M
Matilde Forcella
Researcher at University of Milano-Bicocca
Publications - 56
Citations - 805
Matilde Forcella is an academic researcher from University of Milano-Bicocca. The author has contributed to research in topics: Trehalase & Chironomus riparius. The author has an hindex of 15, co-authored 48 publications receiving 615 citations. Previous affiliations of Matilde Forcella include University of Milan.
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Journal ArticleDOI
Human sialidase NEU4 long and short are extrinsic proteins bound to outer mitochondrial membrane and the endoplasmic reticulum, respectively
Alessandra Bigi,Lavinia Morosi,Chiara Pozzi,Matilde Forcella,Guido Tettamanti,Bruno Venerando,Eugenio Monti,Paola Fusi +7 more
TL;DR: Protein extraction with Triton X-114 and sodium carbonate and cross-linking experiments demonstrate that both forms of NEU4 are extrinsic membrane proteins, anchored via protein-protein interactions, and mitochondria subfractionation experiments suggest thatNEU4 long is bound to the outer mitochondrial membrane.
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NEU3 activity enhances EGFR activation without affecting EGFR expression and acts on its sialylation levels
Alessandra Mozzi,Matilde Forcella,Alice Riva,Carlotta Difrancesco,Francesca Molinari,Vittoria Martin,Nadia Papini,Barbara Bernasconi,Simona Nonnis,Gabriella Tedeschi,Luca Mazzucchelli,Eugenio Monti,Paola Fusi,Milo Frattini +13 more
TL;DR: The data demonstrate that, besides the already reported indirect EGFR activation through GM3, sialidase NEU3 could also play a role on EGFRactivation through its desialylation.
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Identification of a bacteriocin-like compound from Lactobacillus plantarum with antimicrobial activity and effects on normal and cancerogenic human intestinal cells
Alessandra De Giani,Federica Bovio,Matilde Forcella,Paola Fusi,Guido Sello,Patrizia Di Gennaro +5 more
TL;DR: In conclusion, plantaricin P1053 isolated from L. plantarum PBS067 strain could represent one of the first multifunctional bacteriocin-like compound acting on human epithelial intestinal cells.
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Structure–Activity Relationship in Monosaccharide-Based Toll-Like Receptor 4 (TLR4) Antagonists
Fabio A. Facchini,Lenny Zaffaroni,Alberto Minotti,Silvia Rapisarda,Valentina Calabrese,Matilde Forcella,Paola Fusi,Cristina Airoldi,Carlotta Ciaramelli,Jean-Marc Billod,Andra B Schromm,Harald Braun,Charys Palmer,Rudi Beyaert,Fabio Lapenta,Roman Jerala,Grisha Pirianov,Sonsoles Martín-Santamaría,Francesco Peri +18 more
TL;DR: Fourier-transform infrared, nuclear magnetic resonance, and small angle X-ray scattering measurements suggested that the aggregation state in aqueous solution depends on fatty acid chain lengths and that this property can influence TLR4 activity in this series of compounds.
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Casuarine-6-O-α-D-glucoside and its analogues are tight binding inhibitors of insect and bacterial trehalases
Francesca Cardona,Andrea Goti,Camilla Parmeggiani,Paolo Parenti,Matilde Forcella,Paola Fusi,Laura Cipolla,Shirley M. Roberts,Gideon J. Davies,Tracey M. Gloster +9 more
TL;DR: Two novel casuarine-6-alpha-D-glucoside analogues were synthesized and tested as inhibitors towards Chironomus riparius, mammalian pig kidney and Escherichia coli trehalases, and their potent and selective activity is promising for the development of new insecticides.