166 related articles for article (PubMed ID: 11484479)
1. 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]
2. Refolding of bovine mitochondrial rhodanese by chaperonins GroEL and GroES.
Weber F; Hayer-Hartl M
Methods Mol Biol; 2000; 140():117-26. PubMed ID: 11484478
[No Abstract] [Full Text] [Related]
3. 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]
4. 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]
5. 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]
6. From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.
Chatellier J; Hill F; Foster NW; Goloubinoff P; Fersht AR
J Mol Biol; 2000 Dec; 304(5):897-910. PubMed ID: 11124035
[TBL] [Abstract][Full Text] [Related]
7. 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]
8. The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.
Azem A; Diamant S; Kessel M; Weiss C; Goloubinoff P
Proc Natl Acad Sci U S A; 1995 Dec; 92(26):12021-5. PubMed ID: 8618836
[TBL] [Abstract][Full Text] [Related]
9. Assay of chaperonin-assisted refolding of citrate synthase.
Steede NK; Temkin SL; Landry SJ
Methods Mol Biol; 2000; 140():133-8. PubMed ID: 11484480
[No Abstract] [Full Text] [Related]
10. From minichaperone to GroEL 2: importance of avidity of the multisite ring structure.
Chatellier J; Hill F; Fersht AR
J Mol Biol; 2000 Dec; 304(5):883-96. PubMed ID: 11124034
[TBL] [Abstract][Full Text] [Related]
11. 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]
12. Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.
Peralta D; Hartman DJ; Hoogenraad NJ; Høj PB
FEBS Lett; 1994 Feb; 339(1-2):45-9. PubMed ID: 7906229
[TBL] [Abstract][Full Text] [Related]
13. Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro.
Hartman DJ; Surin BP; Dixon NE; Hoogenraad NJ; Høj PB
Proc Natl Acad Sci U S A; 1993 Mar; 90(6):2276-80. PubMed ID: 8096339
[TBL] [Abstract][Full Text] [Related]
14. 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]
15. 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]
16. Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation.
Figueiredo L; Klunker D; Ang D; Naylor DJ; Kerner MJ; Georgopoulos C; Hartl FU; Hayer-Hartl M
J Biol Chem; 2004 Jan; 279(2):1090-9. PubMed ID: 14576149
[TBL] [Abstract][Full Text] [Related]
17. Phosphofructokinase interacts with molecular chaperonins GroEL and GroES.
Melegh B; Minami Y
Acta Biol Hung; 1997; 48(4):399-407. PubMed ID: 9847453
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. Refolding and recognition of mitochondrial malate dehydrogenase by Escherichia coli chaperonins cpn 60 (groEL) and cpn10 (groES).
Hutchinson JP; el-Thaher TS; Miller AD
Biochem J; 1994 Sep; 302 ( Pt 2)(Pt 2):405-10. PubMed ID: 7916564
[TBL] [Abstract][Full Text] [Related]
20. Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL.
Nojima T; Murayama S; Yoshida M; Motojima F
J Biol Chem; 2008 Jun; 283(26):18385-92. PubMed ID: 18430731
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
