These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

199 related articles for article (PubMed ID: 8779722)

  • 1. Release of both native and non-native proteins from a cis-only GroEL ternary complex.
    Burston SG; Weissman JS; Farr GW; Fenton WA; Horwich AL
    Nature; 1996 Sep; 383(6595):96-9. PubMed ID: 8779722
    [TBL] [Abstract][Full Text] [Related]  

  • 2. 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; 388(6644):792-8. PubMed ID: 9285593
    [TBL] [Abstract][Full Text] [Related]  

  • 3. GroEL-mediated protein folding.
    Fenton WA; Horwich AL
    Protein Sci; 1997 Apr; 6(4):743-60. PubMed ID: 9098884
    [TBL] [Abstract][Full Text] [Related]  

  • 4. 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; 22(13):3220-30. PubMed ID: 12839985
    [TBL] [Abstract][Full Text] [Related]  

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

  • 6. GroEL walks the fine line: the subtle balance of substrate and co-chaperonin binding by GroEL. A combinatorial investigation by design, selection and screening.
    Kawe M; Plückthun A
    J Mol Biol; 2006 Mar; 357(2):411-26. PubMed ID: 16427651
    [TBL] [Abstract][Full Text] [Related]  

  • 7. 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; 84(3):481-90. PubMed ID: 8608602
    [TBL] [Abstract][Full Text] [Related]  

  • 8. GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle.
    Miyazaki T; Yoshimi T; Furutsu Y; Hongo K; Mizobata T; Kanemori M; Kawata Y
    J Biol Chem; 2002 Dec; 277(52):50621-8. PubMed ID: 12377767
    [TBL] [Abstract][Full Text] [Related]  

  • 9. 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; 41(4):319-23. PubMed ID: 11222029
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Protein folding assisted by the GroEL/GroES chaperonin system.
    Martin J
    Biochemistry (Mosc); 1998 Apr; 63(4):374-81. PubMed ID: 9556520
    [TBL] [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; 388(6644):741-50. PubMed ID: 9285585
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Structure and function in GroEL-mediated protein folding.
    Sigler PB; Xu Z; Rye HS; Burston SG; Fenton WA; Horwich AL
    Annu Rev Biochem; 1998; 67():581-608. PubMed ID: 9759498
    [TBL] [Abstract][Full Text] [Related]  

  • 13. 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(22):6111-21. PubMed ID: 8947033
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity.
    Shimamura T; Koike-Takeshita A; Yokoyama K; Masui R; Murai N; Yoshida M; Taguchi H; Iwata S
    Structure; 2004 Aug; 12(8):1471-80. PubMed ID: 15296740
    [TBL] [Abstract][Full Text] [Related]  

  • 15. 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; 278(1):267-78. PubMed ID: 9571049
    [TBL] [Abstract][Full Text] [Related]  

  • 16. 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; 101(42):15005-12. PubMed ID: 15479763
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity.
    Betancourt MR; Thirumalai D
    J Mol Biol; 1999 Apr; 287(3):627-44. PubMed ID: 10092464
    [TBL] [Abstract][Full Text] [Related]  

  • 18. The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form.
    von Ahsen O; Tropschug M; Pfanner N; Rassow J
    EMBO J; 1997 Aug; 16(15):4568-78. PubMed ID: 9303301
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding.
    Smith KE; Fisher MT
    J Biol Chem; 1995 Sep; 270(37):21517-23. PubMed ID: 7665563
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Role of chaperonins in protein folding. A new model of the GroEL/GroES complex architecture.
    Basharov MA
    Biochemistry (Mosc); 1997 Apr; 62(4):416-24. PubMed ID: 9312423
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 10.