226 related articles for article (PubMed ID: 11206062)
1. Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: off-pathway aggregation propensity does not determine the co-chaperonin requirement.
Voziyan PA; Fisher MT
Protein Sci; 2000 Dec; 9(12):2405-12. PubMed ID: 11206062
[TBL] [Abstract][Full Text] [Related]
2. GroE chaperonin-assisted folding and assembly of dodecameric glutamine synthetase.
Fisher MT
Biochemistry (Mosc); 1998 Apr; 63(4):382-98. PubMed ID: 9556521
[TBL] [Abstract][Full Text] [Related]
3. Refolding a glutamine synthetase truncation mutant in vitro: identifying superior conditions using a combination of chaperonins and osmolytes.
Voziyan PA; Jadhav L; Fisher MT
J Pharm Sci; 2000 Aug; 89(8):1036-45. PubMed ID: 10906727
[TBL] [Abstract][Full Text] [Related]
4. The effect of groES on the groEL-dependent assembly of dodecameric glutamine synthetase in the presence of ATP and ADP.
Fisher MT
J Biol Chem; 1994 May; 269(18):13629-36. PubMed ID: 7909810
[TBL] [Abstract][Full Text] [Related]
5. 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]
6. Requirement for GroEL/GroES-dependent protein folding under nonpermissive conditions of macromolecular crowding.
Martin J
Biochemistry; 2002 Apr; 41(15):5050-5. PubMed ID: 11939802
[TBL] [Abstract][Full Text] [Related]
7. Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES) do not catalyse the refolding of mitochondrial malate dehydrogenase.
Miller AD; Maghlaoui K; Albanese G; Kleinjan DA; Smith C
Biochem J; 1993 Apr; 291 ( Pt 1)(Pt 1):139-44. PubMed ID: 8097086
[TBL] [Abstract][Full Text] [Related]
8. On the assembly of dodecameric glutamine synthetase from stable chaperonin complexes.
Fisher MT
J Biol Chem; 1993 Jul; 268(19):13777-9. PubMed ID: 8100224
[TBL] [Abstract][Full Text] [Related]
9. 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]
10. Polyols induce ATP-independent folding of GroEL-bound bacterial glutamine synthetase.
Voziyan PA; Fisher MT
Arch Biochem Biophys; 2002 Jan; 397(2):293-7. PubMed ID: 11795885
[TBL] [Abstract][Full Text] [Related]
11. Designing a high throughput refolding array using a combination of the GroEL chaperonin and osmolytes.
Voziyan PA; Johnston M; Chao A; Bomhoff G; Fisher MT
J Struct Funct Genomics; 2005; 6(2-3):183-8. PubMed ID: 16211517
[TBL] [Abstract][Full Text] [Related]
12. Minimal and optimal mechanisms for GroE-mediated protein folding.
Ben-Zvi AP; Chatellier J; Fersht AR; Goloubinoff P
Proc Natl Acad Sci U S A; 1998 Dec; 95(26):15275-80. PubMed ID: 9860959
[TBL] [Abstract][Full Text] [Related]
13. Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin.
Yoshida T; Kawaguchi R; Taguchi H; Yoshida M; Yasunaga T; Wakabayashi T; Yohda M; Maruyama T
J Mol Biol; 2002 Jan; 315(1):73-85. PubMed ID: 11771967
[TBL] [Abstract][Full Text] [Related]
14. Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP.
Fisher MT
Biochemistry; 1992 Apr; 31(16):3955-63. PubMed ID: 1348957
[TBL] [Abstract][Full Text] [Related]
15. The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding.
Weber F; Keppel F; Georgopoulos C; Hayer-Hartl MK; Hartl FU
Nat Struct Biol; 1998 Nov; 5(11):977-85. PubMed ID: 9808043
[TBL] [Abstract][Full Text] [Related]
16. Chaperonin chamber accelerates protein folding through passive action of preventing aggregation.
Apetri AC; Horwich AL
Proc Natl Acad Sci U S A; 2008 Nov; 105(45):17351-5. PubMed ID: 18987317
[TBL] [Abstract][Full Text] [Related]
17. GroEL-GroES assisted folding of multiple recombinant proteins simultaneously over-expressed in Escherichia coli.
Goyal M; Chaudhuri TK
Int J Biochem Cell Biol; 2015 Jul; 64():277-86. PubMed ID: 25957916
[TBL] [Abstract][Full Text] [Related]
18. GroEL-mediated protein folding: making the impossible, possible.
Lin Z; Rye HS
Crit Rev Biochem Mol Biol; 2006; 41(4):211-39. PubMed ID: 16849107
[TBL] [Abstract][Full Text] [Related]
19. 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]
20. On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein folding.
Hayer-Hartl MK; Ewalt KL; Hartl FU
Biol Chem; 1999 May; 380(5):531-40. PubMed ID: 10384959
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]