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Sign in to add traineeCostantino Vetriani | grad student | Tor Vergata University, Roma, Italy |
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Publications
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Tinti M, Panni S, Cesareni G. (2018) Profiling Phosphopeptide-Binding Domain Recognition Specificity Using Peptide Microarrays. Methods in Molecular Biology (Clifton, N.J.). 1518: 177-193 |
Tinti M, Panni S, Cesareni G. (2018) Profiling Phosphopeptide-Binding Domain Recognition Specificity Using Peptide Microarrays. Methods in Molecular Biology (Clifton, N.J.). 1518: 177-193 |
Palma A, Tinti M, Paoluzi S, et al. (2017) Both Intrinsic Substrate Preference and Network Context Contribute to Substrate Selection of Classical Tyrosine Phosphatases. The Journal of Biological Chemistry |
Palma A, Tinti M, Paoluzi S, et al. (2017) Both Intrinsic Substrate Preference and Network Context Contribute to Substrate Selection of Classical Tyrosine Phosphatases. The Journal of Biological Chemistry |
Righino B, Pirolli D, Radicioni G, et al. (2016) Structural studies and SH3 domain binding properties of a human antiviral salivary proline-rich peptide. Biopolymers |
Righino B, Pirolli D, Radicioni G, et al. (2016) Structural studies and SH3 domain binding properties of a human antiviral salivary proline-rich peptide. Biopolymers |
Tinti M, Kiemer L, Costa S, et al. (2013) The SH2 domain interaction landscape. Cell Reports. 3: 1293-305 |
Tinti M, Kiemer L, Costa S, et al. (2013) The SH2 domain interaction landscape. Cell Reports. 3: 1293-305 |
Martinelli S, Nardozza AP, Delle Vigne S, et al. (2012) Counteracting effects operating on Src homology 2 domain-containing protein-tyrosine phosphatase 2 (SHP2) function drive selection of the recurrent Y62D and Y63C substitutions in Noonan syndrome. The Journal of Biological Chemistry. 287: 27066-77 |
Martinelli S, Nardozza AP, Delle Vigne S, et al. (2012) Counteracting effects operating on Src homology 2 domain-containing protein-tyrosine phosphatase 2 (SHP2) function drive selection of the recurrent Y62D and Y63C substitutions in Noonan syndrome. The Journal of Biological Chemistry. 287: 27066-77 |