Rapid and easy thermodynamic optimization of the 5′-end of mRNA dramatically increases the level of wild type protein expression in Escherichia coli
- 1 February 2006
- journal article
- Published by Elsevier in Protein Expression and Purification
- Vol. 45 (2) , 374-380
- https://doi.org/10.1016/j.pep.2005.07.007
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- A codon window in mRNA downstream of the initiation codon where NGG codons give strongly reduced gene expression in Escherichia coliNucleic Acids Research, 2004
- Translational Standby Sites: How Ribosomes May Deal with the Rapid Folding Kinetics of mRNAPublished by Elsevier ,2003
- Effects of codon usage versus putative 5′-mRNA structure on the expression of Fusarium solani cutinase in the Escherichia coli cytoplasmProtein Expression and Purification, 2002
- Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coliProtein Science, 2002
- Effect of the Codon Following the ATG Start Site on the Expression of Ovine Growth Hormone in Escherichia coliProtein Expression and Purification, 1999
- The effect of changes in nucleotide sequence coding for the N-terminus on expression levels of ovine growth hormone variants in Escherichia coliBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1995
- An unstructured mRNA region and a 5′ hairpin represent important elements of theE.colitranslation initiation signal determined by using the bacteriophage 17 gene 1 translation start siteNucleic Acids Research, 1993
- Secondary structure of the ribosome binding site determines translational efficiency: a quantitative analysis.Proceedings of the National Academy of Sciences, 1990
- The influence of mRNA primary and secondary structure on human IFN-γ gene expression inE. coliNucleic Acids Research, 1984
- Optimal computer folding of large RNA sequences using thermodynamics and auxiliary informationNucleic Acids Research, 1981