Author

N. A. Borg

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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Biochemistry· 3 Immunology· 2

Signature Assays, Organisms & Methods

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Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Organism:plant (other)· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Approach:statistical model· 2 Assay:structural biology· 2 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

A. M. Buckle· 4 shared B. T. Riley· 3 shared I. Kass· 3 shared J. Fodor· 2 shared N. Drinkwater· 2 shared S. C. Atkinson· 2 shared S. McGowan· 2 shared T. R. Malcolm· 2 shared

Activity by Year

2018-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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4 shared papersImmunology

A. M. Buckle

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Metal Dependent Dynamic Equilibrium: A Regulatory Mechanism for M17 Aminopeptidases from Plasmodium falciparum and Plasmodium vivax

T. R. Malcolm, M. J. Belousoff, H. Venugopal, N. A. Borg, N. Drinkwater, S. C. Atkinson, S. McGowan

This study identifies a metal-dependent dynamic equilibrium in M17 aminopeptidases from Plasmodium species that regulates hexamer formation and catalytic activity.

bioRxiv · Oct 8, 2020 · PreprintBiochemistry

The Role of Conformational Dynamics in Abacavir-Induced Hypersensitivity Syndrome

J. Fodor, B. T. Riley, I. Kass, A. M. Buckle, N. A. Borg

This study uses molecular dynamics to show abacavir alters peptide conformations bound to HLA-B*57:01, influencing immune self-reactivity and hypersensitivity.

bioRxiv · Feb 27, 2019Immunology

A metal-dependent switch moderates activity of the hexameric M17 aminopeptidases.

N. Drinkwater, W. Yang, B. T. Riley, B. K. Hayes, K. Kannan Sivaraman, T. R. Malcolm, S. C. Atkinson, N. A. Borg, I. Kass, A. M. Buckle, S. McGowan

This study identifies a metal-dependent regulatory mechanism in PfA-M17 aminopeptidase, showing how oligomerization and metal center re-modelling control proteolytic activity.

bioRxiv · Feb 21, 2019 · PreprintBiochemistry

Structural Capacitance in Protein Evolution and Human Diseases

C. Li, L. V. Clark, R. Zhang, B. T. Porebski, J. M. McCoey, N. A. Borg, G. I. Webb, I. Kass, M. Buckle, J. Song, A. Woolfson, A. M. Buckle

The paper identifies structural capacitance as a new mechanism in protein evolution that generates microstructure in disordered regions, linking it to disease and evolutionary adaptability.

bioRxiv · Feb 22, 2018Biochemistry

Previously Hidden Dynamics at the TCR-pMHC Interface Revealed

J. Fodor, B. T. Riley, N. A. Borg, A. M. Buckle

The paper reveals hidden conformational dynamics in TCR-pMHC interactions using ensemble refinement of X-ray crystallographic data, enhancing functional interpretations of immune responses.

bioRxiv · Feb 21, 2018Immunology