Da Costa Paula CA, Gore DM, Shah K, Kuit G, Angunawela RI, Barnett JP, and Tuft SJ (2019). Cytomegalovirus infection is not a major cause of corneal graft failure in the United Kingdom. Eye 33, 833-837.
Coverdale JPC, Barnett JP, Adamu AH, Griffiths EJ, Stewart AJ, and Blindauer CA (2019). A metalloproteomic analysis of interactions between plasma proteins and zinc: elevated fatty acid levels affect zinc distribution. Metallomics 11, 1805-1819.
Pass R, Frudd K, Barnett JP, Blindauer CA, and Brown DR (2015). Prion infection in cells is abolished by a mutated manganese transporter but shows no relation to zinc. Mol Cell Neurosci. 68, 186-193.
Barnett JP, Scanlan DJ, and Blindauer CA (2014). Identification of major zinc-binding proteins from a marine cyanobacterium: insight into metal uptake in oligotrophic environments. Metallomics 6, 1254-1268.
Barnett JP, Blindauer CA, Kassaar O, Khazaipoul S, Martin EM, Sadler PJ, and Stewart AJ (2013). Allosteric modulation of zinc speciation by fatty acids. Biochim Biophys Acta. 1830, 5456-5464.
Barnett JP, Millard A, Ksibe A, Scanlan DJ, Schmid R, and Blindauer CA (2012). Mining genomes of cyanobacteria for elements of zinc homeostasis. Front Microbiol Chem. 3, 1-21.
van der Ploeg R, Monteferrante CG, Piersma S, Barnett JP, Kouwen TR, Robinson C, and van Dijl JM (2012). High salinity growth conditions promote Tat-independent secretion of Tat substrates in Bacillus subtilis. Appl Environ Microbiol. 78, 7733-7744.
Barnett JP, Scanlan DJ, and Blindauer CA (2012). Protein fractionation and detection for metalloproteomics: challenges and approaches. Anal Bioanal Chem. 402, 3311-3322.
Barnett JP, Scanlan DJ, and Blindauer CA (2012). Fractionation and identification of metalloproteins from a marine cyanobacterium. Anal Bioanal Chem. 402, 3371-3377.
van der Ploeg R, Barnett JP, Vasisht N, Goosens VJ, Poether DC, Robinson C, and van Dijl JM (2011). Salt-sensitivity of minimal Twin-arginine translocases. J Biol Chem. 286, 43759-70.
Barnett JP, Robinson C, Scanlan DJ, and Blindauer CA (2011). The Tat protein export pathway and its role in cyanobacterial metalloprotein biosynthesis. FEMS Microbiol Lett. 325, 1-9.
Barnett JP, 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.
Barnett JP, van der Ploeg R, Eijlander RT, Nenninger A, Mendel S, Rozeboom R, Kuipers OP, 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.
Mendel S, McCarthy A, Barnett JP, Eijlander RT, Nenninger A, Kuipers OP, 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.
Barnett JP, Eijlander RT, Kuipers OP, 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.
Oates J, Barrett CM, Barnett JP, Byrne KG, 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.