Author

Kyle T. Cunningham

University of GlasgowORCID 0000-0002-2171-0277Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Organism:mouse· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:proteomics· 1

Frequent Co-Authors

Ananya MukundaniD· 2 shared Andrew P. HinckiD· 2 shared Christina SchoenherriD· 2 shared Cynthia S. HinckiD· 2 shared Gareth J. InmaniD· 2 shared M. A. H. van DintheriD· 2 shared Madeleine P. J. WhiteiD· 2 shared Peter ten DijkeiD· 2 shared

Activity by Year

2024-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersBiochemistry

Ananya MukundanORCID

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2 papers

Recent·Most cited

BiochemistryNature CommunicationsPeer-reviewedFeb 21, 2025

TGM6, a helminth secretory product, mimics TGF-β binding to TβRII to antagonize TGF-β signaling in fibroblasts

Stephen E. White, Tristin A. Schwartze, Ananya Mukundan…·Andrew P. Hinck

This paper shows TGM6, a helminth protein, mimics TGF-β binding to TβRII to inhibit TGF-β signaling in fibroblasts but not T cells.

16 citations

mouseproteomics

𝕏 PostBluesky

ImmunologyEMBO ReportsPeer-reviewedNov 28, 2024

The helminth TGF-beta mimic TGM4 is a modular ligand that binds CD44, CD49d and TGF-beta receptors to preferentially target myeloid cells

Shashi Prakash Singh, Danielle J. Smyth, Kyle T. Cunningham…·Rick M. Maizels

This paper identifies TGM4, a helminth TGF-beta mimic, as a modular ligand that selectively targets myeloid cells through specific receptor interactions, differing from TGM1's broader T cell targeting.

12 citations

mouseexperimental assay

𝕏 PostBluesky