Format
Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 30

1.

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.

Xu Z, Horwich AL, Sigler PB.

Nature. 1997 Aug 21;388(6644):741-50.

PMID:
9285585
2.

GroEL/GroES: structure and function of a two-stroke folding machine.

Xu Z, Sigler PB.

J Struct Biol. 1998 Dec 15;124(2-3):129-41. Review.

PMID:
10049801
3.

Protein folding assisted by the GroEL/GroES chaperonin system.

Martin J.

Biochemistry (Mosc). 1998 Apr;63(4):374-81. Review.

PMID:
9556520
4.

Chaperonin-mediated protein folding: fate of substrate polypeptide.

Fenton WA, Horwich AL.

Q Rev Biophys. 2003 May;36(2):229-56. Review.

PMID:
14686103
5.

La cage aux fold: asymmetry in the crystal structure of GroEL-GroES-(ADP)7.

Harrison CJ.

Structure. 1997 Oct 15;5(10):1261-4. Review.

6.

GroEL-mediated protein folding.

Fenton WA, Horwich AL.

Protein Sci. 1997 Apr;6(4):743-60. Review.

7.

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. Review.

PMID:
9759498
8.

Structural aspects of GroEL function.

Horovitz A.

Curr Opin Struct Biol. 1998 Feb;8(1):93-100. Review.

PMID:
9519301
9.

Structure and allostery of the chaperonin GroEL.

Saibil HR, Fenton WA, Clare DK, Horwich AL.

J Mol Biol. 2013 May 13;425(9):1476-87. doi: 10.1016/j.jmb.2012.11.028. Epub 2012 Nov 24. Review.

PMID:
23183375
10.

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding.

Todd MJ, Viitanen PV, Lorimer GH.

Science. 1994 Jul 29;265(5172):659-66. Review.

PMID:
7913555
11.

Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.

Taguchi H.

J Mol Biol. 2015 Sep 11;427(18):2912-8. doi: 10.1016/j.jmb.2015.04.007. Epub 2015 Apr 18. Review.

PMID:
25900372
12.

Putting a lid on protein folding: structure and function of the co-chaperonin, GroES.

Fenton WA, Weissman JS, Horwich AL.

Chem Biol. 1996 Mar;3(3):157-61. Review.

13.

Molecular chaperone GroEL/ES: unfolding and refolding processes.

Ryabova NA, Marchenkov VV, Marchenkova SY, Kotova NV, Semisotnov GV.

Biochemistry (Mosc). 2013 Dec;78(13):1405-14. doi: 10.1134/S0006297913130038. Review.

14.

The chaperonin cycle and protein folding.

Lund P.

Bioessays. 1994 Apr;16(4):229-31. Review.

PMID:
7913317
15.

The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding.

Hayer-Hartl M, Bracher A, Hartl FU.

Trends Biochem Sci. 2016 Jan;41(1):62-76. doi: 10.1016/j.tibs.2015.07.009. Epub 2015 Sep 25. Review.

PMID:
26422689
16.

Chaperonin-mediated protein folding.

Thirumalai D, Lorimer GH.

Annu Rev Biophys Biomol Struct. 2001;30:245-69. Review.

PMID:
11340060
17.

Chaperonin-co-chaperonin interactions.

Boshoff A.

Subcell Biochem. 2015;78:153-78. doi: 10.1007/978-3-319-11731-7_8. Review.

PMID:
25487021
18.

Allosteric Mechanisms in Chaperonin Machines.

Gruber R, Horovitz A.

Chem Rev. 2016 Jun 8;116(11):6588-606. doi: 10.1021/acs.chemrev.5b00556. Epub 2016 Jan 4. Review.

PMID:
26726755
19.
20.

Supplemental Content

Support Center