You have no saved courses.
It's simple, just look for the 'save this course' buttons when viewing course search results, listings or details.
Saving courses allow you to compare them, it also allows you to create a permanent list of 'favourites' that will always be there when you visit our site.
James Barnett is an Associate Professor of Life Sciences and Professional Academic Lead for Biomedical Science. He graduated from the University of Sheffield in 2000 with a BSc (Hons) in Biochemistry and Genetics and began his career at The Binding Site Ltd, working in the Monoclonal Antibodies Department.
In 2002, James joined the research group of Professor Colin Robinson at the University of Warwick, where he investigated the mechanisms of protein transport in bacteria, with a particular focus on the twin-arginine translocation (Tat) pathway. He completed his PhD in Life Sciences at Warwick in 2009 before moving to the Department of Chemistry as a postdoctoral research fellow in Professor Claudia Blindauer’s group. There, his research explored the zinc requirements of marine cyanobacteria using biochemical, molecular, and proteomic approaches.
In 2014, James transitioned to the biotechnology sector, joining Micropathology Ltd, a specialist biomedical sciences company focused on the rapid diagnosis of infectious diseases. During this time, he developed, validated, and applied PCR-based diagnostic tests for the detection of viral pathogens in clinical specimens.
James returned to higher education in 2019 when he joined Birmingham City University. Since then, he has played a leading role in the development and delivery of biomedical science courses, supporting students across undergraduate and postgraduate programmes. His expertise spans microbiology, molecular biology, biochemistry, and biomedical diagnostics, underpinned by experience gained across academic research, commercial biotechnology, and clinical diagnostics.
BSc (Hons) Biomedical Science
James' research focuses on understanding how bacterial pathogens adapt to and survive within challenging host environments, with a particular emphasis on the acquisition and utilisation of essential trace metals during infection. His work investigates the molecular mechanisms underpinning bacterial pathogenesis, antimicrobial resistance, and host-pathogen interactions.
Current research explores the role of metal homeostasis systems in clinically important opportunistic pathogens, including members of the Burkholderia cepacia complex. His group is investigating the mechanisms of zinc acquisition, trafficking, and regulation in Burkholderia cenocepacia, with the aim of understanding how metal availability influences bacterial fitness, virulence, and persistence within the host.
A second major theme of James' research is the identification and validation of novel antimicrobial targets. By characterising bacterial metal homeostasis pathways and their contribution to infection, his work seeks to develop new strategies to combat antimicrobial resistance and improve the treatment of chronic and difficult-to-treat infections.
He actively collaborates with academic and healthcare partners and is committed to providing research opportunities that enable undergraduate and postgraduate students to contribute to impactful biomedical research.
Ahmad F, Barnett JP, Bienemann A, Janes CA, Theobald P (2026). Quantifying regional and age-dependent microstructural changes in porcine ventricles from neonatal to adulthood using DT-MRI and TPEF-SHG microscopy. Ann Biomed Eng. 54, 3888-3915.
Barnett JP (2023). Transcriptional response of Burkholderia cenocepacia to severe zinc depletion. British Journal of Biomedical Science 80DOI: 10.3389/bjbs.2023.11597
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.
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.
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. BBA. 1830 5456-5464.
Van der Ploeg, Monterferrante CG, Piersma S, Barnett JP, Kouwen TRHM, Robinson C, and van Dilj, JM (2012). High salinity growth conditions promote Tat-independent secretion of Tat substrates in Bacillus subtilis. Appl Environ Microbiol 78 7733-7744.
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.
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, 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, Pother DC, Robinson C, and van Dijl JM (2011). Salt Sensitivity of Minimal Twin Arginine Translocases. 286 43759-43770.
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, Robinson C, Scanlan DJ, and Blindauer CA (2011). The Tat protein export pathway and its role in cyanobacterial metalloprotein biosynthesis. FEMS Microbio Lett. 325 1-9.
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, 661-672.
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 CML, 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.
LinkedIn
Recent searches
No recent searches
Popular searches
Suggested searches