318 related articles for article (PubMed ID: 22445172)
1. ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin.
Clare DK; Vasishtan D; Stagg S; Quispe J; Farr GW; Topf M; Horwich AL; Saibil HR
Cell; 2012 Mar; 149(1):113-23. PubMed ID: 22445172
[TBL] [Abstract][Full Text] [Related]
2. 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]
3. 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]
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. 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]
6. Factors governing the substrate recognition by GroEL chaperone: a sequence correlation approach.
Chaudhuri TK; Gupta P
Cell Stress Chaperones; 2005; 10(1):24-36. PubMed ID: 15832945
[TBL] [Abstract][Full Text] [Related]
7. 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]
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. Visualizing GroEL/ES in the act of encapsulating a folding protein.
Chen DH; Madan D; Weaver J; Lin Z; Schröder GF; Chiu W; Rye HS
Cell; 2013 Jun; 153(6):1354-65. PubMed ID: 23746846
[TBL] [Abstract][Full Text] [Related]
10. Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE.
Cliff MJ; Limpkin C; Cameron A; Burston SG; Clarke AR
J Biol Chem; 2006 Jul; 281(30):21266-21275. PubMed ID: 16684774
[TBL] [Abstract][Full Text] [Related]
11. 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]
12. Chaperonin complex with a newly folded protein encapsulated in the folding chamber.
Clare DK; Bakkes PJ; van Heerikhuizen H; van der Vies SM; Saibil HR
Nature; 2009 Jan; 457(7225):107-10. PubMed ID: 19122642
[TBL] [Abstract][Full Text] [Related]
13. Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.
Motojima F; Chaudhry C; Fenton WA; Farr GW; Horwich AL
Proc Natl Acad Sci U S A; 2004 Oct; 101(42):15005-12. PubMed ID: 15479763
[TBL] [Abstract][Full Text] [Related]
14. Retardation of Folding Rates of Substrate Proteins in the Nanocage of GroEL.
Koculi E; Thirumalai D
Biochemistry; 2021 Feb; 60(6):460-464. PubMed ID: 33464880
[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. Productive folding of a tethered protein in the chaperonin GroEL-GroES cage.
Motojima F; Yoshida M
Biochem Biophys Res Commun; 2015 Oct; 466(1):72-5. PubMed ID: 26325470
[TBL] [Abstract][Full Text] [Related]
17. 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]
18. 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]
19. Structure and function in GroEL-mediated protein folding.
Sigler PB; Xu Z; Rye HS; Burston SG; Fenton WA; Horwich AL
Annu Rev Biochem; 1998; 67():581-608. PubMed ID: 9759498
[TBL] [Abstract][Full Text] [Related]
20. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.
Chen S; Roseman AM; Hunter AS; Wood SP; Burston SG; Ranson NA; Clarke AR; Saibil HR
Nature; 1994 Sep; 371(6494):261-4. PubMed ID: 7915827
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]