Author

Piet Gros

Utrecht UniversityORCID 0000-0002-7782-2585Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 2 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Assay:protein structure· 2 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

Annemiek B. van SprieliD· 1 shared Bart W. BardoeliD· 1 shared Dani A. C. HeesterbeekiD· 1 shared Danique Y. SiereiD· 1 shared Douwe J. DijkstraiD· 1 shared Elisa LamottkeiD· 1 shared Eric G. HuizingaiD· 1 shared Eva M. StruijfiD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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Focal author (center)Selected co-authorORCID co-authorUnlinked name

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1 shared paperBiochemistry

Annemiek B. van SprielORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Identification of a C3b-specific nanobody that does not bind C3 and blocks alternative pathway convertases

Eva M. Struijf, Bart W. Bardoel, Joanne E. van Keulen, Maartje Ruyken, Danique Y. Siere, Douwe J. Dijkstra, Gillian Dekkers, Piet Gros, Raimond Heukers, Dani A. C. Heesterbeek, Suzan H. M. Rooijakkers, Jamie S. Depelteau

This study identifies a C3b-specific nanobody that binds C3b but not C3, and inhibits the alternative pathway convertases of the complement system.

bioRxiv · Sep 3, 2026 · PreprintImmunology

Structural insights into C3 convertase activity of the classical pathway of complement

Karla I. De la O Becerra, T. Harma C. Brondijk, Itziar Serna Martin, Piet Gros

The paper presents cryo-EM structures of classical pathway complement convertases and their substrate complex, revealing mechanisms of C3 cleavage and opsonin production.

Nature Communications · Dec 18, 2025Peer-reviewedBiochemistry

Tetraspanin CD82 reduces the formation of CADM1 oligomers

Elisa Lamottke, Harry M. Warner, Sjoerd J. van Deventer, Fabian Schwerdtfeger, Linde Lanting, Eric G. Huizinga, Annemiek B. van Spriel, Piet Gros

This study shows CD82 reduces CADM1 oligomer formation by interacting with its extracellular domains, affecting transmembrane helix spacing and disrupting cell adhesion.

bioRxiv · Dec 15, 2025 · PreprintBiochemistry