Author

C. J. Lupton

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

Biochemistry· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:cryo-EM· 3 Approach:experimental assay· 3 Organism:human· 3 Research Focus:protein structure prediction· 3 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

C. Bayly-Jones· 3 shared H. Venugopal· 3 shared J. C. Whisstock· 3 shared L. D'Andrea· 2 shared A. de Marco· 1 shared A. M. Ellisdon· 1 shared B. A. Spicer· 1 shared B. H. T. Ho· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 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 papersBiochemistry

C. Bayly-Jones

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

The neoepitope of the complement C5b-9 Membrane Attack Complex is formed by proximity of adjacent ancillary regions of C9

C. Bayly-Jones, B. H. T. Ho, C. Lau, E. W. W. Leung, L. D'Andrea, C. J. Lupton, S. M. Ekkel, H. Venugopal, J. C. Whisstock, T. E. Mollnes, B. A. Spicer, M. A. Dunstone

This study identifies the discontinuous quaternary neoepitope of the C9 protein in the complement C5b-9 complex using cryo-EM, revealing its formation through adjacent domains without major conformational changes.

bioRxiv · Jul 6, 2022 · PreprintBiochemistry

Helical ultrastructure of the oncogenic metalloprotease meprin α in complex with a small molecule hydroxamate inhibitor

C. Bayly-Jones, C. J. Lupton, C. Fritz, H. Venugopal, D. Ramsbeck, M. Wermann, C. Jager, A. de Marco, S. Schilling, D. Schlenzig, J. C. Whisstock

This study determines the high-resolution structure of meprin α, revealing its helical assembly and interactions with an inhibitor and fetuin-B, showing oligomerization enhances stability without affecting activity.

bioRxiv · Mar 13, 2022 · PreprintBiochemistry

The cryo-EM structure of the neurofibromin dimer reveals the molecular basis for von Recklinghausen disease

C. J. Lupton, C. Bayly-Jones, L. D'Andrea, C. Huang, R. B. Schittenhelm, H. Venugopal, J. C. Whisstock, M. L. Halls, A. M. Ellisdon

This paper determines the cryo-EM structure of full-length NF1, revealing its autoinhibited conformation and providing insights into disease mechanisms and therapeutic strategies.

bioRxiv · Feb 18, 2021 · PreprintBiochemistry