Author

T. E. Mollnes

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· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

A. Lawson· 1 shared A. Macpherson· 1 shared B. A. Spicer· 1 shared B. H. T. Ho· 1 shared B. Holmes· 1 shared C. Bayly-Jones· 1 shared C. J. Lupton· 1 shared C. Lau· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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1 shared paperImmunology

A. Lawson

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2 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

The allosteric modulation of Complement C5 by knob domain peptides

A. Macpherson, M. Laabei, Z. Ahdash, M. A. Graewert, J. Birtley, S. Schulze, S. Crennell, S. Robinson, B. Holmes, V. Oleinikovas, P. H. Nilsson, J. Snowden, V. Ellis, T. E. Mollnes, C. M. Deane, , J. van den Elsen

This study shows that knob domain peptides modulate complement C5 through allosteric mechanisms, revealing new therapeutic inhibitors and introducing knob domains as low molecular weight antibody fragments.

bioRxiv · Oct 24, 2020Immunology