Nica Borgese
University of Milan
90 Papers
1.2K Citations
Nica Borgese is an academic researcher from University of Milan. The author has contributed to research in topics: Endoplasmic reticulum & Membrane protein. The author has an hindex of 40, co-authored 88 publications. Previous affiliations of Nica Borgese include Magna Græcia University & Harvard University.
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Papers
Activation of the Endothelial Nitric-oxide Synthase by Tumor Necrosis Factor-α A NOVEL FEEDBACK MECHANISM REGULATING CELL DEATH
TL;DR: The results identify a novel mechanism of regulation of a signal transduction pathway activated by death receptors and suggest that NO may constitute a built-in mechanism by which TNF-α controls its own apoptotic program.
Cell culture models to investigate the selective vulnerability of motoneuronal mitochondria to familial ALS-linked G93ASOD1.
Andrea Raimondi,Alessandra Mangolini,M. Rizzardini,Silvia Tartari,Silvia Massari,Caterina Bendotti,Maura Francolini,Nica Borgese,Lavinia Cantoni,Grazia Pietrini +9 more
TL;DR: The results suggest that mitochondrial vulnerability of motoneurons to G93ASOD1 is recapitulated in NSC‐34 cells, and that peculiar features in network dynamics may account for the selective alterations of mot oneuronal mitochondria.
Unassisted translocation of large polypeptide domains across phospholipid bilayers
TL;DR: It is reported that surprisingly long domains of different sequence and charge placed downstream of b5's TMD can posttranslationally translocate into mammalian microsomes and liposomes at nanomolar nucleotide concentrations and are relevant to membrane evolution, biogenesis, and physiology.
The Ways of Tails: the GET Pathway and more
TL;DR: A review of the state of the field of this targeting route considers the lessons provided by the in vivo analysis of the pathway in different model organisms and by the consideration of its full client spectrum in more recent studies.
The specific subcellular localization of two isoforms of cytochrome b5 suggests novel targeting pathways.
TL;DR: The subcellular distribution of microsomal cytochrome b5 is more restricted than previously thought, suggesting that novel posttranslational targeting mechanisms direct it to the endoplasmic reticulum.