270 related articles for article (PubMed ID: 18567585)
1. 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]
2. 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]
3. 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]
4. Denatured proteins facilitate the formation of the football-shaped GroEL-(GroES)2 complex.
Sameshima T; Iizuka R; Ueno T; Funatsu T
Biochem J; 2010 Mar; 427(2):247-54. PubMed ID: 20121703
[TBL] [Abstract][Full Text] [Related]
5. 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]
6. GroEL and the GroEL-GroES Complex.
Ishii N
Subcell Biochem; 2017; 83():483-504. PubMed ID: 28271487
[TBL] [Abstract][Full Text] [Related]
7. 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]
8. Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings.
Koike-Takeshita A; Arakawa T; Taguchi H; Shimamura T
J Mol Biol; 2014 Oct; 426(21):3634-41. PubMed ID: 25174333
[TBL] [Abstract][Full Text] [Related]
9. 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]
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. Single-molecule study on the decay process of the football-shaped GroEL-GroES complex using zero-mode waveguides.
Sameshima T; Iizuka R; Ueno T; Wada J; Aoki M; Shimamoto N; Ohdomari I; Tanii T; Funatsu T
J Biol Chem; 2010 Jul; 285(30):23159-64. PubMed ID: 20511221
[TBL] [Abstract][Full Text] [Related]
12. Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.
Ye X; Lorimer GH
Proc Natl Acad Sci U S A; 2013 Nov; 110(46):E4289-97. PubMed ID: 24167257
[TBL] [Abstract][Full Text] [Related]
13. GroEL Ring Separation and Exchange in the Chaperonin Reaction.
Yan X; Shi Q; Bracher A; Miličić G; Singh AK; Hartl FU; Hayer-Hartl M
Cell; 2018 Jan; 172(3):605-617.e11. PubMed ID: 29336887
[TBL] [Abstract][Full Text] [Related]
14. 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]
15. 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]
16. Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.
Illingworth M; Ellis H; Chen L
Sci Rep; 2017 Aug; 7(1):9710. PubMed ID: 28852160
[TBL] [Abstract][Full Text] [Related]
17. 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]
18. 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]
19. 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]
20. 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]
[Next] [New Search]
