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Items: 1 to 20 of 23

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.

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. Epub 2008 Nov 7. Review.

PMID:
19027782
3.

Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold.

Thomas JG, Ayling A, Baneyx F.

Appl Biochem Biotechnol. 1997 Jun;66(3):197-238. Review.

PMID:
9276922
4.

Side effects of chaperone gene co-expression in recombinant protein production.

Martínez-Alonso M, García-Fruitós E, Ferrer-Miralles N, Rinas U, Villaverde A.

Microb Cell Fact. 2010 Sep 2;9:64. doi: 10.1186/1475-2859-9-64. Review.

5.

Chaperonin GroEL meets the substrate protein as a "load" of the rings.

Taguchi H.

J Biochem. 2005 May;137(5):543-9. Review.

PMID:
15944406
6.

Molecular and chemical chaperones for improving the yields of soluble recombinant proteins.

de Marco A.

Methods Mol Biol. 2011;705:31-51. doi: 10.1007/978-1-61737-967-3_3. Review.

PMID:
21125379
7.

Chaperomics: in vivo GroEL function defined.

Ellis RJ.

Curr Biol. 2005 Sep 6;15(17):R661-3. Review.

8.

The ins and outs of a molecular chaperone machine.

Richardson A, Landry SJ, Georgopoulos C.

Trends Biochem Sci. 1998 Apr;23(4):138-43. Review.

PMID:
9584617
9.

The intramolecular chaperone-mediated protein folding.

Chen YJ, Inouye M.

Curr Opin Struct Biol. 2008 Dec;18(6):765-70. doi: 10.1016/j.sbi.2008.10.005. Epub 2008 Nov 13. Review.

PMID:
18973809
10.

Chemical and pharmacological chaperones: application for recombinant protein production and protein folding diseases.

Rajan RS, Tsumoto K, Tokunaga M, Tokunaga H, Kita Y, Arakawa T.

Curr Med Chem. 2011;18(1):1-15. Review.

PMID:
21110818
11.

Molecular chaperones: inside and outside the Anfinsen cage.

Ellis RJ.

Curr Biol. 2001 Dec 11;11(24):R1038-40. Review.

12.

[Refolding of recombinant proteins in vitro].

Long JY, Wang HX.

Sheng Li Ke Xue Jin Zhan. 1998 Apr;29(2):103-8. Review. Chinese.

PMID:
12501674
13.

Protein aggregation in recombinant bacteria: biological role of inclusion bodies.

Villaverde A, Carrió MM.

Biotechnol Lett. 2003 Sep;25(17):1385-95. Review.

PMID:
14514038
14.

Engineering the protein folding landscape in gram-negative bacteria.

Mansell TJ, Fisher AC, DeLisa MP.

Curr Protein Pept Sci. 2008 Apr;9(2):138-49. Review.

PMID:
18393885
15.
16.

Chaperonin GroEL: structure and reaction cycle.

Krishna KA, Rao GV, Rao KR.

Curr Protein Pept Sci. 2007 Oct;8(5):418-25. Review.

PMID:
17979757
17.

Antibodies as specific chaperones.

Ermolenko DN, Zherdev AV, Dzantiev BB.

Biochemistry (Mosc). 2004 Nov;69(11):1233-8. Review.

18.

Using folding promoting agents in recombinant protein production: a review.

Fahnert B.

Methods Mol Biol. 2012;824:3-36. doi: 10.1007/978-1-61779-433-9_1. Review.

PMID:
22160891
19.

Enhancing stability and expression of recombinant human hemoglobin in E. coli: Progress in the development of a recombinant HBOC source.

Graves PE, Henderson DP, Horstman MJ, Solomon BJ, Olson JS.

Biochim Biophys Acta. 2008 Oct;1784(10):1471-9. doi: 10.1016/j.bbapap.2008.04.012. Epub 2008 May 1. Review.

PMID:
18489914
20.

Folding-promoting agents in recombinant protein production.

Fahnert B.

Methods Mol Biol. 2004;267:53-74. Review.

PMID:
15269415
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