Author

D. J. Rowlands

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

Biology Disciplines

Click to filter author papers

Microbiology· 3 Biochemistry· 1 Immunology· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 5 Research Focus:host-pathogen & immune response· 3 Assay:cryo-EM· 2 Organism:mouse· 2 Organism:yeast· 2 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

N. J. Stonehouse· 6 shared L. Sherry· 4 shared J. S. Snowden· 3 shared K. Grehan· 3 shared J. Alzahrani· 2 shared M. Stacey· 2 shared N. A. Ranson· 2 shared N. J. Kingston· 2 shared

Activity by Year

2021-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 39 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

6 shared papersMicrobiology

N. J. Stonehouse

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

Amino acid substitutions in norovirus VP1 dictate cell tropism via an attachment process dependent on membrane mobility.

J. T. Mills, S. C. Minogue, J. S. Snowden, K. E. Carnahan, D. J. Rowlands, N. J. Stonehouse, C. E. Wobus, M. R. Herod

This study identifies an amino acid substitution in norovirus VP1 that enhances cellular attachment and alters tropism by affecting receptor recruitment and membrane mobility.

bioRxiv · Feb 17, 2023 · PreprintMicrobiology

Development of Enterovirus anti-viral agents that target the viral 2C protein

R. Kejriwal, T. Evans, J. Calabrese, L. Swistak, L. Alexandrescu, M. Cohen, N. Rahman, N. Henriksen, R. C. Dash, K. Hadden, N. J. Stonehouse, D. J. Rowlands, N. J. Kingston, M. Hartnoll, S. Dobson, S. White

This study develops broad-spectrum anti-viral compounds targeting the conserved EV 2C protein, showing low IC50 values and suggesting a role for 2C in capsid assembly.

bioRxiv · Oct 6, 2022Pharmacology & Toxicology

Protease-independent production of poliovirus virus-like particles in Pichia pastoris: Implications for efficient vaccine development and insights into capsid assembly.

L. Sherry, J. J. Swanson, K. Grehan, H. Xu, M. Uchida, I. M. Jones, N. J. Stonehouse, D. J. Rowlands

This study produces protease-independent poliovirus VLPs in Pichia pastoris, showing they maintain native antigenicity and thermostability, suggesting potential for improved vaccine development.

bioRxiv · Sep 16, 2022Microbiology

A conserved glutathione binding site in poliovirus is a target for antivirals and vaccine stabilisation

M. W. Bahar, V. Nasta, H. Fox, L. Sherry, K. Grehan, C. Porta, A. J. Macadam, N. J. Stonehouse, D. J. Rowlands, E. E. Fry, D. I. Stuart

This study identifies a conserved glutathione binding site in poliovirus VLPs that can be targeted by antivirals and used to stabilize vaccines.

bioRxiv · Sep 8, 2022Biochemistry

VelcroVax: a bolt-on vaccine platform technology improves antibody titres against a viral glycoprotein in mice

N. J. Stonehouse, N. J. Kingston, K. Grehan, J. S. Snowden, M. Hassall, J. Alzahrani, G. C. Paesen, L. Sherry, C. R. Hayward, A. Roe, S. Stephen, D. C. Tomlinson, A. Zeltina, K. J. Doores, N. A. Ranson, , D. J. Rowlands

VelcroVax is a vaccine platform that enhances antibody titres against a viral glycoprotein in mice by combining a modified VLP with a SUMO-tagged antigen.

bioRxiv · Apr 22, 2022 · PreprintImmunology

Structural insight into Pichia pastoris fatty acid synthase

J. S. Snowden, J. Alzahrani, L. Sherry, M. Stacey, D. J. Rowlands, N. A. Ranson, N. J. Stonehouse

The paper determines the structure of P. pastoris fatty acid synthase using cryoEM, identifying structural differences from S. cerevisiae FAS and resolving the mobile ACP domain.

bioRxiv · Jan 27, 2021Microbiology