2001 Nov; 314(1):167-78. PubMed ID: 11724541
[TBL] [Abstract][Full Text] [Related]
17. Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system.
Sekhar A; Lam HN; Cavagnero S
Protein Sci; 2012 Oct; 21(10):1489-502. PubMed ID: 22886941
[TBL] [Abstract][Full Text] [Related]
18. Influence of GrpE on DnaK-substrate interactions.
Brehmer D; Gässler C; Rist W; Mayer MP; Bukau B
J Biol Chem; 2004 Jul; 279(27):27957-64. PubMed ID: 15102842
[TBL] [Abstract][Full Text] [Related]
19. Tuning of DnaK chaperone action by nonnative protein sensor DnaJ and thermosensor GrpE.
Siegenthaler RK; Christen P
J Biol Chem; 2006 Nov; 281(45):34448-56. PubMed ID: 16940296
[TBL] [Abstract][Full Text] [Related]
20. The importance of having thermosensor control in the DnaK chaperone system.
Siegenthaler RK; Christen P
J Biol Chem; 2005 Apr; 280(15):14395-401. PubMed ID: 15705578
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
