Strategies for optimization of heterologous protein expression in E. coli: Roadblocks and reinforcements

J Kaur, A Kumar, J Kaur - International journal of biological …, 2018 - Elsevier
E. coli is most preferred system used for the production of recombinant proteins in bacteria
and the availability of improved genetic tools/methods are making it more valuable than …

Design and production of bispecific antibodies

Q Wang, Y Chen, J Park, X Liu, Y Hu, T Wang… - Antibodies, 2019 - mdpi.com
With the current biotherapeutic market dominated by antibody molecules, bispecific
antibodies represent a key component of the next-generation of antibody therapy. Bispecific …

Recombinant protein expression in Escherichia coli: advances and challenges

GL Rosano, EA Ceccarelli - Frontiers in microbiology, 2014 - frontiersin.org
Escherichia coli is one of the organisms of choice for the production of recombinant proteins.
Its use as a cell factory is well-established and it has become the most popular expression …

Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system

S Costa, A Almeida, A Castro… - Frontiers in microbiology, 2014 - frontiersin.org
Proteins are now widely produced in diverse microbial cell factories. The Escherichia coli is
still the dominant host for recombinant protein production but, as a bacterial cell, it also has …

Enhancement of soluble protein expression through the use of fusion tags

D Esposito, DK Chatterjee - Current opinion in biotechnology, 2006 - Elsevier
The soluble expression of heterologous proteins in Escherichia coli remains a serious
bottleneck in protein production. Although alteration of expression conditions can sometimes …

Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview

B Gasser, M Saloheimo, U Rinas, M Dragosits… - Microbial cell …, 2008 - Springer
Different species of microorganisms including yeasts, filamentous fungi and bacteria have
been used in the past 25 years for the controlled production of foreign proteins of scientific …

[HTML][HTML] Production of prone-to-aggregate proteins

M Lebendiker, T Danieli - FEBS letters, 2014 - Elsevier
Expression of recombinant proteins in Escherichia coli (E. coli) remains the most popular
and cost-effective method for producing proteins in basic research and for pharmaceutical …

[HTML][HTML] Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid-or benzyl alcohol–overexpressed molecular chaperones

A De Marco, L Vigh, S Diamant… - Cell stress & …, 2005 - ncbi.nlm.nih.gov
When massively expressed in bacteria, recombinant proteins often tend to misfold and
accumulate as soluble and insoluble nonfunctional aggregates. A general strategy to …

Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli

VD Nguyen, F Hatahet, KEH Salo, E Enlund… - Microbial cell …, 2011 - Springer
Background Disulfide bonds are one of the most common post-translational modifications
found in proteins. The production of proteins that contain native disulfide bonds is …

The pST44 polycistronic expression system for producing protein complexes in Escherichia coli

S Tan, RC Kern, W Selleck - Protein expression and purification, 2005 - Elsevier
Protein complexes are responsible for key biological processes, but methods to produce
recombinant protein complexes for biochemical and biophysical studies are limited. We …