Dr James Barnett

Lecturer in Biomedical Sciences

School of Health Sciences

Email:: james.barnett@bcu.ac.uk

Dr Barnett joined BCU in 2019, and enjoys teaching on the Biomedical Sciences degree course. He is passionate about science and has had a varied career spending time working in both industry and academia. He has worked on numerous research projects investigating topics such as bacterial protein transport, metalloproteomics, and the rapid diagnosis of infectious diseases. Dr Barnett's research at Birmingham City University will be focussed on understanding how pathogenic bacteria acquire essential metal nutrients such as zinc, including at the host-pathogen interface.

Areas of Expertise

Qualifications

Memberships

Teaching

Research

Publications

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.