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.
123 related articles for article (PubMed ID: 8807841)
1. Putting a lid on protein folding: structure and function of the co-chaperonin, GroES. Fenton WA; Weissman JS; Horwich AL Chem Biol; 1996 Mar; 3(3):157-61. PubMed ID: 8807841 [TBL] [Abstract][Full Text] [Related]
2. 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]
3. The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding. Hayer-Hartl M; Bracher A; Hartl FU Trends Biochem Sci; 2016 Jan; 41(1):62-76. PubMed ID: 26422689 [TBL] [Abstract][Full Text] [Related]
4. Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES. Chi H; Wang X; Li J; Ren H; Huang F Sci Rep; 2015 Nov; 5():17037. PubMed ID: 26585937 [TBL] [Abstract][Full Text] [Related]
5. 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]
6. Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes. Farr GW; Fenton WA; Chaudhuri TK; Clare DK; Saibil HR; Horwich AL EMBO J; 2003 Jul; 22(13):3220-30. PubMed ID: 12839985 [TBL] [Abstract][Full Text] [Related]
7. Flexibility of GroES mobile loop is required for efficient chaperonin function. Nojima T; Ikegami T; Taguchi H; Yoshida M J Mol Biol; 2012 Sep; 422(2):291-9. PubMed ID: 22634549 [TBL] [Abstract][Full Text] [Related]
8. Protein folding assisted by the GroEL/GroES chaperonin system. Martin J Biochemistry (Mosc); 1998 Apr; 63(4):374-81. PubMed ID: 9556520 [TBL] [Abstract][Full Text] [Related]
9. Reversible oligomerization and denaturation of the chaperonin GroES. Seale JW; Gorovits BM; Ybarra J; Horowitz PM Biochemistry; 1996 Apr; 35(13):4079-83. PubMed ID: 8672442 [TBL] [Abstract][Full Text] [Related]
10. 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]
11. Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level. Gupta AJ; Haldar S; Miličić G; Hartl FU; Hayer-Hartl M J Mol Biol; 2014 Jul; 426(15):2739-54. PubMed ID: 24816391 [TBL] [Abstract][Full Text] [Related]
12. The lid that shapes the pot: structure and function of the chaperonin GroES. Saibil H Structure; 1996 Jan; 4(1):1-4. PubMed ID: 8805512 [TBL] [Abstract][Full Text] [Related]
13. 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]
14. GroEL and the GroEL-GroES Complex. Ishii N Subcell Biochem; 2017; 83():483-504. PubMed ID: 28271487 [TBL] [Abstract][Full Text] [Related]
15. Role of chaperonins in protein folding. A new model of the GroEL/GroES complex architecture. Basharov MA Biochemistry (Mosc); 1997 Apr; 62(4):416-24. PubMed ID: 9312423 [TBL] [Abstract][Full Text] [Related]
16. 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]
17. 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]
18. The architecture of the GroEL-GroES-(ADP)(7) chaperonin complex. I. Heptagrammal molecular forms. Janner A Acta Crystallogr D Biol Crystallogr; 2003 May; 59(Pt 5):783-94. PubMed ID: 12777793 [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. Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics. Chaudhry C; Farr GW; Todd MJ; Rye HS; Brunger AT; Adams PD; Horwich AL; Sigler PB EMBO J; 2003 Oct; 22(19):4877-87. PubMed ID: 14517228 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]