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Journal Abstract Search

472 related items for PubMed ID: 7638601

  • 1. Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.
    Hayer-Hartl MK, Martin J, Hartl FU.
    Science; 1995 Aug 11; 269(5225):836-41. PubMed ID: 7638601
    [Abstract] [Full Text] [Related]

  • 2. The role of ATP hydrolysis in the function of the chaperonin GroEL: dynamic complex formation with GroES.
    Kawata Y, Hongo K, Nosaka K, Furutsu Y, Mizobata T, Nagai J.
    FEBS Lett; 1995 Aug 07; 369(2-3):283-6. PubMed ID: 7649273
    [Abstract] [Full Text] [Related]

  • 3. Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.
    Engel A, Hayer-Hartl MK, Goldie KN, Pfeifer G, Hegerl R, Müller S, da Silva AC, Baumeister W, Hartl FU.
    Science; 1995 Aug 11; 269(5225):832-6. PubMed ID: 7638600
    [Abstract] [Full Text] [Related]

  • 4. Triggering protein folding within the GroEL-GroES complex.
    Madan D, Lin Z, Rye HS.
    J Biol Chem; 2008 Nov 14; 283(46):32003-13. PubMed ID: 18782766
    [Abstract] [Full Text] [Related]

  • 5. 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]

  • 6. 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]

  • 7. The affinity of the GroEL/GroES complex for peptides under conditions of protein folding.
    Preuss M, Miller AD.
    FEBS Lett; 2000 Jan 21; 466(1):75-9. PubMed ID: 10648816
    [Abstract] [Full Text] [Related]

  • 8. Stability of the asymmetric Escherichia coli chaperonin complex. Guanidine chloride causes rapid dissociation.
    Todd MJ, Lorimer GH.
    J Biol Chem; 1995 Mar 10; 270(10):5388-94. PubMed ID: 7890652
    [Abstract] [Full Text] [Related]

  • 9. Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.
    Illingworth M, Salisbury J, Li W, Lin D, Chen L.
    Biochem Biophys Res Commun; 2015 Oct 09; 466(1):15-20. PubMed ID: 26271593
    [Abstract] [Full Text] [Related]

  • 10. Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES Complexes.
    Haldar S, Gupta AJ, Yan X, Miličić G, Hartl FU, Hayer-Hartl M.
    J Mol Biol; 2015 Jun 19; 427(12):2244-55. PubMed ID: 25912285
    [Abstract] [Full Text] [Related]

  • 11. BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers.
    Taguchi H, Tsukuda K, Motojima F, Koike-Takeshita A, Yoshida M.
    J Biol Chem; 2004 Oct 29; 279(44):45737-43. PubMed ID: 15347650
    [Abstract] [Full Text] [Related]

  • 12. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings.
    Rye HS, Roseman AM, Chen S, Furtak K, Fenton WA, Saibil HR, Horwich AL.
    Cell; 1999 Apr 30; 97(3):325-38. PubMed ID: 10319813
    [Abstract] [Full Text] [Related]

  • 13. 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]

  • 14. Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.
    Taguchi H.
    J Mol Biol; 2015 Sep 11; 427(18):2912-8. PubMed ID: 25900372
    [Abstract] [Full Text] [Related]

  • 15. ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle.
    Tyagi NK, Fenton WA, Horwich AL.
    FEBS Lett; 2010 Mar 05; 584(5):951-3. PubMed ID: 20083109
    [Abstract] [Full Text] [Related]

  • 16. GroEL and the GroEL-GroES Complex.
    Ishii N.
    Subcell Biochem; 2017 Mar 05; 83():483-504. PubMed ID: 28271487
    [Abstract] [Full Text] [Related]

  • 17. GroEL mediates protein folding with a two successive timer mechanism.
    Ueno T, Taguchi H, Tadakuma H, Yoshida M, Funatsu T.
    Mol Cell; 2004 May 21; 14(4):423-34. PubMed ID: 15149592
    [Abstract] [Full Text] [Related]

  • 18. TEM and STEM-EDS evaluation of metal nanoparticle encapsulation in GroEL/GroES complexes according to the reaction mechanism of chaperonin.
    Yoda H, Koike-Takeshita A.
    Microscopy (Oxf); 2021 Jun 06; 70(3):289-296. PubMed ID: 33173948
    [Abstract] [Full Text] [Related]

  • 19. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.
    Weissman JS, Rye HS, Fenton WA, Beechem JM, Horwich AL.
    Cell; 1996 Feb 09; 84(3):481-90. PubMed ID: 8608602
    [Abstract] [Full Text] [Related]

  • 20. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
    Martin J, Mayhew M, Langer T, Hartl FU.
    Nature; 1993 Nov 18; 366(6452):228-33. PubMed ID: 7901770
    [Abstract] [Full Text] [Related]

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