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Items: 1 to 20 of 208

1.

Directed evolution of substrate-optimized GroEL/S chaperonins.

Wang JD, Herman C, Tipton KA, Gross CA, Weissman JS.

Cell. 2002 Dec 27;111(7):1027-39.

2.

Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli.

Gupta P, Aggarwal N, Batra P, Mishra S, Chaudhuri TK.

Int J Biochem Cell Biol. 2006;38(11):1975-85. Epub 2006 Jun 2. Erratum in: Int J Biochem Cell Biol. 2007;39(3):660.

PMID:
16822698
3.

Chaperonin-mediated folding of green fluorescent protein.

Makino Y, Amada K, Taguchi H, Yoshida M.

J Biol Chem. 1997 May 9;272(19):12468-74.

4.

From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.

Chatellier J, Hill F, Foster NW, Goloubinoff P, Fersht AR.

J Mol Biol. 2000 Dec 15;304(5):897-910.

PMID:
11124035
5.
6.

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 9;466(1):15-20. doi: 10.1016/j.bbrc.2015.08.034. Epub 2015 Aug 11.

PMID:
26271593
7.

GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle.

Miyazaki T, Yoshimi T, Furutsu Y, Hongo K, Mizobata T, Kanemori M, Kawata Y.

J Biol Chem. 2002 Dec 27;277(52):50621-8. Epub 2002 Oct 10.

9.

Essential role of the chaperonin folding compartment in vivo.

Tang YC, Chang HC, Chakraborty K, Hartl FU, Hayer-Hartl M.

EMBO J. 2008 May 21;27(10):1458-68. doi: 10.1038/emboj.2008.77. Epub 2008 Apr 17.

10.

Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation.

Figueiredo L, Klunker D, Ang D, Naylor DJ, Kerner MJ, Georgopoulos C, Hartl FU, Hayer-Hartl M.

J Biol Chem. 2004 Jan 9;279(2):1090-9. Epub 2003 Oct 23.

11.

Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.

Kerner MJ, Naylor DJ, Ishihama Y, Maier T, Chang HC, Stines AP, Georgopoulos C, Frishman D, Hayer-Hartl M, Mann M, Hartl FU.

Cell. 2005 Jul 29;122(2):209-20.

12.

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

Weber-Ban EU, Reid BG, Miranker AD, Horwich AL.

Nature. 1999 Sep 2;401(6748):90-3.

PMID:
10485712
13.

Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.

Tang YC, Chang HC, Roeben A, Wischnewski D, Wischnewski N, Kerner MJ, Hartl FU, Hayer-Hartl M.

Cell. 2006 Jun 2;125(5):903-14.

14.
15.
16.

[Role of GroEL/GroES chaperonin system and Lon protease in regulation of expression Vibrio fischeri lux genes in Escherichia coli cells].

Manukhov IV, Kotova VIu, Zavil'genskiĭ GB.

Mol Biol (Mosk). 2006 Mar-Apr;40(2):277-83. Russian.

PMID:
16637268
17.

Phosphofructokinase interacts with molecular chaperonins GroEL and GroES.

Melegh B, Minami Y.

Acta Biol Hung. 1997;48(4):399-407.

PMID:
9847453
19.

GroEL/S substrate specificity based on substrate unfolding propensity.

Parent KN, Teschke CM.

Cell Stress Chaperones. 2007 Spring;12(1):20-32.

20.

Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding.

Motojima F, Makio T, Aoki K, Makino Y, Kuwajima K, Yoshida M.

Biochem Biophys Res Commun. 2000 Jan 27;267(3):842-9.

PMID:
10673379

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