BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

320 related articles for article (PubMed ID: 9312423)

  • 1. 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]  

  • 2. 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]  

  • 3. 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]  

  • 4. 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]  

  • 5. 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; 36(17):5149-56. PubMed ID: 9136876
    [TBL] [Abstract][Full Text] [Related]  

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

  • 7. Prediction of the structure of GroES and its interaction with GroEL.
    Valencia A; Hubbard TJ; Muga A; Bañuelos S; Llorca O; Carrascosa JL; Valpuesta JM
    Proteins; 1995 Jul; 22(3):199-209. PubMed ID: 7479694
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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]  

  • 9. Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding.
    Motojima F; Makio T; Aoki K; Makino Y; Kuwajima K; Yoshida M
    Biochem Biophys Res Commun; 2000 Jan; 267(3):842-9. PubMed ID: 10673379
    [TBL] [Abstract][Full Text] [Related]  

  • 10. 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
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Reversible oligomerization and denaturation of the chaperonin GroES.
    Seale JW; Gorovits BM; Ybarra J; Horowitz PM
    Biochemistry; 1996 Apr; 35(13):4079-83. PubMed ID: 8672442
    [TBL] [Abstract][Full Text] [Related]  

  • 12. 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]  

  • 13. 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]  

  • 14. Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.
    Tang YC; Chang HC; Roeben A; Wischnewski D; Wischnewski N; Kerner MJ; Hartl FU; Hayer-Hartl M
    Cell; 2006 Jun; 125(5):903-14. PubMed ID: 16751100
    [TBL] [Abstract][Full Text] [Related]  

  • 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; 427(12):2244-55. PubMed ID: 25912285
    [TBL] [Abstract][Full Text] [Related]  

  • 16. The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding.
    Weber F; Keppel F; Georgopoulos C; Hayer-Hartl MK; Hartl FU
    Nat Struct Biol; 1998 Nov; 5(11):977-85. PubMed ID: 9808043
    [TBL] [Abstract][Full Text] [Related]  

  • 17. 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]  

  • 18. The mechanism of GroEL/GroES folding/refolding of protein substrates revisited.
    Jones H; Preuss M; Wright M; Miller AD
    Org Biomol Chem; 2006 Apr; 4(7):1223-35. PubMed ID: 16557310
    [TBL] [Abstract][Full Text] [Related]  

  • 19. 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]  

  • 20. 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]  

    [Next]    [New Search]
    of 16.