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 *

280 related articles for article (PubMed ID: 19358587)

  • 1. Effect of crowding agents, signal peptide, and chaperone SecB on the folding and aggregation of E. coli maltose binding protein.
    Kulothungan SR; Das M; Johnson M; Ganesh C; Varadarajan R
    Langmuir; 2009 Jun; 25(12):6637-48. PubMed ID: 19358587
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Effect of signal peptide on the stability and folding kinetics of maltose binding protein.
    Beena K; Udgaonkar JB; Varadarajan R
    Biochemistry; 2004 Mar; 43(12):3608-19. PubMed ID: 15035631
    [TBL] [Abstract][Full Text] [Related]  

  • 3. The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro.
    Weiss JB; Bassford PJ
    J Bacteriol; 1990 Jun; 172(6):3023-9. PubMed ID: 2188948
    [TBL] [Abstract][Full Text] [Related]  

  • 4. SecB-mediated protein export need not occur via kinetic partitioning.
    Krishnan B; Kulothungan SR; Patra AK; Udgaonkar JB; Varadarajan R
    J Mol Biol; 2009 Jan; 385(4):1243-56. PubMed ID: 19028503
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Export of the periplasmic maltose-binding protein of Escherichia coli.
    Bassford PJ
    J Bioenerg Biomembr; 1990 Jun; 22(3):401-39. PubMed ID: 2202725
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Direct observation of chaperone-induced changes in a protein folding pathway.
    Bechtluft P; van Leeuwen RG; Tyreman M; Tomkiewicz D; Nouwen N; Tepper HL; Driessen AJ; Tans SJ
    Science; 2007 Nov; 318(5855):1458-61. PubMed ID: 18048690
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Mutations that improve export of maltose-binding protein in SecB- cells of Escherichia coli.
    Collier DN; Bassford PJ
    J Bacteriol; 1989 Sep; 171(9):4640-7. PubMed ID: 2670890
    [TBL] [Abstract][Full Text] [Related]  

  • 8. A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB.
    Volkert TL; Baleja JD; Kumamoto CA
    Biochem Biophys Res Commun; 1999 Nov; 264(3):949-54. PubMed ID: 10544036
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB.
    Kimsey HH; Dagarag MD; Kumamoto CA
    J Biol Chem; 1995 Sep; 270(39):22831-5. PubMed ID: 7559415
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein.
    Gannon PM; Kumamoto CA
    J Biol Chem; 1993 Jan; 268(3):1590-5. PubMed ID: 8420934
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Functional identification of the SecB homologue in Methanococcus jannaschii and direct interaction of SecB with trigger factor.
    Ha SC; Lee TH; Cha SS; Kim KK
    Biochem Biophys Res Commun; 2004 Mar; 315(4):1039-44. PubMed ID: 14985117
    [TBL] [Abstract][Full Text] [Related]  

  • 12. The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein.
    Collier DN; Bankaitis VA; Weiss JB; Bassford PJ
    Cell; 1988 Apr; 53(2):273-83. PubMed ID: 2834066
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.
    Weiss JB; Ray PH; Bassford PJ
    Proc Natl Acad Sci U S A; 1988 Dec; 85(23):8978-82. PubMed ID: 2848249
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Kinetics and energetics of the translocation of maltose binding protein folding mutants.
    Tomkiewicz D; Nouwen N; Driessen AJ
    J Mol Biol; 2008 Mar; 377(1):83-90. PubMed ID: 18241889
    [TBL] [Abstract][Full Text] [Related]  

  • 15. SecB-independent export of Escherichia coli ribose-binding protein (RBP): some comparisons with export of maltose-binding protein (MBP) and studies with RBP-MBP hybrid proteins.
    Collier DN; Strobel SM; Bassford PJ
    J Bacteriol; 1990 Dec; 172(12):6875-84. PubMed ID: 2254262
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Reversible formation of on-pathway macroscopic aggregates during the folding of maltose binding protein.
    Ganesh C; Zaidi FN; Udgaonkar JB; Varadarajan R
    Protein Sci; 2001 Aug; 10(8):1635-44. PubMed ID: 11468360
    [TBL] [Abstract][Full Text] [Related]  

  • 17. The structure of SecB/OmpA as visualized by electron microscopy: The mature region of the precursor protein binds asymmetrically to SecB.
    Tang Y; Pan X; Tai PC; Sui SF
    Biochem Biophys Res Commun; 2010 Mar; 393(4):698-702. PubMed ID: 20170640
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export.
    Hardy SJ; Randall LL
    Philos Trans R Soc Lond B Biol Sci; 1993 Mar; 339(1289):343-52; discussion 352-4. PubMed ID: 8098539
    [TBL] [Abstract][Full Text] [Related]  

  • 19. High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein.
    Watanabe M; Blobel G
    Proc Natl Acad Sci U S A; 1995 Oct; 92(22):10133-6. PubMed ID: 7479740
    [TBL] [Abstract][Full Text] [Related]  

  • 20. SecB is a bona fide generalized chaperone in Escherichia coli.
    Ullers RS; Luirink J; Harms N; Schwager F; Georgopoulos C; Genevaux P
    Proc Natl Acad Sci U S A; 2004 May; 101(20):7583-8. PubMed ID: 15128935
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 14.