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154 related items for PubMed ID: 9087913

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

  • 4. 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]

  • 5. Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL14(groES7)2 is favored by an asymmetric distribution of nucleotides.
    Gorovits BM, Ybarra J, Seale JW, Horowitz PM.
    J Biol Chem; 1997 Oct 24; 272(43):26999-7004. PubMed ID: 9341138
    [Abstract] [Full Text] [Related]

  • 6. A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL.
    Poso D, Clarke AR, Burston SG.
    J Mol Biol; 2004 May 14; 338(5):969-77. PubMed ID: 15111060
    [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. Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy.
    Roseman AM, Ranson NA, Gowen B, Fuller SD, Saibil HR.
    J Struct Biol; 2001 Aug 21; 135(2):115-25. PubMed ID: 11580261
    [Abstract] [Full Text] [Related]

  • 9. Nucleotide-induced transition of GroEL from the high-affinity to the low-affinity state for a target protein: effects of ATP and ADP on the GroEL-affected refolding of alpha-lactalbumin.
    Makio T, Takasu-Ishikawa E, Kuwajima K.
    J Mol Biol; 2001 Sep 21; 312(3):555-67. PubMed ID: 11563916
    [Abstract] [Full Text] [Related]

  • 10. Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP.
    Inobe T, Makio T, Takasu-Ishikawa E, Terada TP, Kuwajima K.
    Biochim Biophys Acta; 2001 Feb 09; 1545(1-2):160-73. PubMed ID: 11342042
    [Abstract] [Full Text] [Related]

  • 11. 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]

  • 12. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.
    Hayer-Hartl MK, Weber F, Hartl FU.
    EMBO J; 1996 Nov 15; 15(22):6111-21. PubMed ID: 8947033
    [Abstract] [Full Text] [Related]

  • 13. 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]

  • 14. Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.
    Motojima F, Chaudhry C, Fenton WA, Farr GW, Horwich AL.
    Proc Natl Acad Sci U S A; 2004 Oct 19; 101(42):15005-12. PubMed ID: 15479763
    [Abstract] [Full Text] [Related]

  • 15. Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL.
    Yokokawa M, Wada C, Ando T, Sakai N, Yagi A, Yoshimura SH, Takeyasu K.
    EMBO J; 2006 Oct 04; 25(19):4567-76. PubMed ID: 16977315
    [Abstract] [Full Text] [Related]

  • 16. Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states.
    Chaudhry C, Horwich AL, Brunger AT, Adams PD.
    J Mol Biol; 2004 Sep 03; 342(1):229-45. PubMed ID: 15313620
    [Abstract] [Full Text] [Related]

  • 17. Effects of the inter-ring communication in GroEL structural and functional asymmetry.
    Llorca O, Pérez-Pérez J, Carrascosa JL, Galán A, Muga A, Valpuesta JM.
    J Biol Chem; 1997 Dec 26; 272(52):32925-32. PubMed ID: 9407071
    [Abstract] [Full Text] [Related]

  • 18. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.
    Roseman AM, Chen S, White H, Braig K, Saibil HR.
    Cell; 1996 Oct 18; 87(2):241-51. PubMed ID: 8861908
    [Abstract] [Full Text] [Related]

  • 19. Allostery wiring diagrams in the transitions that drive the GroEL reaction cycle.
    Tehver R, Chen J, Thirumalai D.
    J Mol Biol; 2009 Mar 27; 387(2):390-406. PubMed ID: 19121324
    [Abstract] [Full Text] [Related]

  • 20. Allosteric control by ATP of non-folded protein binding to GroEL.
    Yifrach O, Horovitz A.
    J Mol Biol; 1996 Jan 26; 255(3):356-61. PubMed ID: 8568880
    [Abstract] [Full Text] [Related]

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