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Items: 1 to 20 of 346

1.

Enhancement of over expression and chaperone assisted yield of folded recombinant aconitase in Escherichia coli in bioreactor cultures.

Gupta P, Ghosalkar A, Mishra S, Chaudhuri TK.

J Biosci Bioeng. 2009 Feb;107(2):102-7. doi: 10.1016/j.jbiosc.2008.10.020.

PMID:
19217544
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. Erratum in: Int J Biochem Cell Biol. 2007;39(3):660.

PMID:
16822698
3.

GroEL-GroES assisted folding of multiple recombinant proteins simultaneously over-expressed in Escherichia coli.

Goyal M, Chaudhuri TK.

Int J Biochem Cell Biol. 2015 Jul;64:277-86. doi: 10.1016/j.biocel.2015.04.018.

PMID:
25957916
4.

Design of a molecular chaperone-assisted protein folding bioreactor.

Kohler RJ, Preuss M, Miller AD.

Biotechnol Prog. 2000 Jul-Aug;16(4):671-5.

PMID:
10933845
5.

Chaperone over-expression in Escherichia coli: apparent increased yields of soluble recombinant protein kinases are due mainly to soluble aggregates.

Haacke A, Fendrich G, Ramage P, Geiser M.

Protein Expr Purif. 2009 Apr;64(2):185-93. doi: 10.1016/j.pep.2008.10.022.

PMID:
19038347
6.

Chaperone mediated solubilization of 69-kDa recombinant maltodextrin glucosidase in Escherichia coli.

Paul S, Chaudhuri TK.

J Appl Microbiol. 2008 Jan;104(1):35-41. doi: 10.1111/j.1365-2672.2007.03519.x.

7.

GroEL/GroES-mediated folding of a protein too large to be encapsulated.

Chaudhuri TK, Farr GW, Fenton WA, Rospert S, Horwich AL.

Cell. 2001 Oct 19;107(2):235-46.

8.

Expression of soluble, biologically active recombinant human endostatin in Escherichia coli.

Xu HM, Zhang GY, Ji XD, Cao L, Shu L, Hua ZC.

Protein Expr Purif. 2005 Jun;41(2):252-8.

PMID:
15866710
9.

Effective enhancement of Pseudomonas stutzeri D-phenylglycine aminotransferase functional expression in Pichia pastoris by co-expressing Escherichia coli GroEL-GroES.

Jariyachawalid K, Laowanapiban P, Meevootisom V, Wiyakrutta S.

Microb Cell Fact. 2012 Apr 19;11:47. doi: 10.1186/1475-2859-11-47.

10.

Reduced stability and enhanced surface hydrophobicity drive the binding of apo-aconitase with GroEL during chaperone assisted refolding.

Gupta P, Mishra S, Chaudhuri TK.

Int J Biochem Cell Biol. 2010 May;42(5):683-92. doi: 10.1016/j.biocel.2010.01.002.

PMID:
20060926
11.

Chaperone-assisted refolding of Escherichia coli maltodextrin glucosidase.

Paul S, Punam S, Chaudhuri TK.

FEBS J. 2007 Nov;274(22):6000-10.

12.

In vivo and in vitro folding of a recombinant metalloenzyme, phosphomannose isomerase.

Proudfoot AE, Goffin L, Payton MA, Wells TN, Bernard AR.

Biochem J. 1996 Sep 1;318 ( Pt 2):437-42.

13.
14.

Consortium of fold-catalyzing proteins increases soluble expression of cyclohexanone monooxygenase in recombinant Escherichia coli.

Lee DH, Kim MD, Lee WH, Kweon DH, Seo JH.

Appl Microbiol Biotechnol. 2004 Feb;63(5):549-52.

PMID:
12827321
15.

Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli.

de Marco A, Deuerling E, Mogk A, Tomoyasu T, Bukau B.

BMC Biotechnol. 2007 Jun 12;7:32.

16.

Effects of E. coli chaperones on the solubility of human receptors in an in vitro expression system.

Endo S, Tomimoto Y, Shimizu H, Taniguchi Y, Onizuka T.

Mol Biotechnol. 2006 Jul;33(3):199-209.

PMID:
16946450
17.

The folding of nascent mitochondrial aspartate aminotransferase synthesized in a cell-free extract can be assisted by GroEL and GroES.

Mattingly JR Jr, Yañez AJ, Martinez-Carrion M.

Arch Biochem Biophys. 2000 Oct 1;382(1):113-22.

PMID:
11051104
18.
19.

GroEL assisted folding of large polypeptide substrates in Escherichia coli: Present scenario and assignments for the future.

Chaudhuri TK, Verma VK, Maheshwari A.

Prog Biophys Mol Biol. 2009 Jan;99(1):42-50. doi: 10.1016/j.pbiomolbio.2008.10.007. Review.

PMID:
19027782
20.
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