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Ivano Eberini
Researcher at University of Milan
Publications - 153
Citations - 5058
Ivano Eberini is an academic researcher from University of Milan. The author has contributed to research in topics: Chemistry & Receptor. The author has an hindex of 37, co-authored 142 publications receiving 4554 citations. Previous affiliations of Ivano Eberini include Mario Negri Institute for Pharmacological Research & Imperial College London.
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Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes.
Maddalena Fratelli,Hans Demol,Magda Puype,Simona Casagrande,Ivano Eberini,Mario Salmona,Valentina Bonetto,Manuela Mengozzi,Francis Duffieux,Emeric Miclet,Angela Bachi,Joël Vandekerckhove,Elisabetta Gianazza,Pietro Ghezzi +13 more
TL;DR: It is suggested that enolase and cyclophilin are heavily glutathionylated under basal conditions and might be a common mechanism for the global regulation of protein functions.
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Glutathionylation of human thioredoxin: A possible crosstalk between the glutathione and thioredoxin systems
Simona Casagrande,Valentina Bonetto,Maddalena Fratelli,Elisabetta Gianazza,Ivano Eberini,Tania Massignan,Mario Salmona,Geng Chang,Arne Holmgren,Pietro Ghezzi +9 more
TL;DR: The intracellular glutathione/glutathione disulfide ratio, an indicator of the redox state of the cell, can regulate Trx functions reversibly through thiol-disulfide exchange reactions, suggesting a process of autoactivation due to the ability of Trx to de-glutATHionylate itself.
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Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells
Maddalena Fratelli,Hans Demol,Magda Puype,Simona Casagrande,Pia Villa,Ivano Eberini,Joël Vandekerckhove,Elisabetta Gianazza,Pietro Ghezzi +8 more
TL;DR: To identify proteins undergoing glutathionylation in primary rat hepatocytes and in human HepG2 hepatoma cells, radiolabeled the intracellular GSH pool with L‐[35S] cysteine and separated proteins by two‐dimensional gel electrophoresis under nonreducing conditions.
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The oxysterol–CXCR2 axis plays a key role in the recruitment of tumor-promoting neutrophils
Laura Raccosta,Raffaella Fontana,Daniela Maggioni,Claudia Lanterna,Eduardo J. Villablanca,Aida Paniccia,Andrea Musumeci,Elena Chiricozzi,Maria Letizia Trincavelli,Simona Daniele,Claudia Martini,Jan-Åke Gustafsson,Jan-Åke Gustafsson,Claudio Doglioni,Safiyè Gonzalvo Feo,Andrea Leiva,Maria Grazia Ciampa,Laura Mauri,Cristina Sensi,Alessandro Prinetti,Ivano Eberini,J. Rodrigo Mora,Claudio Bordignon,Claudio Bordignon,Knut R. Steffensen,Sandro Sonnino,Silvano Sozzani,Catia Traversari,Vincenzo Russo +28 more
TL;DR: Tumor-derived oxysterols recruit protumor neutrophils in an LXR-independent, CXCR2-dependent manner, thus favoring tumor growth by promoting neoangiogenesis and immunosuppression.
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The Molecular Basis of Lecithin:Cholesterol Acyltransferase Deficiency Syndromes: A Comprehensive Study of Molecular and Biochemical Findings in 13 Unrelated Italian Families
Laura Calabresi,Livia Pisciotta,Anna Costantin,Ilaria Frigerio,Ivano Eberini,Paola Alessandrini,Marcello Arca,Gabriele Bittolo Bon,Giuliano Boscutti,Busnach G,Giovanni M. Frascà,Loreto Gesualdo,Maddalena Gigante,Graziana Lupattelli,Anna Montali,Stefano Pizzolitto,Ivana Rabbone,M. Rolleri,Giacomo Ruotolo,Tiziana Sampietro,Adalberto Sessa,Gaetano Vaudo,Alfredo Cantafora,Fabrizio Veglia,Sebastiano Calandra,Stefano Bertolini,Guido Franceschini +26 more
TL;DR: In a large series of subjects carrying mutations in the LCAT gene, the inheritance of a mutated LCAT genotype causes a gene–dose-dependent alteration in the plasma lipid/lipoprotein profile, which is remarkably similar between subjects classified as FLD or FED.