Entry ID | Original Release date | Data summary | Entry Title | Citation Title | Authors |
---|---|---|---|---|---|
34822 | 2024-05-07 | Chemical Shifts: 1 set |
Structural characterization of PHOX2B and its DNA interactions shed lights into the molecular basis of the + 7Ala variant pathogenicity in CCHS | Structural characterization of PHOX2B and its DNA interactions shed lights into the molecular basis of the + 7Ala variant pathogenicity in CCHS | A Corvino, C Acconcia, C Isernia, D Diana, D Fornasari, E Pedone, G D Abrosca, G Malgieri, L Caldinelli, L Pirone, L Pollegioni, L Russo, M Madheswaran, R Benfante, R Fattorusso, S Di Gaetano, S Di Lascio |
34213 | 2018-07-26 | Chemical Shifts: 1 set |
NMR structure of EphA2-Sam stapled peptides (S13ST) | Sam domain-based stapled peptides: Structural analysis and interaction studies with the Sam domains from the EphA2 receptor and the lipid phosphatase Ship2 | C Di Natale, D Marasco, E M Pedone, F A Mercurio, L Pirone, M Leone |
34214 | 2018-07-26 | Chemical Shifts: 1 set |
NMR structure of EphA2-Sam stapled peptides (S13STshort) | Sam domain-based stapled peptides: Structural analysis and interaction studies with the Sam domains from the EphA2 receptor and the lipid phosphatase Ship2 | C Di Natale, D Marasco, E M Pedone, F A Mercurio, L Pirone, M Leone |
34215 | 2018-07-26 | Chemical Shifts: 1 set |
NMR structure of an Odin-Sam1 stapled peptide | Sam domain-based stapled peptides: Structural analysis and interaction studies with the Sam domains from the EphA2 receptor and the lipid phosphatase Ship2 | C Di Natale, D Marasco, E M Pedone, F A Mercurio, L Pirone, M Leone |
34138 | 2017-12-13 | Chemical Shifts: 1 set Spectral_peak_list: 1 set |
NMR structure of an EphA2-Sam fragment | The Sam-Sam interaction between Ship2 and the EphA2 receptor: design and analysis of peptide inhibitors | C Di Natale, D Marasco, E M Pedone, F A Mercurio, L Pirone, M Leone, R Iannitti, R Palumbo |
15373 | 2008-03-13 | Chemical Shifts: 1 set |
The prokaryotic Cys2His2 zinc finger adopts a novel fold as revealed by the NMR structure of A. tumefaciens Ros DNA binding domain | The prokaryotic Cys2His2 zinc finger adopts a novel fold as revealed by the NMR structure of A.tumefaciens Ros DNA binding domain | B Di Blasio, C Isernia, E M Pedone, Gaetano Malgieri, I Baglivo, L Russo, L Zaccaro, P V Pedone, R Fattorusso, S Esposito |