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Inna S. Afonina
Researcher at Ghent University
Publications - 30
Citations - 2652
Inna S. Afonina is an academic researcher from Ghent University. The author has contributed to research in topics: Proinflammatory cytokine & Cytokine. The author has an hindex of 14, co-authored 24 publications receiving 2022 citations. Previous affiliations of Inna S. Afonina include Trinity College, Dublin.
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Journal ArticleDOI
Suppression of Interleukin-33 Bioactivity through Proteolysis by Apoptotic Caspases
Alexander U. Lüthi,Sean P. Cullen,Edel A. McNeela,Patrick J. Duriez,Inna S. Afonina,Clare Sheridan,Gabriela Brumatti,Rebecca C. Taylor,Kristof Kersse,Peter Vandenabeele,Ed C. Lavelle,Seamus J. Martin +11 more
TL;DR: It is shown that IL-33 was processed by caspases activated during apoptosis but was not a physiological substrate for caspasing associated with inflammation, and caspase-mediated proteolysis acts as a switch to dampen the proinflammatory properties of IL- 33.
Journal ArticleDOI
Limiting inflammation-the negative regulation of NF-κB and the NLRP3 inflammasome.
TL;DR: The key molecular mechanisms that contribute to the self-limiting nature of inflammatory signaling are discussed, with emphasis on the negative regulation of the NF-κB pathway and the NLRP3 inflammasome.
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Proteolytic Processing of Interleukin-1 Family Cytokines: Variations on a Common Theme
TL;DR: The identity of the proteases involved in the proteolytic processing of IL-1 family cytokines and the therapeutic implications in inflammatory disease are reviewed.
Journal ArticleDOI
Granzyme B-Dependent Proteolysis Acts as a Switch to Enhance the Proinflammatory Activity of IL-1α
Inna S. Afonina,Graham A. Tynan,Susan E. Logue,Sean P. Cullen,Michael Bots,Alexander U. Lüthi,Emer P. Reeves,Noel G. McElvaney,Jan Paul Medema,Ed C. Lavelle,Seamus J. Martin +10 more
TL;DR: It is shown that IL-1α is a substrate for granzyme B and that proteolysis potently enhanced the biological activity of this cytokine in vitro as well as in vivo, and granzymes B-processed IL- 1α exhibited more potent activity as an immunoadjuvant in–vivo.
Journal ArticleDOI
Neutrophil-Derived Proteases Escalate Inflammation through Activation of IL-36 Family Cytokines.
Conor M. Henry,Graeme P. Sullivan,Danielle M. Clancy,Inna S. Afonina,Dagmar Kulms,Seamus J. Martin +5 more
TL;DR: Neutrophil granule proteases are identified as potent IL-36-activating enzymes, adding to the understanding of how neutrophils escalate inflammatory reactions, and inhibition of neutrophil-derived proteases may have therapeutic benefits in psoriasis.