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Articles by Sofia Rossini
Monovalent pseudo-natural products supercharge degradation of IDO1 by its native E3 KLHDC3 - Nature Chemistry
Abstract Targeted protein degradation modulates protein function beyond the inhibition of enzyme activity or protein–protein interactions. Most degrader drugs function by directly mediating the proximity between a neosubstrate and a hijacked E3 ligase. Here we identify pseudo-natural products derived from (−)-myrtanol, termed iDegs, that inhibit and induce degradation of the immunomodulatory enzyme indoleamine-2,3-dioxygenase 1 (IDO1) by a distinct mechanism.
A back-door insights into the modulation of Src kinase activity by the polyamine spermidine
Accepted manuscript, PDF only. Full online edition to follow. Author Accepted Manuscript PDF only version. The full online version will follow soon. Accepted Manuscript published June 30, 2023 (This version) Accepted June 28, 2023 Received December 29, 2022 Share this article Cite this article A back-door insights into the modulation of Src kinase activity by the polyamine spermidine eLife 12:e85872.
A Back-Door Insights into the modulation of Src kinase activity by the polyamine spermidine
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V Region of IgG Controls the Molecular Properties of the Binding Site for Neonatal Fc Receptor
Sofia Rossini, Rémi Noé, Victoria Daventure, Maxime Lecerf, Sune Justesen and Jordan D. Dimitrov J Immunol November 15, 2020, 205 (10) 2850-2860; DOI: https://doi.org/10.4049/jimmunol.2000732 Key Points IgG1 Abs with different V regions bind to FcRn with different affinity.
Polyamines and Kynurenines at the Intersection of Immune Modulation
Highlights Polyamines (i.e., putrescine, spermidine, and spermine) are bioactive polycations derived from the decarboxylation of ʟ-ornithine catalyzed by ornithine decarboxylase (ODC). Emerging data suggest that spermidine exerts anti-inflammatory/immunoregulatory effects; it can protect mice from experimental autoimmune encephalomyelitis and imiquimod-induced psoriasis.
V Region of IgG Controls the Molecular Properties of the Binding Site for Neonatal Fc Receptor
Sofia Rossini, Rémi Noé, Victoria Daventure, Maxime Lecerf, Sune Justesen and Jordan D. Dimitrov J Immunol October 19, 2020, ji2000732; DOI: https://doi.org/10.4049/jimmunol.2000732 Key Points IgG1 Abs with different V regions bind to FcRn with different affinity. The V region of IgG1 dictates the mechanism of molecular recognition by FcRn. Formation of immune complexes modifies the mechanism of IgG binding to FcRn. Abstract Neonatal Fc receptor (FcRn) has a key role in the homeostasis of IgG.
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