1. van der Ploeg R., Barnett, J.P., Vasisht, N., Goosens, V. J., Poether, D. C., Robinson, C., and van Dijl, J. M. (2011) Salt-sensitivity of minimal Twin-arginine translocases. J Biol Chem. In Press

2. Barnett, J. P., Robinson C., Scanlan D. J., and Blindauer C (2011) The Tat protein export pathway and its role in cyanobacterial metalloprotein biosynthesis. FEMS Microbiol Lett. 325, 1-9.

3. Barnett, J. P., Lawrence, J., Mendel, S., and Robinson C (2011). Expression of the bifunctional Bacillus subtilis TatAd protein in Escherichia coli reveals distinct TatA/B-family and TatB specific domains. Arch Microbiol 193, 583-94.

4. Barnett, J. P., van der Ploeg R., Eijlander R. T., Nenninger A., Mendel S., Rozeboom R., Kuipers O. P., van Dijl JM., and Robinson C (2009). The twin-arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirements. FEBS J 276, 232-43.

5. Mendel S., McCarthy A., Barnett, J. P., Eijlander R. T, Nenninger A, Kuipers O. P., and Robinson C (2008). The Escherichia coli TatABC system and a Bacillus subtilis TatAC-type system recognise three distinct targeting determinants in twin-arginine signal peptides. J Mol Biol 375, 661-72.

6. Barnett, J. P., Eijlander R. T., Kuipers O. P., and Robinson C (2008). A minimal Tat system from a gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes. J Biol Chem 283, 2534-42.

7. Oates J., Barrett C. M., Barnett, J. P., Byrne K. G., Bolhuis A., and Robinson C (2005). The Escherichia coli twin-arginine translocation apparatus incorporates a distinct form of TatABC complex, spectrum of modular TatA complexes and minor TatAB complex. J Mol Biol 346, 295-305.