BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

286 related articles for article (PubMed ID: 16683761)

  • 21. Monitoring protein conformation along the pathway of chaperonin-assisted folding.
    Sharma S; Chakraborty K; Müller BK; Astola N; Tang YC; Lamb DC; Hayer-Hartl M; Hartl FU
    Cell; 2008 Apr; 133(1):142-53. PubMed ID: 18394994
    [TBL] [Abstract][Full Text] [Related]  

  • 22. Translocation boost protein-folding efficiency of double-barreled chaperonins.
    Coluzza I; van der Vies SM; Frenkel D
    Biophys J; 2006 May; 90(10):3375-81. PubMed ID: 16473898
    [TBL] [Abstract][Full Text] [Related]  

  • 23. Protein folding. Folding with a two-stroke motor.
    Lorimer G
    Nature; 1997 Aug; 388(6644):720-1, 723. PubMed ID: 9285577
    [No Abstract]   [Full Text] [Related]  

  • 24. Characterisation of mutations in GroES that allow GroEL to function as a single ring.
    Liu H; Kovács E; Lund PA
    FEBS Lett; 2009 Jul; 583(14):2365-71. PubMed ID: 19545569
    [TBL] [Abstract][Full Text] [Related]  

  • 25. How chaperones tell wrong from right.
    Saibil HR
    Nat Struct Biol; 1994 Dec; 1(12):838-42. PubMed ID: 7773768
    [No Abstract]   [Full Text] [Related]  

  • 26. 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]  

  • 27. Identification of substrate binding site of GroEL minichaperone in solution.
    Tanaka N; Fersht AR
    J Mol Biol; 1999 Sep; 292(1):173-80. PubMed ID: 10493866
    [TBL] [Abstract][Full Text] [Related]  

  • 28. Principles of chaperone-mediated protein folding.
    Hartl FU
    Philos Trans R Soc Lond B Biol Sci; 1995 Apr; 348(1323):107-12. PubMed ID: 7770479
    [TBL] [Abstract][Full Text] [Related]  

  • 29. Effects of divalent cations on encapsulation and release in the GroEL-assisted folding.
    Okuda H; Sakuhana C; Yamamoto R; Kawai R; Mizukami Y; Matsuda K
    Biometals; 2007 Dec; 20(6):903-10. PubMed ID: 17242865
    [TBL] [Abstract][Full Text] [Related]  

  • 30. [Reactivation of denatured lysozyme with immobilized molecular chaperones GroE].
    Dong XY; Yang H; Gan YR; Bai S; Sun Y
    Sheng Wu Gong Cheng Xue Bao; 2000 Mar; 16(2):169-72. PubMed ID: 10976320
    [TBL] [Abstract][Full Text] [Related]  

  • 31. Global minimization of an off-lattice potential energy function using a chaperone-based refolding method.
    Gorse D
    Biopolymers; 2001 Nov; 59(6):411-26. PubMed ID: 11598876
    [TBL] [Abstract][Full Text] [Related]  

  • 32. Unfolded DapA forms aggregates when diluted into free solution, confounding comparison with folding by the GroEL/GroES chaperonin system.
    Ambrose A; Fenton W; Mason DJ; Chapman E; Horwich AL
    FEBS Lett; 2015 Feb; 589(4):497-499. PubMed ID: 25601566
    [TBL] [Abstract][Full Text] [Related]  

  • 33. NMR analysis of a 900K GroEL GroES complex.
    Fiaux J; Bertelsen EB; Horwich AL; Wüthrich K
    Nature; 2002 Jul; 418(6894):207-11. PubMed ID: 12110894
    [TBL] [Abstract][Full Text] [Related]  

  • 34. GroEL-mediated protein folding: making the impossible, possible.
    Lin Z; Rye HS
    Crit Rev Biochem Mol Biol; 2006; 41(4):211-39. PubMed ID: 16849107
    [TBL] [Abstract][Full Text] [Related]  

  • 35. Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy.
    Hofmann H; Hillger F; Delley C; Hoffmann A; Pfeil SH; Nettels D; Lipman EA; Schuler B
    Biophys J; 2014 Dec; 107(12):2891-2902. PubMed ID: 25517154
    [TBL] [Abstract][Full Text] [Related]  

  • 36. An expanded conformation of single-ring GroEL-GroES complex encapsulates an 86 kDa substrate.
    Chen DH; Song JL; Chuang DT; Chiu W; Ludtke SJ
    Structure; 2006 Nov; 14(11):1711-22. PubMed ID: 17098196
    [TBL] [Abstract][Full Text] [Related]  

  • 37. Domain-specific chaperone-induced expansion is required for beta-actin folding: a comparison of beta-actin conformations upon interactions with GroEL and tail-less complex polypeptide 1 ring complex (TRiC).
    Villebeck L; Moparthi SB; Lindgren M; Hammarström P; Jonsson BH
    Biochemistry; 2007 Nov; 46(44):12639-47. PubMed ID: 17939680
    [TBL] [Abstract][Full Text] [Related]  

  • 38. Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins.
    Saibil H
    Curr Opin Struct Biol; 2000 Apr; 10(2):251-8. PubMed ID: 10753820
    [TBL] [Abstract][Full Text] [Related]  

  • 39. Co-chaperonin GroES as a modulator of proteasomal activity.
    Cuccioloni M; Montecchia F; Amici M; Mozzicafreddo M; Eleuteri AM; Angeletti M
    J Mol Recognit; 2009; 22(1):46-54. PubMed ID: 19006106
    [TBL] [Abstract][Full Text] [Related]  

  • 40. Allostery wiring diagrams in the transitions that drive the GroEL reaction cycle.
    Tehver R; Chen J; Thirumalai D
    J Mol Biol; 2009 Mar; 387(2):390-406. PubMed ID: 19121324
    [TBL] [Abstract][Full Text] [Related]  

    [Previous]   [Next]    [New Search]
    of 15.