BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

469 related articles for article (PubMed ID: 7638601)

  • 1. Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.
    Hayer-Hartl MK; Martin J; Hartl FU
    Science; 1995 Aug; 269(5225):836-41. PubMed ID: 7638601
    [TBL] [Abstract][Full Text] [Related]  

  • 2. The role of ATP hydrolysis in the function of the chaperonin GroEL: dynamic complex formation with GroES.
    Kawata Y; Hongo K; Nosaka K; Furutsu Y; Mizobata T; Nagai J
    FEBS Lett; 1995 Aug; 369(2-3):283-6. PubMed ID: 7649273
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.
    Engel A; Hayer-Hartl MK; Goldie KN; Pfeifer G; Hegerl R; Müller S; da Silva AC; Baumeister W; Hartl FU
    Science; 1995 Aug; 269(5225):832-6. PubMed ID: 7638600
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Triggering protein folding within the GroEL-GroES complex.
    Madan D; Lin Z; Rye HS
    J Biol Chem; 2008 Nov; 283(46):32003-13. PubMed ID: 18782766
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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]  

  • 6. 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]  

  • 7. The affinity of the GroEL/GroES complex for peptides under conditions of protein folding.
    Preuss M; Miller AD
    FEBS Lett; 2000 Jan; 466(1):75-9. PubMed ID: 10648816
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Stability of the asymmetric Escherichia coli chaperonin complex. Guanidine chloride causes rapid dissociation.
    Todd MJ; Lorimer GH
    J Biol Chem; 1995 Mar; 270(10):5388-94. PubMed ID: 7890652
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.
    Illingworth M; Salisbury J; Li W; Lin D; Chen L
    Biochem Biophys Res Commun; 2015 Oct; 466(1):15-20. PubMed ID: 26271593
    [TBL] [Abstract][Full Text] [Related]  

  • 10. 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]  

  • 11. BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers.
    Taguchi H; Tsukuda K; Motojima F; Koike-Takeshita A; Yoshida M
    J Biol Chem; 2004 Oct; 279(44):45737-43. PubMed ID: 15347650
    [TBL] [Abstract][Full Text] [Related]  

  • 12. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings.
    Rye HS; Roseman AM; Chen S; Furtak K; Fenton WA; Saibil HR; Horwich AL
    Cell; 1999 Apr; 97(3):325-38. PubMed ID: 10319813
    [TBL] [Abstract][Full Text] [Related]  

  • 13. 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]  

  • 14. Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.
    Taguchi H
    J Mol Biol; 2015 Sep; 427(18):2912-8. PubMed ID: 25900372
    [TBL] [Abstract][Full Text] [Related]  

  • 15. ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle.
    Tyagi NK; Fenton WA; Horwich AL
    FEBS Lett; 2010 Mar; 584(5):951-3. PubMed ID: 20083109
    [TBL] [Abstract][Full Text] [Related]  

  • 16. GroEL and the GroEL-GroES Complex.
    Ishii N
    Subcell Biochem; 2017; 83():483-504. PubMed ID: 28271487
    [TBL] [Abstract][Full Text] [Related]  

  • 17. GroEL mediates protein folding with a two successive timer mechanism.
    Ueno T; Taguchi H; Tadakuma H; Yoshida M; Funatsu T
    Mol Cell; 2004 May; 14(4):423-34. PubMed ID: 15149592
    [TBL] [Abstract][Full Text] [Related]  

  • 18. TEM and STEM-EDS evaluation of metal nanoparticle encapsulation in GroEL/GroES complexes according to the reaction mechanism of chaperonin.
    Yoda H; Koike-Takeshita A
    Microscopy (Oxf); 2021 Jun; 70(3):289-296. PubMed ID: 33173948
    [TBL] [Abstract][Full Text] [Related]  

  • 19. 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]  

  • 20. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
    Martin J; Mayhew M; Langer T; Hartl FU
    Nature; 1993 Nov; 366(6452):228-33. PubMed ID: 7901770
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 24.