117 related articles for article (PubMed ID: 7904492)
1. A simple and rapid method for the purification of GroEL, an Escherichia coli homolog of the heat shock protein 60 family of molecular chaperonins.
Khandekar SS; Bettencourt BM; Kelley KC; Recny MA
Protein Expr Purif; 1993 Dec; 4(6):580-4. PubMed ID: 7904492
[TBL] [Abstract][Full Text] [Related]
2. (Mg-ATP)-dependent self-assembly of molecular chaperone GroEL.
Lissin NM; Venyaminov SYu ; Girshovich AS
Nature; 1990 Nov; 348(6299):339-42. PubMed ID: 1979147
[TBL] [Abstract][Full Text] [Related]
3. Purification and characterization of Chromatium vinosum GroEL and GroES proteins overexpressed in Escherichia coli cells lacking the endogenous groESL operon.
Dionisi HM; Viale AM
Protein Expr Purif; 1998 Nov; 14(2):275-82. PubMed ID: 9790891
[TBL] [Abstract][Full Text] [Related]
4. Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation.
Sherman MYu ; Goldberg AL
Nature; 1992 May; 357(6374):167-9. PubMed ID: 1349729
[TBL] [Abstract][Full Text] [Related]
5. GroEL assisted folding of large polypeptide substrates in Escherichia coli: Present scenario and assignments for the future.
Chaudhuri TK; Verma VK; Maheshwari A
Prog Biophys Mol Biol; 2009 Jan; 99(1):42-50. PubMed ID: 19027782
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis.
Mogk A; Homuth G; Scholz C; Kim L; Schmid FX; Schumann W
EMBO J; 1997 Aug; 16(15):4579-90. PubMed ID: 9303302
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. [The interaction of the GroEL chaperone with early kinetic intermediates of renaturing proteins inhibits the formation of their native structure].
Marchenkov VV; Sokolovskiĭ IV; Kotova NV; Galzitskaya OV; Bochkareva ES; Girshovich AS; Semisotnov GV
Biofizika; 2004; 49(6):987-94. PubMed ID: 15612537
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. GroEL-like protein complex of thermophilic bacterium Thermus aquaticus.
Mikulík K; Benada O
Biochem Biophys Res Commun; 1993 Dec; 197(2):716-21. PubMed ID: 7903530
[TBL] [Abstract][Full Text] [Related]
12. The chaperonin cycle and protein folding.
Lund P
Bioessays; 1994 Apr; 16(4):229-31. PubMed ID: 7913317
[TBL] [Abstract][Full Text] [Related]
13. Three GroEL homologues from Rhizobium leguminosarum have distinct in vitro properties.
George R; Kelly SM; Price NC; Erbse A; Fisher M; Lund PA
Biochem Biophys Res Commun; 2004 Nov; 324(2):822-8. PubMed ID: 15474501
[TBL] [Abstract][Full Text] [Related]
14. The heat-sensitive Escherichia coli grpE280 phenotype: impaired interaction of GrpE(G122D) with DnaK.
Grimshaw JP; Siegenthaler RK; Züger S; Schönfeld HJ; Z'graggen BR; Christen P
J Mol Biol; 2005 Nov; 353(4):888-96. PubMed ID: 16198374
[TBL] [Abstract][Full Text] [Related]
15. The ATPase activity of chaperonin GroEL is highly stimulated at elevated temperatures.
Mendoza JA; Warren T; Dulin P
Biochem Biophys Res Commun; 1996 Dec; 229(1):271-4. PubMed ID: 8954117
[TBL] [Abstract][Full Text] [Related]
16. Overexpression of dnaK/dnaJ and groEL confers freeze tolerance to Escherichia coli.
Chow KC; Tung WL
Biochem Biophys Res Commun; 1998 Dec; 253(2):502-5. PubMed ID: 9878565
[TBL] [Abstract][Full Text] [Related]
17. The lower hydrolysis of ATP by the stress protein GroEL is a major factor responsible for the diminished chaperonin activity at low temperature.
Mendoza JA; Dulin P; Warren T
Cryobiology; 2000 Dec; 41(4):319-23. PubMed ID: 11222029
[TBL] [Abstract][Full Text] [Related]
18. [Denatured transitions of the molecular chaperone GroEL from Escherichia coli].
Surin AK; Kotova NV; Marchenkova SIu; Sokolovskiĭ IV; Rodionova NA; Iaklichkin SIu; Semisotnov GV
Bioorg Khim; 1997 Apr; 23(4):251-6. PubMed ID: 9221726
[TBL] [Abstract][Full Text] [Related]
19. Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE.
Groemping Y; Klostermeier D; Herrmann C; Veit T; Seidel R; Reinstein J
J Mol Biol; 2001 Feb; 305(5):1173-83. PubMed ID: 11162122
[TBL] [Abstract][Full Text] [Related]
20. Purification and characterization of the GroESLx chaperonins from the symbiotic X-bacteria in Amoeba proteus.
Jung GH; Ahn TI
Protein Expr Purif; 2001 Dec; 23(3):459-67. PubMed ID: 11722184
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
