Purification of viral neuraminidase from inclusion bodies produced by recombinant Escherichia coli
- 10 June 2020
- journal article
- research article
- Published by Elsevier BV in Journal of Biotechnology
- Vol. 316, 27-34
- https://doi.org/10.1016/j.jbiotec.2020.04.005
Abstract
No abstract availableKeywords
Funding Information
- Slovak Research and Development Agency (APVV-17-0239)
This publication has 52 references indexed in Scilit:
- Influenza A penetrates host mucus by cleaving sialic acids with neuraminidaseVirology Journal, 2013
- Glycomic Analysis of Human Respiratory Tract Tissues and Correlation with Influenza Virus InfectionPLoS Pathogens, 2013
- Recombinant Production of Human Interleukin 6 in Escherichia coliPLOS ONE, 2013
- Kinetics of Inclusion Body Formation and Its Correlation with the Characteristics of Protein Aggregates in Escherichia coliPLOS ONE, 2012
- A Generic System for the Expression and Purification of Soluble and Stable Influenza NeuraminidasePLOS ONE, 2011
- Isolation of cell-free bacterial inclusion bodiesMicrobial Cell Factories, 2010
- Rare codon content affects the solubility of recombinant proteins in a codon bias-adjusted Escherichia coli strainMicrobial Cell Factories, 2009
- Effect of osmotic stress and heat shock in recombinant protein overexpression and crystallizationProtein Expression and Purification, 2007
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970