Author

I. Goodfellow

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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Microbiology· 6 Biochemistry· 2 Evolutionary Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:host-pathogen & immune response· 5 Research Focus:cell type annotation· 3 Organism:human· 3 Organism:mouse· 3 Assay:proteomics· 3 Approach:statistical model· 3 Research Focus:cell signaling & trafficking· 2

Frequent Co-Authors

M. Hosmillo· 5 shared A. S. Jahun· 3 shared E. Emmott· 2 shared F. Sorgeloos· 2 shared J. Lu· 2 shared N. Locker· 2 shared A. Albecka· 1 shared A. Cuvry· 1 shared

Activity by Year

2017-2024 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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5 shared papersMicrobiology

M. Hosmillo

Mutual co-authors in cluster

Author profile →

9 papers

Recent·Most cited

Variable rates of SARS-CoV-2 evolution in chronic infections

E. Smith, W. L. Hamilton, B. Warne, E. R. Walker, A. S. Jahun, M. Hosmillo, ISARIC Consortium, R. K. Gupta, I. Goodfellow, E. Gkrania-Klotsas, M. E. Torok, C. J. R. Illingworth

This study analyzes within-host SARS-CoV-2 evolution in chronic infections, finding variable rates of evolution and evidence of subpopulation structure.

bioRxiv · May 31, 2024Evolutionary Biology

TRIM7 restricts Coxsackievirus and norovirus infection by detecting the C-terminalglutamine generated by 3C protease processing

J. Luptak, D. Mallery, A. S. Jahun, A. Albecka, D. Clift, O. Ather, G. Slodkowicz, I. Goodfellow, L. James

The paper identifies TRIM7 as a viral restriction factor that recognizes a conserved C-terminal glutamine motif generated by viral proteases, inhibiting Coxsackie and norovirus replication.

bioRxiv · Jun 28, 2022Biochemistry

A thermostable, closed, SARS-CoV-2 spike protein trimer.

X. Xiong, K. Qu, K. A. Ciazynska, M. Hosmillo, A. P. Carter, S. Ebrahimi, Z. Ke, S. H. W. Scheres, L. Bergamaschi, G. L. Grice, Y. Zhang, The CITIID-NIHR COVID-19 BioResource Collaboration, J. A. Nathan, S. Baker, L. C. James, , J. A. G. Briggs

This paper designs a thermostable, closed SARS-CoV-2 spike protein trimer that remains in the pre-fusion state and can be used in serological assays.

bioRxiv · Jun 15, 2020Biochemistry

Murine norovirus virulence factor 1 (VF1) protein contributes to viral fitness during persistent infection

C. Borg, A. S. Jahun, L. Thorne, F. Sorgeloos, D. Bailey, I. Goodfellow

This study shows that VF1 in MNV contributes to viral fitness during persistent infection but is not essential for persistence.

bioRxiv · May 23, 2019Microbiology

Noroviruses subvert the core stress granule component G3BP1 to promote viral VPg-dependent translation.

M. Hosmillo, J. Lu, M. R. McAllaster, J. B. Eaglesham, X. Wang, E. Emmott, P. Domingues, Y. Chaudhry, T. J. Fitzmaurice, M. K. H. Tung, M. Panas, G. McInerney, N. Locker, C. B. Willen, I. Goodfellow

This study identifies G3BP1 as a host factor essential for norovirus infection and reveals its role in VPg-dependent translation initiation.

bioRxiv · Mar 8, 2019Microbiology

A robust human norovirus replication model in zebrafish larvae

J. Van Dycke, A. Ny, N. Conceicao-Neto, J. Maes, M. Hosmillo, A. Cuvry, I. Goodfellow, T. C. de Araujo Nogueira, E. Verbeken, J. Matthijnssens, P. de Witte, J. Neyts, J. Rocha-Pereira

This study establishes a zebrafish larval model for human norovirus replication, showing high viral titers and antiviral response potential.

bioRxiv · Jan 23, 2019Microbiology

Epigenetic suppression of interferon lambda receptor expression leads to enhanced HuNoV replication in vitro

S. E. Arthur, F. Sorgeloos, M. Hosmillo, I. Goodfellow

This study identifies epigenetic suppression of IFNLR1 as a mechanism enhancing HuNoV replication in vitro by reducing antiviral interferon lambda signaling.

bioRxiv · Jan 21, 2019Microbiology

Norovirus infection results in assembly of virus-specific G3BP1 granules and evasion of eIF2α signaling.

M. Brocard, V. Iadevaia, P. Klein, B. Hall, G. Lewis, J. Lu, J. Burke, R. Parker, A. Ruggieri, I. Goodfellow, N. Locker

This study shows that norovirus infection leads to the formation of virus-specific granules and disrupts eIF2α signaling to evade host stress responses.

bioRxiv · Dec 10, 2018 · PreprintMicrobiology

Spatial and temporal control of norovirus protease activity is determined by polyprotein processing and intermolecular interactions within the viral replication complex.

E. Emmott, A. de Rougemont, J. Haas, I. Goodfellow

This study investigates how norovirus protease activity is regulated by polyprotein processing and intermolecular interactions within the replication complex, showing that precursor forms are active in vitro but their activity in cells depends on localization and substrate access.

bioRxiv · Aug 11, 2017Microbiology