144 related articles for article (PubMed ID: 7499341)
1. Increased efficiency of GroE-assisted protein folding by manganese ions.
Diamant S; Azem A; Weiss C; Goloubinoff P
J Biol Chem; 1995 Nov; 270(47):28387-91. PubMed ID: 7499341
[TBL] [Abstract][Full Text] [Related]
2. 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]
3. 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]
4. 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]
5. Fluorescence detection of symmetric GroEL14(GroES7)2 heterooligomers involved in protein release during the chaperonin cycle.
Török Z; Vigh L; Goloubinoff P
J Biol Chem; 1996 Jul; 271(27):16180-6. PubMed ID: 8663256
[TBL] [Abstract][Full Text] [Related]
6. GroES binding regulates GroEL chaperonin activity under heat shock.
Goloubinoff P; Diamant S; Weiss C; Azem A
FEBS Lett; 1997 Apr; 407(2):215-9. PubMed ID: 9166902
[TBL] [Abstract][Full Text] [Related]
7. Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL14.
Diamant S; Azem A; Weiss C; Goloubinoff P
Biochemistry; 1995 Jan; 34(1):273-7. PubMed ID: 7819207
[TBL] [Abstract][Full Text] [Related]
8. Refolding of yeast enolase in the presence of the chaperonin GroE. The nucleotide specificity of GroE and the role of GroES.
Kubo T; Mizobata T; Kawata Y
J Biol Chem; 1993 Sep; 268(26):19346-51. PubMed ID: 8103517
[TBL] [Abstract][Full Text] [Related]
9. 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]
10. Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.
Azem A; Kessel M; Goloubinoff P
Science; 1994 Jul; 265(5172):653-6. PubMed ID: 7913553
[TBL] [Abstract][Full Text] [Related]
11. A comparison of the GroE chaperonin requirements for sequentially and structurally homologous malate dehydrogenases: the importance of folding kinetics and solution environment.
Tieman BC; Johnston MF; Fisher MT
J Biol Chem; 2001 Nov; 276(48):44541-50. PubMed ID: 11551947
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL14(groES7)2 is favored by an asymmetric distribution of nucleotides.
Gorovits BM; Ybarra J; Seale JW; Horowitz PM
J Biol Chem; 1997 Oct; 272(43):26999-7004. PubMed ID: 9341138
[TBL] [Abstract][Full Text] [Related]
14. 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]
15. Catalysis, commitment and encapsulation during GroE-mediated folding.
Beissinger M; Rutkat K; Buchner J
J Mol Biol; 1999 Jun; 289(4):1075-92. PubMed ID: 10369783
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. Temperature Regulates Stability, Ligand Binding (Mg
Walker TE; Shirzadeh M; Sun HM; McCabe JW; Roth A; Moghadamchargari Z; Clemmer DE; Laganowsky A; Rye H; Russell DH
J Am Chem Soc; 2022 Feb; 144(6):2667-2678. PubMed ID: 35107280
[TBL] [Abstract][Full Text] [Related]
18. Structural analysis of GroE chaperonin complexes using chemical cross-linking.
Azem A; Weiss C; Goloubinoff P
Methods Enzymol; 1998; 290():253-68. PubMed ID: 9534168
[TBL] [Abstract][Full Text] [Related]
19. 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]
20. Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase.
Ayling A; Baneyx F
Protein Sci; 1996 Mar; 5(3):478-87. PubMed ID: 8868484
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
