C. F. Matos

发表

High‐level secretion of a recombinant protein to the culture medium with a Bacillus subtilis twin‐arginine translocation system in Escherichia coli

R. Freedman, A. Albiniak, E. Keshavarz‐Moore, 2013, The FEBS journal.

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

R. Freedman, A. Albiniak, A. Dhanoya, 2012, Biotechnology and bioengineering.

Investigation of the impact of Tat export pathway enhancement on E. coli culture, protein production and early stage recovery

R. Freedman, E. Keshavarz‐Moore, C. F. Matos, 2012, Biotechnology and bioengineering.

Tuning recombinant protein expression to match secretion capacity

R. Morra, N. Dixon, Chris Wyre, 2018, Microbial Cell Factories.

Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria.

N. Vasisht, S. Mendel, C. F. Matos, 2011, Biochimica et biophysica acta.

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.

L. Ruddock, R. Freedman, E. Keshavarz‐Moore, 2015, Biochimica et biophysica acta.

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

L. Ruddock, R. Freedman, E. Keshavarz‐Moore, 2014, Biotechnology progress.

Malfolded recombinant Tat substrates are Tat‐independently degraded in Escherichia coli

T. Brüser, Ute Lindenstrauss, C. F. Matos, 2010, FEBS letters.

The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules

C. F. Matos, C. Robinson, A. Di Cola, 2008, The EMBO journal.

TatD is a central component of a Tat translocon‐initiated quality control system for exported FeS proteins in Escherichia coli

C. F. Matos, C. Robinson, A. Di Cola, 2009, EMBO reports.