Spettrometro di massa Orbitrap Fusion
spettrometro di massa ad altissima risoluzione basato sulla tecnologia Orbitrap
Edificio
U28; 4; 4023
Dipartimento
Responsabile scientifico
Voci tariffario
MS.01; MS.02A; MS.02C; MS.03B; MS.04; MS.05A; MS.05B; MS.05C; MS.06; MS.07; MS…
Sito tariffario
Sito Web
Immagine

Pubblicazioni
- Santambrogio, C; Ponzini, E; Grandori, R (2022) Native mass spectrometry for the investigation of protein structural (dis)order. Dettaglio
- Ponzini, E; Santambrogio, C; De Palma, A; Mauri, P; Tavazzi, S; Grandori, R (2022) Mass spectrometry-based tear proteomics for noninvasive biomarker discovery. Dettaglio
- Bianchi, G; Mangiagalli, M; Barbiroli, A; Longhi, S; Grandori, R; Santambrogio, C; Brocca, S (2022) Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. Dettaglio
- Luise, A; De Cecco, E; Ponzini, E; Sollazzo, M; Mauri, P; Sobott, F; Legname, G; Grandori, R; Santambrogio, C (2021) Profiling Dopamine-Induced Oxidized Proteoforms of β-synuclein by Top-Down Mass Spectrometry. Dettaglio
- Ponzini, E; Ami, D; Duse, A; Santambrogio, C; De Palma, A; Di Silvestre, D; Mauri, P; Pezzoli, F; Natalello, A; Tavazzi, S; Grandori, R (2021) Single-Tear Proteomics: A Feasible Approach to Precision Medicine. Dettaglio
- Achour, A; Broggini, L; Han, X; Sun, R; Santambrogio, C; Buratto, J; Visentin, C; Barbiroli, A; De Luca, C; Sormanni, P; Moda, F; De Simone, A; Sandalova, T; Grandori, R; Camilloni, C; Ricagno, S (2020) Biochemical and biophysical comparison of human and mouse beta-2 microglobulin reveals the molecular determinants of low amyloid propensity. Dettaglio
- Bianchi, G; Longhi, S; Grandori, R; Brocca, S (2020) Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins. Dettaglio
- Tira, R; De Cecco, E; Rigamonti, V; Santambrogio, C; Barracchia, C; Munari, F; Romeo, A; Legname, G; Prosperi, D; Grandori, R; Assfalg, M (2020) Dynamic molecular exchange and conformational transitions of alpha-synuclein at the nano-bio interface. Dettaglio
- Carija, A; Pinheiro, F; Pujols, J; Bras, I; Lazaro, D; Santambrogio, C; Grandori, R; Outeiro, T; Navarro, S; Ventura, S (2019) Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity. Dettaglio