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 *

534 related articles for article (PubMed ID: 16427651)

  • 1. 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]  

  • 2. 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]  

  • 3. 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]  

  • 4. 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]  

  • 5. From minichaperone to GroEL 2: importance of avidity of the multisite ring structure.
    Chatellier J; Hill F; Fersht AR
    J Mol Biol; 2000 Dec; 304(5):883-96. PubMed ID: 11124034
    [TBL] [Abstract][Full Text] [Related]  

  • 6. 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]  

  • 7. 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]  

  • 8. 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]  

  • 9. Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring.
    van Duijn E; Simmons DA; van den Heuvel RH; Bakkes PJ; van Heerikhuizen H; Heeren RM; Robinson CV; van der Vies SM; Heck AJ
    J Am Chem Soc; 2006 Apr; 128(14):4694-702. PubMed ID: 16594706
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Productive folding of a tethered protein in the chaperonin GroEL-GroES cage.
    Motojima F; Yoshida M
    Biochem Biophys Res Commun; 2015 Oct; 466(1):72-5. PubMed ID: 26325470
    [TBL] [Abstract][Full Text] [Related]  

  • 11. 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]  

  • 12. Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli.
    Gupta P; Aggarwal N; Batra P; Mishra S; Chaudhuri TK
    Int J Biochem Cell Biol; 2006; 38(11):1975-85. PubMed ID: 16822698
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level.
    Gupta AJ; Haldar S; Miličić G; Hartl FU; Hayer-Hartl M
    J Mol Biol; 2014 Jul; 426(15):2739-54. PubMed ID: 24816391
    [TBL] [Abstract][Full Text] [Related]  

  • 14. 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]  

  • 15. Multiple structural transitions of the GroEL subunit are sensitive to intermolecular interactions with cochaperonin and refolding polypeptide.
    Yoshimi T; Hongo K; Mizobata T; Kawata Y
    J Biochem; 2006 Mar; 139(3):407-19. PubMed ID: 16567406
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Characterisation of mutations in GroES that allow GroEL to function as a single ring.
    Liu H; Kovács E; Lund PA
    FEBS Lett; 2009 Jul; 583(14):2365-71. PubMed ID: 19545569
    [TBL] [Abstract][Full Text] [Related]  

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

  • 18. 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]  

  • 19. Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES.
    Makio T; Arai M; Kuwajima K
    J Mol Biol; 1999 Oct; 293(1):125-37. PubMed ID: 10512721
    [TBL] [Abstract][Full Text] [Related]  

  • 20. 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]  

    [Next]    [New Search]
    of 27.