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Protein transport by the bacterial Tat pathway.
Patel R, Smith SM, Robinson C. Patel R, et al. Biochim Biophys Acta. 2014 Aug;1843(8):1620-8. doi: 10.1016/j.bbamcr.2014.02.013. Epub 2014 Feb 26. Biochim Biophys Acta. 2014. PMID: 24583120
High-level secretion of a recombinant protein to the culture medium with a Bacillus subtilis twin-arginine translocation system in Escherichia coli.
Albiniak AM, Matos CF, Branston SD, Freedman RB, Keshavarz-Moore E, Robinson C. Albiniak AM, et al. FEBS J. 2013 Aug;280(16):3810-21. doi: 10.1111/febs.12376. Epub 2013 Jul 5. FEBS J. 2013. PMID: 23745597
High-yield export of a native heterologous protein to the periplasm by the tat translocation pathway in Escherichia coli.
Matos CF, Branston SD, Albiniak A, Dhanoya A, Freedman RB, Keshavarz-Moore E, Robinson C. Matos CF, et al. Biotechnol Bioeng. 2012 Oct;109(10):2533-42. doi: 10.1002/bit.24535. Epub 2012 May 11. Biotechnol Bioeng. 2012. PMID: 22539025
The Tat protein export pathway and its role in cyanobacterial metalloprotein biosynthesis.
Barnett JP, Robinson C, Scanlan DJ, Blindauer CA. Barnett JP, et al. FEMS Microbiol Lett. 2011 Dec;325(1):1-9. doi: 10.1111/j.1574-6968.2011.02391.x. Epub 2011 Sep 20. FEMS Microbiol Lett. 2011. PMID: 22092855 Review.
Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network.
Vladimirou E, Li M, Aldridge CP, Frigerio L, Kirkilionis M, Robinson C. Vladimirou E, et al. FEBS Lett. 2009 Nov 19;583(22):3690-6. doi: 10.1016/j.febslet.2009.10.057. Epub 2009 Oct 23. FEBS Lett. 2009. PMID: 19854178
The twin-arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirements.
Barnett JP, van der Ploeg R, Eijlander RT, Nenninger A, Mendel S, Rozeboom R, Kuipers OP, van Dijl JM, Robinson C. Barnett JP, et al. FEBS J. 2009 Jan;276(1):232-43. doi: 10.1111/j.1742-4658.2008.06776.x. Epub 2008 Nov 25. FEBS J. 2009. PMID: 19049517
An Escherichia coli twin-arginine signal peptide switches between helical and unstructured conformations depending on the hydrophobicity of the environment.
San Miguel M, Marrington R, Rodger PM, Rodger A, Robinson C. San Miguel M, et al. Eur J Biochem. 2003 Aug;270(16):3345-52. doi: 10.1046/j.1432-1033.2003.03710.x. Eur J Biochem. 2003. PMID: 12899691
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