These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

241 related articles for article (PubMed ID: 12606060)

  • 1. Role of molecular chaperones in inclusion body formation.
    Carrió MM; Villaverde A
    FEBS Lett; 2003 Feb; 537(1-3):215-21. PubMed ID: 12606060
    [TBL] [Abstract][Full Text] [Related]  

  • 2. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells.
    Thomas JG; Baneyx F
    Mol Microbiol; 2000 Jun; 36(6):1360-70. PubMed ID: 10931286
    [TBL] [Abstract][Full Text] [Related]  

  • 3. 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]  

  • 4. 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]  

  • 5. Divergent genetic control of protein solubility and conformational quality in Escherichia coli.
    García-Fruitós E; Martínez-Alonso M; Gonzàlez-Montalbán N; Valli M; Mattanovich D; Villaverde A
    J Mol Biol; 2007 Nov; 374(1):195-205. PubMed ID: 17920630
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Localization of chaperones DnaK and GroEL in bacterial inclusion bodies.
    Carrió MM; Villaverde A
    J Bacteriol; 2005 May; 187(10):3599-601. PubMed ID: 15866952
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones.
    de Marco A; Vigh L; Diamant S; Goloubinoff P
    Cell Stress Chaperones; 2005; 10(4):329-39. PubMed ID: 16333986
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing Heat-shock proteins.
    Thomas JG; Baneyx F
    J Biol Chem; 1996 May; 271(19):11141-7. PubMed ID: 8626659
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Microbial molecular chaperones.
    Lund PA
    Adv Microb Physiol; 2001; 44():93-140. PubMed ID: 11407116
    [TBL] [Abstract][Full Text] [Related]  

  • 10. The impact of dnaKJ overexpression on recombinant protein solubility results from antagonistic effects on the control of protein quality.
    Petersson L; Carrió MM; Vera A; Villaverde A
    Biotechnol Lett; 2004 Apr; 26(7):595-601. PubMed ID: 15168861
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Recent advances in understanding catalysis of protein folding by molecular chaperones.
    Balchin D; Hayer-Hartl M; Hartl FU
    FEBS Lett; 2020 Sep; 594(17):2770-2781. PubMed ID: 32446288
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Role of the disaggregase ClpB in processing of proteins aggregated as inclusion bodies.
    Zblewska K; Krajewska J; Zolkiewski M; Kędzierska-Mieszkowska S
    Arch Biochem Biophys; 2014 Aug; 555-556():23-7. PubMed ID: 24943258
    [TBL] [Abstract][Full Text] [Related]  

  • 13. IbpA the small heat shock protein from Escherichia coli forms fibrils in the absence of its cochaperone IbpB.
    Ratajczak E; Strózecka J; Matuszewska M; Zietkiewicz S; Kuczyńska-Wiśnik D; Laskowska E; Liberek K
    FEBS Lett; 2010 Jun; 584(11):2253-7. PubMed ID: 20433838
    [TBL] [Abstract][Full Text] [Related]  

  • 14. 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]  

  • 15. 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]  

  • 16. Differential degradation for small heat shock proteins IbpA and IbpB is synchronized in Escherichia coli: implications for their functional cooperation in substrate refolding.
    Shi X; Yan L; Zhang H; Sun K; Chang Z; Fu X
    Biochem Biophys Res Commun; 2014 Sep; 452(3):402-7. PubMed ID: 25173932
    [TBL] [Abstract][Full Text] [Related]  

  • 17. 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]  

  • 18. 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]  

  • 19. 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]  

  • 20. 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]  

    [Next]    [New Search]
    of 13.