Author

J. Turnbull

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· 4 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:host-pathogen & immune response· 3 Organism:bacteria (other)· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

C. Mycroft-West· 4 shared E. Yates· 4 shared M. Guerrini· 4 shared A. Bisio· 3 shared D. Fernig· 3 shared D. Su· 3 shared G. Miller· 3 shared M. Lima· 3 shared

Activity by Year

2019-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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4 shared papersBiochemistry

C. Mycroft-West

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

In Vitro Evolution to Increase the Titers of Difficult Bacteriophages: Rapid Appelmans Protocol

D. N. Kok, J. Turnbull, N. Takeuchi, P. Tsourkas, H. L. Hendrickson

This paper presents two methods to increase bacteriophage titers, with the Rapid Appelmans Protocol (RAP) achieving faster and higher titer improvements in four days.

bioRxiv · Mar 2, 2023 · PreprintMicrobiology

Glycosaminoglycans induce conformational change in the SARS-CoV-2 Spike S1 Receptor Binding Domain.

C. Mycroft-West, D. Su, Y. Li, S. Guimond, T. Rudd, S. Elli, G. Miller, Q. Nunes, P. Procter, A. Bisio, N. Forsyth, J. Turnbull, M. Guerrini, D. Fernig, E. Yates, , M. Skidmore

This study shows that various glycosaminoglycans, beyond heparin, can induce conformational changes in the SARS-CoV-2 Spike S1 receptor binding domain.

bioRxiv · Apr 29, 2020 · PreprintBiochemistry

SARS-CoV-2 Spike S1 Receptor Binding Domain undergoes Conformational Change upon Interaction with Low Molecular Weight Heparins.

C. Mycroft-West, D. Su, Y. Li, S. Guimond, T. Rudd, S. Elli, G. Miller, Q. Nunes, P. Procter, A. Bisio, N. Forsyth, J. Turnbull, M. Guerrini, D. Fernig, E. Yates, , M. Skidmore

This study shows low molecular weight heparins induce conformational changes in SARS-CoV-2 Spike RBD, suggesting potential for repurposing as antiviral agents.

bioRxiv · Apr 29, 2020 · PreprintBiochemistry

Heparin inhibits cellular invasion by SARS-CoV-2: structural dependence of the interaction of the surface protein (spike) S1 receptor binding domain with heparin.

C. Mycroft-West, D. Su, I. Pagani, T. Rudd, S. Elli, S. Guimond, G. Miller, M. Meneghetti, H. Nader, Y. Li, Q. Nunes, P. Procter, N. Mancini, M. Clementi, A. Bisio, , M. A. Skidmore

This study shows heparin inhibits SARS-CoV-2 invasion by binding to the Spike protein's RBD and inducing conformational changes, with structural features of heparin playing a key role.

bioRxiv · Apr 28, 2020Biochemistry

Analysis of solid-state heparin samples by ATR-FTIR spectroscopy

A. Devlin, C. Mycroft-West, J. Turnbull, M. Guerrini, E. Yates, M. Skidmore

This paper proposes using ATR-FTIR spectroscopy with multivariate analysis to rapidly and cost-effectively monitor heparin purity and detect contaminants.

bioRxiv · Sep 19, 2019 · PreprintBiochemistry