369 related articles for article (PubMed ID: 22160895)
1. Heat-shock protein fusion vectors for improved expression of soluble recombinant proteins in Escherichia coli.
Kyratsous CA; Panagiotidis CA
Methods Mol Biol; 2012; 824():109-29. PubMed ID: 22160895
[TBL] [Abstract][Full Text] [Related]
2. Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.
Buchberger A; Schröder H; Hesterkamp T; Schönfeld HJ; Bukau B
J Mol Biol; 1996 Aug; 261(3):328-33. PubMed ID: 8780775
[TBL] [Abstract][Full Text] [Related]
3. Recombinant maize protoporphyrinogen IX oxidase expressed in Escherichia coli forms complexes with GroEL and DnaK chaperones.
de Marco A; Volrath S; Bruyere T; Law M; Fonné-Pfister R
Protein Expr Purif; 2000 Oct; 20(1):81-6. PubMed ID: 11035954
[TBL] [Abstract][Full Text] [Related]
4. Toothpicks, serendipity and the emergence of the Escherichia coli DnaK (Hsp70) and GroEL (Hsp60) chaperone machines.
Georgopoulos C
Genetics; 2006 Dec; 174(4):1699-707. PubMed ID: 17182732
[No Abstract] [Full Text] [Related]
5. DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli.
Chen Y; Song J; Sui SF; Wang DN
Protein Expr Purif; 2003 Dec; 32(2):221-31. PubMed ID: 14965767
[TBL] [Abstract][Full Text] [Related]
6. Interferon-gamma is a target for binding and folding by both Escherichia coli chaperone model systems GroEL/GroES and DnaK/DnaJ/GrpE.
Vandenbroeck K; Billiau A
Biochimie; 1998; 80(8-9):729-37. PubMed ID: 9865495
[TBL] [Abstract][Full Text] [Related]
7. Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli.
Rinas U; Hoffmann F; Betiku E; Estapé D; Marten S
J Biotechnol; 2007 Jan; 127(2):244-57. PubMed ID: 16945443
[TBL] [Abstract][Full Text] [Related]
8. Consortium of fold-catalyzing proteins increases soluble expression of cyclohexanone monooxygenase in recombinant Escherichia coli.
Lee DH; Kim MD; Lee WH; Kweon DH; Seo JH
Appl Microbiol Biotechnol; 2004 Feb; 63(5):549-52. PubMed ID: 12827321
[TBL] [Abstract][Full Text] [Related]
9. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.
Kerner MJ; Naylor DJ; Ishihama Y; Maier T; Chang HC; Stines AP; Georgopoulos C; Frishman D; Hayer-Hartl M; Mann M; Hartl FU
Cell; 2005 Jul; 122(2):209-20. PubMed ID: 16051146
[TBL] [Abstract][Full Text] [Related]
10. GroEL to DnaK chaperone network behind the stability modulation of σ(32) at physiological temperature in Escherichia coli.
Patra M; Roy SS; Dasgupta R; Basu T
FEBS Lett; 2015 Dec; 589(24 Pt B):4047-52. PubMed ID: 26545493
[TBL] [Abstract][Full Text] [Related]
11. Bacterial inclusion bodies are cytotoxic in vivo in absence of functional chaperones DnaK or GroEL.
González-Montalbán N; Carrió MM; Cuatrecasas S; Arís A; Villaverde A
J Biotechnol; 2005 Sep; 118(4):406-12. PubMed ID: 16024126
[TBL] [Abstract][Full Text] [Related]
12. Chaperone-fusion expression plasmid vectors for improved solubility of recombinant proteins in Escherichia coli.
Kyratsous CA; Silverstein SJ; DeLong CR; Panagiotidis CA
Gene; 2009 Jul; 440(1-2):9-15. PubMed ID: 19328840
[TBL] [Abstract][Full Text] [Related]
13. 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]
14. Complementation studies of the DnaK-DnaJ-GrpE chaperone machineries from Vibrio harveyi and Escherichia coli, both in vivo and in vitro.
Zmijewski MA; Kwiatkowska JM; Lipińska B
Arch Microbiol; 2004 Dec; 182(6):436-49. PubMed ID: 15448982
[TBL] [Abstract][Full Text] [Related]
15. DnaJ potentiates the interaction between DnaK and alpha-helical peptides.
de Crouy-Chanel A; Hodges RS; Kohiyama M; Richarme G
Biochem Biophys Res Commun; 1997 Apr; 233(3):627-30. PubMed ID: 9168902
[TBL] [Abstract][Full Text] [Related]
16. GroEL chaperone binding to beetle luciferases and the implications for refolding when co-expressed.
Venkatesh B; Arifuzzaman M; Mori H; Taguchi T; Ohmiya Y
Biosci Biotechnol Biochem; 2004 Oct; 68(10):2096-103. PubMed ID: 15502355
[TBL] [Abstract][Full Text] [Related]
17. Construction of Escherichia coli dnaK-deletion mutant infected by lambdaDE3 for overexpression and purification of recombinant GrpE proteins.
Sugimoto S; Higashi C; Yoshida H; Sonomoto K
Protein Expr Purif; 2008 Jul; 60(1):31-6. PubMed ID: 18434193
[TBL] [Abstract][Full Text] [Related]
18. Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli.
Gupta P; Aggarwal N; Batra P; Mishra S; Chaudhuri TK
Int J Biochem Cell Biol; 2006; 38(11):1975-85. PubMed ID: 16822698
[TBL] [Abstract][Full Text] [Related]
19. The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis.
Mogk A; Homuth G; Scholz C; Kim L; Schmid FX; Schumann W
EMBO J; 1997 Aug; 16(15):4579-90. PubMed ID: 9303302
[TBL] [Abstract][Full Text] [Related]
20. Kinetics of heat-shock response and inclusion body formation during temperature-induced production of basic fibroblast growth factor in high-cell-density cultures of recombinant Escherichia coli.
Hoffmann F; Rinas U
Biotechnol Prog; 2000; 16(6):1000-7. PubMed ID: 11101327
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
