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Journal Abstract Search

392 related items for PubMed ID: 9571049

  • 1. 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
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  • 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
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  • 4. 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
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  • 5. 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
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  • 7. 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
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  • 8. 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
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  • 9. 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
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  • 10. 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
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  • 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
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  • 14. 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
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  • 15. 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
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  • 20. The lower hydrolysis of ATP by the stress protein GroEL is a major factor responsible for the diminished chaperonin activity at low temperature.
    Mendoza JA, Dulin P, Warren T.
    Cryobiology; 2000 Dec 19; 41(4):319-23. PubMed ID: 11222029
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