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Journal Abstract Search

472 related items for PubMed ID: 10384959

  • 1. On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein folding.
    Hayer-Hartl MK, Ewalt KL, Hartl FU.
    Biol Chem; 1999 May; 380(5):531-40. PubMed ID: 10384959
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  • 4. Protein folding assisted by the GroEL/GroES chaperonin system.
    Martin J.
    Biochemistry (Mosc); 1998 Apr; 63(4):374-81. PubMed ID: 9556520
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  • 5. GroEL-mediated protein folding.
    Fenton WA, Horwich AL.
    Protein Sci; 1997 Apr; 6(4):743-60. PubMed ID: 9098884
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  • 6. Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction.
    Ranson NA, Burston SG, Clarke AR.
    J Mol Biol; 1997 Mar 07; 266(4):656-64. PubMed ID: 9102459
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  • 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
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  • 10. Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes.
    Farr GW, Fenton WA, Chaudhuri TK, Clare DK, Saibil HR, Horwich AL.
    EMBO J; 2003 Jul 01; 22(13):3220-30. PubMed ID: 12839985
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  • 17. 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 01; 20(6):903-10. PubMed ID: 17242865
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  • 19. Role of chaperonins in protein folding. A new model of the GroEL/GroES complex architecture.
    Basharov MA.
    Biochemistry (Mosc); 1997 Apr 01; 62(4):416-24. PubMed ID: 9312423
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