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Similar articles for PubMed (Select 10532860)

1.

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH.

Nature. 1989 Dec 21-28;342(6252):884-9.

PMID:
10532860
2.
3.

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent.

Viitanen PV, Lubben TH, Reed J, Goloubinoff P, O'Keefe DP, Lorimer GH.

Biochemistry. 1990 Jun 19;29(24):5665-71.

PMID:
1974461
4.

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 30;97(3):325-38.

5.

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.

Todd MJ, Lorimer GH, Thirumalai D.

Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4030-5.

7.

The single-ring Thermoanaerobacter brockii chaperonin 60 (Tbr-EL7) dimerizes to Tbr-EL14.Tbr-ES7 under protein folding conditions.

Todd MJ, Walke S, Lorimer G, Truscott K, Scopes RK.

Biochemistry. 1995 Nov 14;34(45):14932-41.

PMID:
7578105
8.
9.

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.

Azem A, Diamant S, Kessel M, Weiss C, Goloubinoff P.

Proc Natl Acad Sci U S A. 1995 Dec 19;92(26):12021-5.

10.

GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state.

Tyagi NK, Fenton WA, Horwich AL.

Proc Natl Acad Sci U S A. 2009 Dec 1;106(48):20264-9. doi: 10.1073/pnas.0911556106. Epub 2009 Nov 13.

11.

Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria.

Rospert S, Glick BS, Jenö P, Schatz G, Todd MJ, Lorimer GH, Viitanen PV.

Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):10967-71.

12.

Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring.

Viitanen PV, Lorimer GH, Seetharam R, Gupta RS, Oppenheim J, Thomas JO, Cowan NJ.

J Biol Chem. 1992 Jan 15;267(2):695-8.

13.

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese.

Mendoza JA, Rogers E, Lorimer GH, Horowitz PM.

J Biol Chem. 1991 Jul 15;266(20):13044-9.

14.

Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding.

van der Vies SM, Gatenby AA, Georgopoulos C.

Nature. 1994 Apr 14;368(6472):654-6.

PMID:
7908418
15.

Expansion and compression of a protein folding intermediate by GroEL.

Lin Z, Rye HS.

Mol Cell. 2004 Oct 8;16(1):23-34. Erratum in: Mol Cell. 2004 Oct 22;16(2):317.

16.

The ins and outs of GroEL-mediated protein folding.

Weissman JS.

Mol Cell. 2001 Oct;8(4):730-2.

17.

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.

Azem A, Kessel M, Goloubinoff P.

Science. 1994 Jul 29;265(5172):653-6.

PMID:
7913553
18.

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 21;388(6644):792-8.

PMID:
9285593
19.

Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.

Lin Z, Puchalla J, Shoup D, Rye HS.

J Biol Chem. 2013 Oct 25;288(43):30944-55. doi: 10.1074/jbc.M113.480178. Epub 2013 Sep 10.

20.

Identification of a groES-like chaperonin in mitochondria that facilitates protein folding.

Lubben TH, Gatenby AA, Donaldson GK, Lorimer GH, Viitanen PV.

Proc Natl Acad Sci U S A. 1990 Oct;87(19):7683-7.

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