BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

305 related articles for article (PubMed ID: 24022487)

  • 1. Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.
    Lin Z; Puchalla J; Shoup D; Rye HS
    J Biol Chem; 2013 Oct; 288(43):30944-55. PubMed ID: 24022487
    [TBL] [Abstract][Full Text] [Related]  

  • 2. 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]  

  • 3. The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate protein.
    Weaver J; Rye HS
    J Biol Chem; 2014 Aug; 289(33):23219-23232. PubMed ID: 24970895
    [TBL] [Abstract][Full Text] [Related]  

  • 4. 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]  

  • 5. Expansion and compression of a protein folding intermediate by GroEL.
    Lin Z; Rye HS
    Mol Cell; 2004 Oct; 16(1):23-34. PubMed ID: 15469819
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Chaperones GroEL/GroES accelerate the refolding of a multidomain protein through modulating on-pathway intermediates.
    Dahiya V; Chaudhuri TK
    J Biol Chem; 2014 Jan; 289(1):286-98. PubMed ID: 24247249
    [TBL] [Abstract][Full Text] [Related]  

  • 7. 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]  

  • 8. Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant.
    Koike-Takeshita A; Yoshida M; Taguchi H
    J Biol Chem; 2008 Aug; 283(35):23774-81. PubMed ID: 18567584
    [TBL] [Abstract][Full Text] [Related]  

  • 9. A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin.
    Natesh R; Clare DK; Farr GW; Horwich AL; Saibil HR
    Int J Biol Macromol; 2018 Oct; 118(Pt A):671-675. PubMed ID: 29959019
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Molecular chaperone GroEL/ES: unfolding and refolding processes.
    Ryabova NA; Marchenkov VV; Marchenkova SY; Kotova NV; Semisotnov GV
    Biochemistry (Mosc); 2013 Dec; 78(13):1405-14. PubMed ID: 24490731
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Asymmetric functional interaction between chaperonin and its plastidic cofactors.
    Guo P; Jiang S; Bai C; Zhang W; Zhao Q; Liu C
    FEBS J; 2015 Oct; 282(20):3959-70. PubMed ID: 26237751
    [TBL] [Abstract][Full Text] [Related]  

  • 12. 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]  

  • 13. Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.
    Sameshima T; Ueno T; Iizuka R; Ishii N; Terada N; Okabe K; Funatsu T
    J Biol Chem; 2008 Aug; 283(35):23765-73. PubMed ID: 18567585
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins.
    Machida K; Fujiwara R; Tanaka T; Sakane I; Hongo K; Mizobata T; Kawata Y
    Biochim Biophys Acta; 2009 Sep; 1794(9):1344-54. PubMed ID: 19130907
    [TBL] [Abstract][Full Text] [Related]  

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

  • 16. Local energetic frustration affects the dependence of green fluorescent protein folding on the chaperonin GroEL.
    Bandyopadhyay B; Goldenzweig A; Unger T; Adato O; Fleishman SJ; Unger R; Horovitz A
    J Biol Chem; 2017 Dec; 292(50):20583-20591. PubMed ID: 29066625
    [TBL] [Abstract][Full Text] [Related]  

  • 17. GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state.
    Tyagi NK; Fenton WA; Horwich AL
    Proc Natl Acad Sci U S A; 2009 Dec; 106(48):20264-9. PubMed ID: 19915138
    [TBL] [Abstract][Full Text] [Related]  

  • 18. GroEL stimulates protein folding through forced unfolding.
    Lin Z; Madan D; Rye HS
    Nat Struct Mol Biol; 2008 Mar; 15(3):303-11. PubMed ID: 18311152
    [TBL] [Abstract][Full Text] [Related]  

  • 19. 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]  

  • 20. The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding.
    Hayer-Hartl M; Bracher A; Hartl FU
    Trends Biochem Sci; 2016 Jan; 41(1):62-76. PubMed ID: 26422689
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 16.