Author

B. D. Bax

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Biochemistry· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 3 Assay:protein structure· 3 Research Focus:protein structure prediction· 3 Research Focus:protein folding & dynamics· 1 Assay:structural biology· 1

Frequent Co-Authors

J. R. Atack· 2 shared K. T. Elvers· 2 shared M. Lipka-Lloyd· 2 shared A. J. Warren· 1 shared C. R. Koulouris· 1 shared E. Mahenthiralingam· 1 shared G. D. Fenn· 1 shared H. Morgan· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersBiophysics

J. R. Atack

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Author profile →

4 papers

Recent·Most cited

A 2.8A structure of zoliflodacin in a DNA-cleavage complex with Staphylococcus aureus DNA gyrase

H. Morgan, M. Lipka-Lloyd, A. J. Warren, N. Hughes, J. Holmes, N. P. Burton, E. Mahenthiralingam, B. D. Bax

This paper reports the 2.8Å X-ray structure of zoliflodacin bound to Staphylococcus aureus DNA gyrase, showing its mechanism of DNA cleavage inhibition and improved antibacterial activity.

bioRxiv · Nov 30, 2022 · PreprintBiophysics

Structures of the Human SPAK and OSR1 Conserved C-Terminal (CCT) Domains

K. T. Elvers, M. Lipka-Lloyd, R. C. Trueman, B. D. Bax, Y. Mehellou

The paper determines the crystal structures of human SPAK and OSR1 CCT domains and measures their binding affinity to a WNK4 peptide, providing a basis for designing inhibitors targeting SPAK-activation.

bioRxiv · Aug 19, 2021Biochemistry

Tyrosine 121 moves revealing a druggable pocket that couples catalysis to ATP-binding in serine racemase

C. R. Koulouris, S. E. Gardiner, T. K. Harris, K. T. Elvers, S. M. Roe, J. A. Gillespie, S. E. Ward, O. Grubisha, R. A. Nicholls, J. R. Atack, B. D. Bax

The paper identifies a druggable pocket involving Tyr121 that couples catalysis to ATP-binding in serine racemase by analyzing structural changes in closed and open enzyme forms.

bioRxiv · Feb 12, 2021 · PreprintBiophysics

Crystallization and structure of ebselen bound to cysteine 141 of human inositol monophosphatase (IMPase).

G. D. Fenn, H. Waller-Evans, J. R. Atack, B. D. Bax

The paper presents the 1.47 Å crystal structure of human IMPase bound to ebselen, showing covalent attachment to Cys141 and tetramer formation through dimer interactions.

bioRxiv · Jul 8, 2020 · PreprintPharmacology & Toxicology