Escherichia coli “TatExpress” strains export several g/L human growth hormone to the periplasm by the Tat pathway

Comparative proteome analysis in an Escherichia coli CyDisCo strain identifies stress responses related to protein production, oxidative stress and accumulation of misfolded protein

(2019) Isabel Guerrero Montero et al.   Microbial Cell Factories

High purity recombinant human growth hormone (rhGH) expression in Escherichia coli under phoA promoter

(2016) Hao Song et al.   Bioengineered

Efficient export of human growth hormone, interferon α2b and antibody fragments to the periplasm by the Escherichia coli Tat pathway in the absence of prior disulfide bond formation

(2015) Heli I. Alanen et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

Biopharmaceutical benchmarks 2014

(2014) Gary Walsh   NATURE BIOTECHNOLOGY

Efficient export of prefolded, disulfide-bonded recombinant proteins to the periplasm by the Tat pathway in Escherichia coli CyDisCo strains

(2013) Cristina F. R. O. Matos et al.   BIOTECHNOLOGY PROGRESS

High-yield export of a native heterologous protein to the periplasm by the tat translocation pathway in Escherichia coli

(2012) Cristina F.R.O. Matos et al.   BIOTECHNOLOGY AND BIOENGINEERING

Periplasmic production via the pET expression system of soluble, bioactive human growth hormone

(2012) Jonathan T. Sockolosky et al.   PROTEIN EXPRESSION AND PURIFICATION

Advances in product release strategies and impact on bioprocess design

(2009) Bangaru Balasundaram et al.   TRENDS IN BIOTECHNOLOGY

Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane—Distinct translocases and mechanisms

(2007) Paolo Natale et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES