270 related articles for article (PubMed ID: 9102459)
1. Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction.
Ranson NA; Burston SG; Clarke AR
J Mol Biol; 1997 Mar; 266(4):656-64. PubMed ID: 9102459
[TBL] [Abstract][Full Text] [Related]
2. 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]
3. Coupling between protein folding and allostery in the GroE chaperonin system.
Yifrach O; Horovitz A
Proc Natl Acad Sci U S A; 2000 Feb; 97(4):1521-4. PubMed ID: 10677493
[TBL] [Abstract][Full Text] [Related]
4. Folding of malate dehydrogenase inside the GroEL-GroES cavity.
Chen J; Walter S; Horwich AL; Smith DL
Nat Struct Biol; 2001 Aug; 8(8):721-8. PubMed ID: 11473265
[TBL] [Abstract][Full Text] [Related]
5. Assay of malate dehydrogenase. A substrate for the E. coli chaperonins GroEL and GroES.
Hayer-Hartl M
Methods Mol Biol; 2000; 140():127-32. PubMed ID: 11484479
[No Abstract] [Full Text] [Related]
6. 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]
7. Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity.
Betancourt MR; Thirumalai D
J Mol Biol; 1999 Apr; 287(3):627-44. PubMed ID: 10092464
[TBL] [Abstract][Full Text] [Related]
8. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings.
Kad NM; Ranson NA; Cliff MJ; Clarke AR
J Mol Biol; 1998 Apr; 278(1):267-78. PubMed ID: 9571049
[TBL] [Abstract][Full Text] [Related]
9. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
Martin J; Mayhew M; Langer T; Hartl FU
Nature; 1993 Nov; 366(6452):228-33. PubMed ID: 7901770
[TBL] [Abstract][Full Text] [Related]
10. Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds.
Ranson NA; Dunster NJ; Burston SG; Clarke AR
J Mol Biol; 1995 Jul; 250(5):581-6. PubMed ID: 7623376
[TBL] [Abstract][Full Text] [Related]
11. 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]
12. 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]
13. 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]
14. 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]
15. Specificity in chaperonin-mediated protein folding.
Tian G; Vainberg IE; Tap WD; Lewis SA; Cowan NJ
Nature; 1995 May; 375(6528):250-3. PubMed ID: 7746329
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form.
von Ahsen O; Tropschug M; Pfanner N; Rassow J
EMBO J; 1997 Aug; 16(15):4568-78. PubMed ID: 9303301
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. Recognition of partially-folded mitochondrial malate dehydrogenase by GroEL. Steady and time-dependent emission anisotropy measurements.
Churchich JE
Protein Sci; 1998 Dec; 7(12):2587-94. PubMed ID: 9865953
[TBL] [Abstract][Full Text] [Related]
20. 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]
[Next] [New Search]
