88 related articles for article (PubMed ID: 16791320)
1. Hydrogel polymer appears to mimic the performance of the GroEL/GroES molecular chaperone machine.
Jones H; Dalmaris J; Wright M; Steinke JH; Miller AD
Org Biomol Chem; 2006 Jul; 4(13):2568-74. PubMed ID: 16791320
[TBL] [Abstract][Full Text] [Related]
2. Design of a molecular chaperone-assisted protein folding bioreactor.
Kohler RJ; Preuss M; Miller AD
Biotechnol Prog; 2000; 16(4):671-5. PubMed ID: 10933845
[TBL] [Abstract][Full Text] [Related]
3. The mechanism of GroEL/GroES folding/refolding of protein substrates revisited.
Jones H; Preuss M; Wright M; Miller AD
Org Biomol Chem; 2006 Apr; 4(7):1223-35. PubMed ID: 16557310
[TBL] [Abstract][Full Text] [Related]
4. Comparison of refolding activities between nanogel artificial chaperone and GroEL systems.
Asayama W; Sawada S; Taguchi H; Akiyoshi K
Int J Biol Macromol; 2008 Apr; 42(3):241-6. PubMed ID: 18179818
[TBL] [Abstract][Full Text] [Related]
5. 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]
6. Global minimization of an off-lattice potential energy function using a chaperone-based refolding method.
Gorse D
Biopolymers; 2001 Nov; 59(6):411-26. PubMed ID: 11598876
[TBL] [Abstract][Full Text] [Related]
7. GroEL walks the fine line: the subtle balance of substrate and co-chaperonin binding by GroEL. A combinatorial investigation by design, selection and screening.
Kawe M; Plückthun A
J Mol Biol; 2006 Mar; 357(2):411-26. PubMed ID: 16427651
[TBL] [Abstract][Full Text] [Related]
8. GroEL-GroES-mediated protein folding.
Horwich AL; Farr GW; Fenton WA
Chem Rev; 2006 May; 106(5):1917-30. PubMed ID: 16683761
[No Abstract] [Full Text] [Related]
9. Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity.
Shimamura T; Koike-Takeshita A; Yokoyama K; Masui R; Murai N; Yoshida M; Taguchi H; Iwata S
Structure; 2004 Aug; 12(8):1471-80. PubMed ID: 15296740
[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. Recovery and reuse of the molecular chaperone GroEL for in vitro protein refolding.
Guise AD; Chaudhuri JB
Biotechnol Prog; 1998; 14(2):343-6. PubMed ID: 9548790
[TBL] [Abstract][Full Text] [Related]
12. Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones.
Park ES; Fenton WA; Horwich AL
Proc Natl Acad Sci U S A; 2007 Feb; 104(7):2145-50. PubMed ID: 17283341
[TBL] [Abstract][Full Text] [Related]
13. Hidden order in the GroEL-GroES-(ADP)7 chaperonin: forms, folding, and ADP-binding sites.
Janner A
Proteins; 2003 Apr; 51(1):126-36. PubMed ID: 12596269
[TBL] [Abstract][Full Text] [Related]
14. Monitoring protein conformation along the pathway of chaperonin-assisted folding.
Sharma S; Chakraborty K; Müller BK; Astola N; Tang YC; Lamb DC; Hayer-Hartl M; Hartl FU
Cell; 2008 Apr; 133(1):142-53. PubMed ID: 18394994
[TBL] [Abstract][Full Text] [Related]
15. Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli.
Gupta P; Aggarwal N; Batra P; Mishra S; Chaudhuri TK
Int J Biochem Cell Biol; 2006; 38(11):1975-85. PubMed ID: 16822698
[TBL] [Abstract][Full Text] [Related]
16. Probing dynamics and conformational change of the GroEL-GroES complex by 13C NMR spectroscopy.
Nishida N; Motojima F; Idota M; Fujikawa H; Yoshida M; Shimada I; Kato K
J Biochem; 2006 Oct; 140(4):591-8. PubMed ID: 16963786
[TBL] [Abstract][Full Text] [Related]
17. 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]
18. Chaperones in bacteriophage T4 assembly.
Marusich EI; Kurochkina LP; Mesyanzhinov VV
Biochemistry (Mosc); 1998 Apr; 63(4):399-406. PubMed ID: 9556522
[TBL] [Abstract][Full Text] [Related]
19. Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.
Tang YC; Chang HC; Roeben A; Wischnewski D; Wischnewski N; Kerner MJ; Hartl FU; Hayer-Hartl M
Cell; 2006 Jun; 125(5):903-14. PubMed ID: 16751100
[TBL] [Abstract][Full Text] [Related]
20. Multiple structural transitions of the GroEL subunit are sensitive to intermolecular interactions with cochaperonin and refolding polypeptide.
Yoshimi T; Hongo K; Mizobata T; Kawata Y
J Biochem; 2006 Mar; 139(3):407-19. PubMed ID: 16567406
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
