Role of the chaperone DnaK in protein solubility and conformational quality in inclusion body-formingEscherichia colicells-Reference-Cited by-同舟云学术

Role of the chaperone DnaK in protein solubility and conformational quality in inclusion body-formingEscherichia colicells

Published:2007-08 Issue:2 Volume:273 Page:187-195
ISSN:0378-1097
Container-title:FEMS Microbiology Letters
language:en
Short-container-title:

Author:

MartÃnez-Alonso MÃ³nica,Vera Andrea,Villaverde Antonio

Publisher

Oxford University Press (OUP)

Subject

Genetics,Molecular Biology,Microbiology

Link

http://academic.oup.com/femsle/article-pdf/273/2/187/19428673/273-2-187.pdf

Reference51 articles.

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2. Amrein KE , Takacs B , Stieger M , Molnos J , Flint NA & Burn P (1995) Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL. Proc Natl Acad Sci USA 92: 1048â1052.

3. Arie JP , Miot M , Sassoon N & Betton JM (2006) Formation of active inclusion bodies in the periplasm of Escherichia coli. Mol Microbiol 62: 427â437.

4. Baldwin RL (1986) Temperature dependence of the hydrophobic interaction in protein folding. Proc Natl Acad Sci USA 83: 8069â8072.

5. Baneyx F (2004) Keeping up with protein folding. Microb Cell Fact 3: 6.

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