393 related articles for article (PubMed ID: 11222029)
1. 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]
2. 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]
3. 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]
4. 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]
5. Interaction of oxidized chaperonin GroEL with an unfolded protein at low temperatures.
Melkani GC; Sielaff R; Zardeneta G; Mendoza JA
Biosci Rep; 2012 Jun; 32(3):299-303. PubMed ID: 22273181
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. On the chaperonin activity of GroEL at heat-shock temperature.
Melkani GC; Zardeneta G; Mendoza JA
Int J Biochem Cell Biol; 2005 Jul; 37(7):1375-85. PubMed ID: 15833270
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. Release of both native and non-native proteins from a cis-only GroEL ternary complex.
Burston SG; Weissman JS; Farr GW; Fenton WA; Horwich AL
Nature; 1996 Sep; 383(6595):96-9. PubMed ID: 8779722
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. A chaperonin from a thermophilic bacterium, Thermus thermophilus.
Yoshida M; Ishii N; Muneyuki E; Taguchi H
Philos Trans R Soc Lond B Biol Sci; 1993 Mar; 339(1289):305-12. PubMed ID: 8098535
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. 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]
14. Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.
Martin J; Geromanos S; Tempst P; Hartl FU
Nature; 1993 Nov; 366(6452):279-82. PubMed ID: 7901771
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. 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]
17. 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]
18. 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]
19. 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]
20. 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]
[Next] [New Search]
