Justin Bradley

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Phone3830
EmailJustin.Bradleyuea.acuk

2.24 Chemistry

1 Finished
1 Active

Spectroscopic and synthetic facilities for supramolecular and macromolecular systems
Le Brun, N., Beekman, A., Bidula, S., Bradley, J., Butt, J., Cammidge, A., Cheesman, M., Crack, J., Delso, I., Ganesan, A., Gates, A., Hamilton, C., Sachdeva, A., Searcey, M. & Wallace, M.
Engineering and Physical Sciences Research Council
1/01/25 → 30/06/26
Project: Research
Mechanistic studies of mitochondrial ferritin, a key player in iron mediated oxidative stress response and cellular iron metabolism
Le Brun, N., Bradley, J., Hemmings, A. & Moore, G.
Biotechnology and Biological Sciences Research Council
1/10/17 → 30/09/20
Project: Research

29 Article
2 Review article

Human mitochondrial ferritin exhibits highly unusual iron-O2 chemistry distinct from that of cytosolic ferritins
Bradley, J. M., Bugg, Z., Pullin, J., Moore, G. R., Svistunenko, D. A. & Le Brun, N. E., 23 Apr 2025, (Accepted/In press) In: Nature Communications.
Research output: Contribution to journal › Article › peer-review
Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins
Pullin, J., Rodríguez-Celma, J., Franceschetti, M., Mundy, J. E. A., Svistunenko, D. A., Bradley, J. M., Le Brun, N. E. & Balk, J., 2 Apr 2025, In: Nature Communications.
Research output: Contribution to journal › Article › peer-review
Observation of the assembly of the nascent mineral core at the nucleation site of human mitochondrial ferritin
Bradley, J. M., Bugg, Z., Moore, G. R., Hemmings, A. M. & Le Brun, N. E., 23 Apr 2025, In: Journal of the American Chemical Society. 147, 16, p. 13699–13710 12 p.
Research output: Contribution to journal › Article › peer-review

Open Access
File
The ferroxidase centre of Escherichia coli bacterioferritin plays a key role in the reductive mobilisation of the mineral iron core
Bradley, J. M., Bugg, Z., Sackey, A., Andrews, S. C., Wilson, M. T., Svistunenko, D. A., Moore, G. R. & Le Brun, N. E., 15 Apr 2024, In: Angewandte Chemie-International Edition. 63, 16, e202401379.
Research output: Contribution to journal › Article › peer-review

Open Access
File

1 Citation (Scopus)

6 Downloads (Pure)
Protein encapsulation within the internal cavity of a bacterioferritin
Bradley, J. M., Gray, E., Richardson, J., Moore, G. R. & Le Brun, N. E., 14 Sept 2022, In: Nanoscale. 14, 34, p. 12322-12331 10 p.
Research output: Contribution to journal › Article › peer-review

Open Access
File

4 Citations (Scopus)

23 Downloads (Pure)

Justin Bradley

Collaborations and top research areas from the last five years

Dive into details

Spectroscopic and synthetic facilities for supramolecular and macromolecular systems

Mechanistic studies of mitochondrial ferritin, a key player in iron mediated oxidative stress response and cellular iron metabolism

Human mitochondrial ferritin exhibits highly unusual iron-O2 chemistry distinct from that of cytosolic ferritins

Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins

Observation of the assembly of the nascent mineral core at the nucleation site of human mitochondrial ferritin

The ferroxidase centre of Escherichia coli bacterioferritin plays a key role in the reductive mobilisation of the mineral iron core

Protein encapsulation within the internal cavity of a bacterioferritin

Justin Bradley

Collaborations and top research areas from the last five years

Projects

Spectroscopic and synthetic facilities for supramolecular and macromolecular systems

Mechanistic studies of mitochondrial ferritin, a key player in iron mediated oxidative stress response and cellular iron metabolism

Research output

Human mitochondrial ferritin exhibits highly unusual iron-O2 chemistry distinct from that of cytosolic ferritins

Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins

Observation of the assembly of the nascent mineral core at the nucleation site of human mitochondrial ferritin

The ferroxidase centre of Escherichia coli bacterioferritin plays a key role in the reductive mobilisation of the mineral iron core

Protein encapsulation within the internal cavity of a bacterioferritin