288 related articles for article (PubMed ID: 29415503)
1. 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]
2. 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]
3. Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.
Taguchi H
J Mol Biol; 2015 Sep; 427(18):2912-8. PubMed ID: 25900372
[TBL] [Abstract][Full Text] [Related]
4. Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.
Sameshima T; Ueno T; Iizuka R; Ishii N; Terada N; Okabe K; Funatsu T
J Biol Chem; 2008 Aug; 283(35):23765-73. PubMed ID: 18567585
[TBL] [Abstract][Full Text] [Related]
5. GroEL and the GroEL-GroES Complex.
Ishii N
Subcell Biochem; 2017; 83():483-504. PubMed ID: 28271487
[TBL] [Abstract][Full Text] [Related]
6. HSP60 possesses a GTPase activity and mediates protein folding with HSP10.
Okamoto T; Yamamoto H; Kudo I; Matsumoto K; Odaka M; Grave E; Itoh H
Sci Rep; 2017 Dec; 7(1):16931. PubMed ID: 29208924
[TBL] [Abstract][Full Text] [Related]
7. Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant.
Koike-Takeshita A; Yoshida M; Taguchi H
J Biol Chem; 2008 Aug; 283(35):23774-81. PubMed ID: 18567584
[TBL] [Abstract][Full Text] [Related]
8. Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES Complexes.
Haldar S; Gupta AJ; Yan X; Miličić G; Hartl FU; Hayer-Hartl M
J Mol Biol; 2015 Jun; 427(12):2244-55. PubMed ID: 25912285
[TBL] [Abstract][Full Text] [Related]
9. Denatured proteins facilitate the formation of the football-shaped GroEL-(GroES)2 complex.
Sameshima T; Iizuka R; Ueno T; Funatsu T
Biochem J; 2010 Mar; 427(2):247-54. PubMed ID: 20121703
[TBL] [Abstract][Full Text] [Related]
10. Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.
Dubaquié Y; Looser R; Rospert S
Proc Natl Acad Sci U S A; 1997 Aug; 94(17):9011-6. PubMed ID: 9256426
[TBL] [Abstract][Full Text] [Related]
11. Evaluation of the stability of an SR398/GroES chaperonin complex.
Ishino S; Kawata Y; Ikegami T; Matsuzaki K; Hoshino M
J Biochem; 2014 May; 155(5):295-300. PubMed ID: 24563543
[TBL] [Abstract][Full Text] [Related]
12. Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.
Hayer-Hartl MK; Martin J; Hartl FU
Science; 1995 Aug; 269(5225):836-41. PubMed ID: 7638601
[TBL] [Abstract][Full Text] [Related]
13. 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]
14. Mitochondrial heat shock protein (Hsp) 70 and Hsp10 cooperate in the formation of Hsp60 complexes.
Böttinger L; Oeljeklaus S; Guiard B; Rospert S; Warscheid B; Becker T
J Biol Chem; 2015 May; 290(18):11611-22. PubMed ID: 25792736
[TBL] [Abstract][Full Text] [Related]
15. Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings.
Koike-Takeshita A; Arakawa T; Taguchi H; Shimamura T
J Mol Biol; 2014 Oct; 426(21):3634-41. PubMed ID: 25174333
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. 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]
18. 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]
19. 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]
20. The role of ATP hydrolysis in the function of the chaperonin GroEL: dynamic complex formation with GroES.
Kawata Y; Hongo K; Nosaka K; Furutsu Y; Mizobata T; Nagai J
FEBS Lett; 1995 Aug; 369(2-3):283-6. PubMed ID: 7649273
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]