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 *

260 related articles for article (PubMed ID: 35107280)

  • 1. Temperature Regulates Stability, Ligand Binding (Mg
    Walker TE; Shirzadeh M; Sun HM; McCabe JW; Roth A; Moghadamchargari Z; Clemmer DE; Laganowsky A; Rye H; Russell DH
    J Am Chem Soc; 2022 Feb; 144(6):2667-2678. PubMed ID: 35107280
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL14(groES7)2 is favored by an asymmetric distribution of nucleotides.
    Gorovits BM; Ybarra J; Seale JW; Horowitz PM
    J Biol Chem; 1997 Oct; 272(43):26999-7004. PubMed ID: 9341138
    [TBL] [Abstract][Full Text] [Related]  

  • 3. 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]  

  • 4. 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]  

  • 5. 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]  

  • 6. 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]  

  • 7. 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]  

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

  • 9. 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]  

  • 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. 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]  

  • 12. 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]  

  • 13. On the distribution of ligands within the asymmetric chaperonin complex, GroEL14.ADP7.GroES7.
    Girshovich AS; Bochkareva ES; Todd MJ; Lorimer GH
    FEBS Lett; 1995 Jun; 366(1):17-20. PubMed ID: 7789507
    [TBL] [Abstract][Full Text] [Related]  

  • 14. The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.
    Azem A; Diamant S; Kessel M; Weiss C; Goloubinoff P
    Proc Natl Acad Sci U S A; 1995 Dec; 92(26):12021-5. PubMed ID: 8618836
    [TBL] [Abstract][Full Text] [Related]  

  • 15. 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]  

  • 16. Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution.
    Marchenkov V; Gorokhovatsky A; Marchenko N; Ivashina T; Semisotnov G
    Biomolecules; 2020 Jan; 10(1):. PubMed ID: 31968530
    [TBL] [Abstract][Full Text] [Related]  

  • 17. An expanded protein folding cage in the GroEL-gp31 complex.
    Clare DK; Bakkes PJ; van Heerikhuizen H; van der Vies SM; Saibil HR
    J Mol Biol; 2006 May; 358(3):905-11. PubMed ID: 16549073
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Dissociation of the GroEL-GroES asymmetric complex is accelerated by increased cooperativity in ATP binding to the GroEL ring distal to GroES.
    Fridmann Y; Kafri G; Danziger O; Horovitz A
    Biochemistry; 2002 May; 41(18):5938-44. PubMed ID: 11980498
    [TBL] [Abstract][Full Text] [Related]  

  • 19. 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]  

  • 20. 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]  

    [Next]    [New Search]
    of 13.