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Journal Abstract Search

182 related items for PubMed ID: 7776368

  • 1. The origins and consequences of asymmetry in the chaperonin reaction cycle.
    Burston SG, Ranson NA, Clarke AR.
    J Mol Biol; 1995 May 26; 249(1):138-52. PubMed ID: 7776368
    [Abstract] [Full Text] [Related]

  • 2. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings.
    Kad NM, Ranson NA, Cliff MJ, Clarke AR.
    J Mol Biol; 1998 Apr 24; 278(1):267-78. PubMed ID: 9571049
    [Abstract] [Full Text] [Related]

  • 3. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.
    Jackson GS, Staniforth RA, Halsall DJ, Atkinson T, Holbrook JJ, Clarke AR, Burston SG.
    Biochemistry; 1993 Mar 16; 32(10):2554-63. PubMed ID: 8095403
    [Abstract] [Full Text] [Related]

  • 4. Functional consequences of single:double ring transitions in chaperonins: life in the cold.
    Ferrer M, Lünsdorf H, Chernikova TN, Yakimov M, Timmis KN, Golyshin PN.
    Mol Microbiol; 2004 Jul 16; 53(1):167-82. PubMed ID: 15225312
    [Abstract] [Full Text] [Related]

  • 5. Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions.
    Behlke J, Ristau O, Schönfeld HJ.
    Biochemistry; 1997 Apr 29; 36(17):5149-56. PubMed ID: 9136876
    [Abstract] [Full Text] [Related]

  • 6. GroEL/GroES: structure and function of a two-stroke folding machine.
    Xu Z, Sigler PB.
    J Struct Biol; 1998 Dec 15; 124(2-3):129-41. PubMed ID: 10049801
    [Abstract] [Full Text] [Related]

  • 7. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.
    Rye HS, Burston SG, Fenton WA, Beechem JM, Xu Z, Sigler PB, Horwich AL.
    Nature; 1997 Aug 21; 388(6644):792-8. PubMed ID: 9285593
    [Abstract] [Full Text] [Related]

  • 8. Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant.
    Guidry JJ, Moczygemba CK, Steede NK, Landry SJ, Wittung-Stafshede P.
    Protein Sci; 2000 Nov 21; 9(11):2109-17. PubMed ID: 11152122
    [Abstract] [Full Text] [Related]

  • 9. Hydrolysable ATP is a requirement for the correct interaction of molecular chaperonins cpn60 and cpn10.
    Walters C, Errington N, Rowe AJ, Harding SE.
    Biochem J; 2002 Jun 15; 364(Pt 3):849-55. PubMed ID: 12049650
    [Abstract] [Full Text] [Related]

  • 10. Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10.
    Staniforth RA, Burston SG, Atkinson T, Clarke AR.
    Biochem J; 1994 Jun 15; 300 ( Pt 3)(Pt 3):651-8. PubMed ID: 7912068
    [Abstract] [Full Text] [Related]

  • 11. The chaperonin cycle and protein folding.
    Lund P.
    Bioessays; 1994 Apr 15; 16(4):229-31. PubMed ID: 7913317
    [Abstract] [Full Text] [Related]

  • 12. Differential effects of co-chaperonin homologs on cpn60 oligomers.
    Bonshtien AL, Parnas A, Sharkia R, Niv A, Mizrahi I, Azem A, Weiss C.
    Cell Stress Chaperones; 2009 Sep 15; 14(5):509-19. PubMed ID: 19224397
    [Abstract] [Full Text] [Related]

  • 13. The second step of ATP binding to DnaK induces peptide release.
    Theyssen H, Schuster HP, Packschies L, Bukau B, Reinstein J.
    J Mol Biol; 1996 Nov 15; 263(5):657-70. PubMed ID: 8947566
    [Abstract] [Full Text] [Related]

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  • 15. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.
    Cliff MJ, Kad NM, Hay N, Lund PA, Webb MR, Burston SG, Clarke AR.
    J Mol Biol; 1999 Oct 29; 293(3):667-84. PubMed ID: 10543958
    [Abstract] [Full Text] [Related]

  • 16. Conformational changes in the GroEL oligomer during the functional cycle.
    Llorca O, Marco S, Carrascosa JL, Valpuesta JM.
    J Struct Biol; 1997 Feb 29; 118(1):31-42. PubMed ID: 9087913
    [Abstract] [Full Text] [Related]

  • 17.
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  • 18. Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES.
    Makio T, Arai M, Kuwajima K.
    J Mol Biol; 1999 Oct 15; 293(1):125-37. PubMed ID: 10512721
    [Abstract] [Full Text] [Related]

  • 19. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.
    Xu Z, Horwich AL, Sigler PB.
    Nature; 1997 Aug 21; 388(6644):741-50. PubMed ID: 9285585
    [Abstract] [Full Text] [Related]

  • 20. A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation.
    Sewell BT, Best RB, Chen S, Roseman AM, Farr GW, Horwich AL, Saibil HR.
    Nat Struct Mol Biol; 2004 Nov 21; 11(11):1128-33. PubMed ID: 15475965
    [Abstract] [Full Text] [Related]

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