363 related articles for article (PubMed ID: 22576372)
1. 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]
2. 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]
3. Allostery wiring diagrams in the transitions that drive the GroEL reaction cycle.
Tehver R; Chen J; Thirumalai D
J Mol Biol; 2009 Mar; 387(2):390-406. PubMed ID: 19121324
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations.
Kass I; Horovitz A
Proteins; 2002 Sep; 48(4):611-7. PubMed ID: 12211028
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. 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]
8. 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]
9. 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]
10. 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]
11. GroEL/GroES: structure and function of a two-stroke folding machine.
Xu Z; Sigler PB
J Struct Biol; 1998 Dec; 124(2-3):129-41. PubMed ID: 10049801
[TBL] [Abstract][Full Text] [Related]
12. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.
Xu Z; Horwich AL; Sigler PB
Nature; 1997 Aug; 388(6644):741-50. PubMed ID: 9285585
[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. The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/GroES-assisted folding.
Paul S; Singh C; Mishra S; Chaudhuri TK
FASEB J; 2007 Sep; 21(11):2874-85. PubMed ID: 17494995
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.
Cliff MJ; Kad NM; Hay N; Lund PA; Webb MR; Burston SG; Clarke AR
J Mol Biol; 1999 Oct; 293(3):667-84. PubMed ID: 10543958
[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. Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy.
Roseman AM; Ranson NA; Gowen B; Fuller SD; Saibil HR
J Struct Biol; 2001 Aug; 135(2):115-25. PubMed ID: 11580261
[TBL] [Abstract][Full Text] [Related]
19. 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]
20. 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]
[Next] [New Search]
