215 related articles for article (PubMed ID: 24563543)
1. Evaluation of the stability of an SR398/GroES chaperonin complex.
Ishino S; Kawata Y; Ikegami T; Matsuzaki K; Hoshino M
J Biochem; 2014 May; 155(5):295-300. PubMed ID: 24563543
[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. 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]
5. Cryo-EM structure of the native GroEL-GroES complex from thermus thermophilus encapsulating substrate inside the cavity.
Kanno R; Koike-Takeshita A; Yokoyama K; Taguchi H; Mitsuoka K
Structure; 2009 Feb; 17(2):287-93. PubMed ID: 19217399
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. 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]
8. Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP.
Motojima F; Yoshida M
J Biol Chem; 2003 Jul; 278(29):26648-54. PubMed ID: 12736270
[TBL] [Abstract][Full Text] [Related]
9. 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]
10. 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]
11. 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]
12. 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]
13. A dynamic model of long-range conformational adaptations triggered by nucleotide binding in GroEL-GroES.
Skjaerven L; Muga A; Reuter N; Martinez A
Proteins; 2012 Oct; 80(10):2333-46. PubMed ID: 22576372
[TBL] [Abstract][Full Text] [Related]
14. 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]
15. 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]
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. Physicochemical Properties of the Mammalian Molecular Chaperone HSP60.
Ishida R; Okamoto T; Motojima F; Kubota H; Takahashi H; Tanabe M; Oka T; Kitamura A; Kinjo M; Yoshida M; Otaka M; Grave E; Itoh H
Int J Mol Sci; 2018 Feb; 19(2):. PubMed ID: 29415503
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. 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]
20. 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]
[Next] [New Search]
