215 related articles for article (PubMed ID: 9702195)
1. A single ring is sufficient for productive chaperonin-mediated folding in vivo.
Nielsen KL; Cowan NJ
Mol Cell; 1998 Jul; 2(1):93-9. PubMed ID: 9702195
[TBL] [Abstract][Full Text] [Related]
2. Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.
Illingworth M; Salisbury J; Li W; Lin D; Chen L
Biochem Biophys Res Commun; 2015 Oct; 466(1):15-20. PubMed ID: 26271593
[TBL] [Abstract][Full Text] [Related]
3. Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.
Illingworth M; Ramsey A; Zheng Z; Chen L
J Biol Chem; 2011 Sep; 286(35):30401-30408. PubMed ID: 21757689
[TBL] [Abstract][Full Text] [Related]
4. Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity.
Kovács E; Sun Z; Liu H; Scott DJ; Karsisiotis AI; Clarke AR; Burston SG; Lund PA
J Mol Biol; 2010 Mar; 396(5):1271-83. PubMed ID: 20006619
[TBL] [Abstract][Full Text] [Related]
5. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.
Xu Z; Horwich AL; Sigler PB
Nature; 1997 Aug; 388(6644):741-50. PubMed ID: 9285585
[TBL] [Abstract][Full Text] [Related]
6. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.
Roseman AM; Chen S; White H; Braig K; Saibil HR
Cell; 1996 Oct; 87(2):241-51. PubMed ID: 8861908
[TBL] [Abstract][Full Text] [Related]
7. Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.
Illingworth M; Ellis H; Chen L
Sci Rep; 2017 Aug; 7(1):9710. PubMed ID: 28852160
[TBL] [Abstract][Full Text] [Related]
8. The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding.
Weber F; Keppel F; Georgopoulos C; Hayer-Hartl MK; Hartl FU
Nat Struct Biol; 1998 Nov; 5(11):977-85. PubMed ID: 9808043
[TBL] [Abstract][Full Text] [Related]
9. Physicochemical Properties of the Mammalian Molecular Chaperone HSP60.
Ishida R; Okamoto T; Motojima F; Kubota H; Takahashi H; Tanabe M; Oka T; Kitamura A; Kinjo M; Yoshida M; Otaka M; Grave E; Itoh H
Int J Mol Sci; 2018 Feb; 19(2):. PubMed ID: 29415503
[TBL] [Abstract][Full Text] [Related]
10. A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo.
Nielsen KL; McLennan N; Masters M; Cowan NJ
J Bacteriol; 1999 Sep; 181(18):5871-5. PubMed ID: 10482535
[TBL] [Abstract][Full Text] [Related]
11. Structure and function in GroEL-mediated protein folding.
Sigler PB; Xu Z; Rye HS; Burston SG; Fenton WA; Horwich AL
Annu Rev Biochem; 1998; 67():581-608. PubMed ID: 9759498
[TBL] [Abstract][Full Text] [Related]
12. Functional structure and physiological functions of mammalian wild-type HSP60.
Okamoto T; Ishida R; Yamamoto H; Tanabe-Ishida M; Haga A; Takahashi H; Takahashi K; Goto D; Grave E; Itoh H
Arch Biochem Biophys; 2015 Nov; 586():10-9. PubMed ID: 26427351
[TBL] [Abstract][Full Text] [Related]
13. Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.
Farr GW; Furtak K; Rowland MB; Ranson NA; Saibil HR; Kirchhausen T; Horwich AL
Cell; 2000 Mar; 100(5):561-73. PubMed ID: 10721993
[TBL] [Abstract][Full Text] [Related]
14. A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation.
Sewell BT; Best RB; Chen S; Roseman AM; Farr GW; Horwich AL; Saibil HR
Nat Struct Mol Biol; 2004 Nov; 11(11):1128-33. PubMed ID: 15475965
[TBL] [Abstract][Full Text] [Related]
15. Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.
Motojima F; Chaudhry C; Fenton WA; Farr GW; Horwich AL
Proc Natl Acad Sci U S A; 2004 Oct; 101(42):15005-12. PubMed ID: 15479763
[TBL] [Abstract][Full Text] [Related]
16. Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins.
Saibil H
Curr Opin Struct Biol; 2000 Apr; 10(2):251-8. PubMed ID: 10753820
[TBL] [Abstract][Full Text] [Related]
17. Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.
Ranson NA; Clare DK; Farr GW; Houldershaw D; Horwich AL; Saibil HR
Nat Struct Mol Biol; 2006 Feb; 13(2):147-52. PubMed ID: 16429154
[TBL] [Abstract][Full Text] [Related]
18. GroEL and the GroEL-GroES Complex.
Ishii N
Subcell Biochem; 2017; 83():483-504. PubMed ID: 28271487
[TBL] [Abstract][Full Text] [Related]
19. Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level.
Gupta AJ; Haldar S; Miličić G; Hartl FU; Hayer-Hartl M
J Mol Biol; 2014 Jul; 426(15):2739-54. PubMed ID: 24816391
[TBL] [Abstract][Full Text] [Related]
20. GroEL/GroES-mediated folding of a protein too large to be encapsulated.
Chaudhuri TK; Farr GW; Fenton WA; Rospert S; Horwich AL
Cell; 2001 Oct; 107(2):235-46. PubMed ID: 11672530
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
