Author

C. Porta

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:protein structure· 1 Organism:yeast· 1

Frequent Co-Authors

D. I. Stuart· 3 shared E. E. Fry· 3 shared K. Grehan· 3 shared L. Sherry· 3 shared M. W. Bahar· 3 shared N. J. Stonehouse· 3 shared A. J. Macadam· 2 shared D. J. Rowlands· 2 shared

Activity by Year

2022-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 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

3 shared papersMicrobiology

D. I. Stuart

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Risk-free polio vaccine: Recombinant expression systems for production of stabilised virus-like particles

L. Sherry, M. W. Bahar, C. Porta, H. Fox, K. Grehan, V. Nasta, H. M. Duyvesteyn, L. de Colibus, J. Marsian, I. Murdoch, D. Ponndorf, S.-R. Kim, S. Shah, S. Carlyle, J. J. Swanson, , D. J. Rowlands

This study produces stabilized poliovirus VLPs using recombinant systems, showing equivalent or better immunogenicity than current vaccines.

bioRxiv · May 13, 2024 · PreprintMicrobiology

Production and characterisation of stabilised PV-3 virus-like particles using Pichia pastoris

L. Sherry, K. Grehan, J. J. Swanson, M. W. Bahar, C. Porta, E. E. Fry, D. I. Stuart, D. Rowlands, N. J. Stonehouse

This paper produces and characterizes stabilized PV-3 virus-like particles using Pichia pastoris, showing improved thermostability and antigen ratio compared to wild-type PV-3.

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