265 related articles for article (PubMed ID: 11484478)
1. 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]
2. 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]
3. Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding.
Smith KE; Fisher MT
J Biol Chem; 1995 Sep; 270(37):21517-23. PubMed ID: 7665563
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. Prevention of rhodanese aggregation by the chaperonin GroEL.
Weber F; Hayer-Hartl M
Methods Mol Biol; 2000; 140():111-5. PubMed ID: 11484477
[No Abstract] [Full Text] [Related]
6. Chaperonin-assisted protein folding of the enzyme rhodanese by GroEL/GroES.
Horowitz PM
Methods Mol Biol; 1995; 40():361-8. PubMed ID: 7633531
[No Abstract] [Full Text] [Related]
7. Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese.
Mendoza JA; Rogers E; Lorimer GH; Horowitz PM
J Biol Chem; 1991 Jul; 266(20):13044-9. PubMed ID: 1677004
[TBL] [Abstract][Full Text] [Related]
8. Productive folding of a tethered protein in the chaperonin GroEL-GroES cage.
Motojima F; Yoshida M
Biochem Biophys Res Commun; 2015 Oct; 466(1):72-5. PubMed ID: 26325470
[TBL] [Abstract][Full Text] [Related]
9. GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation.
Melkani GC; Zardeneta G; Mendoza JA
Biochem Biophys Res Commun; 2002 Jun; 294(4):893-9. PubMed ID: 12061791
[TBL] [Abstract][Full Text] [Related]
10. 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]
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. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.
Weissman JS; Rye HS; Fenton WA; Beechem JM; Horwich AL
Cell; 1996 Feb; 84(3):481-90. PubMed ID: 8608602
[TBL] [Abstract][Full Text] [Related]
13. Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP.
Makino Y; Taguchi H; Yoshida M
FEBS Lett; 1993 Dec; 336(2):363-7. PubMed ID: 7903258
[TBL] [Abstract][Full Text] [Related]
14. GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle.
Miyazaki T; Yoshimi T; Furutsu Y; Hongo K; Mizobata T; Kanemori M; Kawata Y
J Biol Chem; 2002 Dec; 277(52):50621-8. PubMed ID: 12377767
[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. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.
Hayer-Hartl MK; Weber F; Hartl FU
EMBO J; 1996 Nov; 15(22):6111-21. PubMed ID: 8947033
[TBL] [Abstract][Full Text] [Related]
17. The formation of symmetrical GroEL-GroES complexes in the presence of ATP.
Llorca O; Marco S; Carrascosa JL; Valpuesta JM
FEBS Lett; 1994 May; 345(2-3):181-6. PubMed ID: 7911087
[TBL] [Abstract][Full Text] [Related]
18. Stable expression and rapid purification of Escherichia coli GroEL and GroES chaperonins.
Kamireddi M; Eisenstein E; Reddy P
Protein Expr Purif; 1997 Oct; 11(1):47-52. PubMed ID: 9325138
[TBL] [Abstract][Full Text] [Related]
19. Rhodanese can partially refold in its GroEL-GroES-ADP complex and can be released to give a homogeneous product.
Bhattacharyya AM; Horowitz PM
Biochemistry; 2002 Feb; 41(7):2421-8. PubMed ID: 11841236
[TBL] [Abstract][Full Text] [Related]
20. Biochemical characterization of symmetric GroEL-GroES complexes. Evidence for a role in protein folding.
Llorca O; Carrascosa JL; Valpuesta JM
J Biol Chem; 1996 Jan; 271(1):68-76. PubMed ID: 8550627
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]