306 related articles for article (PubMed ID: 7649273)
1. 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]
2. 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]
3. The affinity of the GroEL/GroES complex for peptides under conditions of protein folding.
Preuss M; Miller AD
FEBS Lett; 2000 Jan; 466(1):75-9. PubMed ID: 10648816
[TBL] [Abstract][Full Text] [Related]
4. BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers.
Taguchi H; Tsukuda K; Motojima F; Koike-Takeshita A; Yoshida M
J Biol Chem; 2004 Oct; 279(44):45737-43. PubMed ID: 15347650
[TBL] [Abstract][Full Text] [Related]
5. TEM and STEM-EDS evaluation of metal nanoparticle encapsulation in GroEL/GroES complexes according to the reaction mechanism of chaperonin.
Yoda H; Koike-Takeshita A
Microscopy (Oxf); 2021 Jun; 70(3):289-296. PubMed ID: 33173948
[TBL] [Abstract][Full Text] [Related]
6. Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL14(groES7)2 is favored by an asymmetric distribution of nucleotides.
Gorovits BM; Ybarra J; Seale JW; Horowitz PM
J Biol Chem; 1997 Oct; 272(43):26999-7004. PubMed ID: 9341138
[TBL] [Abstract][Full Text] [Related]
7. Dissociation of the GroEL-GroES asymmetric complex is accelerated by increased cooperativity in ATP binding to the GroEL ring distal to GroES.
Fridmann Y; Kafri G; Danziger O; Horovitz A
Biochemistry; 2002 May; 41(18):5938-44. PubMed ID: 11980498
[TBL] [Abstract][Full Text] [Related]
8. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings.
Rye HS; Roseman AM; Chen S; Furtak K; Fenton WA; Saibil HR; Horwich AL
Cell; 1999 Apr; 97(3):325-38. PubMed ID: 10319813
[TBL] [Abstract][Full Text] [Related]
9. Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions.
Behlke J; Ristau O; Schönfeld HJ
Biochemistry; 1997 Apr; 36(17):5149-56. PubMed ID: 9136876
[TBL] [Abstract][Full Text] [Related]
10. GroEL and the GroEL-GroES Complex.
Ishii N
Subcell Biochem; 2017; 83():483-504. PubMed ID: 28271487
[TBL] [Abstract][Full Text] [Related]
11. 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]
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. ATP induces non-identity of two rings in chaperonin GroEL.
Bochkareva ES; Girshovich AS
J Biol Chem; 1994 Sep; 269(39):23869-71. PubMed ID: 7929031
[TBL] [Abstract][Full Text] [Related]
14. 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]
15. ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle.
Tyagi NK; Fenton WA; Horwich AL
FEBS Lett; 2010 Mar; 584(5):951-3. PubMed ID: 20083109
[TBL] [Abstract][Full Text] [Related]
16. Triggering protein folding within the GroEL-GroES complex.
Madan D; Lin Z; Rye HS
J Biol Chem; 2008 Nov; 283(46):32003-13. PubMed ID: 18782766
[TBL] [Abstract][Full Text] [Related]
17. Stability of the asymmetric Escherichia coli chaperonin complex. Guanidine chloride causes rapid dissociation.
Todd MJ; Lorimer GH
J Biol Chem; 1995 Mar; 270(10):5388-94. PubMed ID: 7890652
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. 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]
20. 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]
[Next] [New Search]