DEL CONTE, REBECCA
DEL CONTE, REBECCA
[2Fe-2S] cluster transfer in iron-sulfur protein biogenesis
2014 Banci L, Brancaccio D, Ciofi-Baffoni S, Del Conte R, Gadepalli R, Mikolajczyk M, Neri S, Piccioli M, Winkelmann J.
A further clue to understanding the mobility of mitochondrial yeast cytocrome c: a 15N T1p investigation of the oxidized and reduced species.
2001 BARKER P.D.; I. BERTINI; R. DEL CONTE; S.J. FERGUSON; P. HAJIEVA; P. TOMLINSON; P. TURANO; M.S. VIEZZOLI
A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal
2005 L.Banci; I.Bertini; V.Calderone; F.Cramaro; R.Del Conte; A. Fantoni; S.Mangani; A.Quattrone; M.S.Viezzoli
Assignment of backbone NMR resonances and secondary structural elements of a reduced monomeric mutant of copper/zinc superoxide dismutase
1997 L. Banci; M. Benedetto; I. Bertini; R. DelConte; M. Piccioli; T. Richert; M. S. Viezzoli
Backbone Dynamics of Human Cu, Zn Superoxide Dismustase and of its Monomeric F50/EG51E/E133Q Mutant: The influence of Dimerization on Mobility and Function.
2000 BANCI L.; I. BERTINI; F. CRAMARO; R. DEL CONTE; A. ROSATO; M.S. VIEZZOLI
Catalytic domain of MMP20 (Enamelysin) - the NMR strucutre of a new matrix metalloproteinase
2007 Y.Arendt;L.Banci;I.Bertini;F.Cantini;R.Cozzi;R.Del Conte;L.Gonnelli
Copper trafficking: the solution structure of Bacillus subtilis CopZ
2001 BANCI L.; I. BERTINI; R. DEL CONTE; J. MARKEY; F.J. RUIZ-DUENAS
Cytochrome c and organic molecules: solution structure of the p-aminophenol adduct
2007 M.Assfalg; I.Bertini; R.Del Conte; A.Giachetti; P.Turano
Enhanced Pru p 3 IgE-binding activity by selective free fatty acid-interaction
2017 Dubiela, Pawel; Aina, Roberta; Polak, Dominika; Geiselhart, Sabine; Humeniuk, Piotr; Bohle, Barbara; Alessandri, Stefano; Del Conte, Rebecca; Cantini, Francesca; Borowski, Tomasz; Bublin, Merima; Hoffmann-sommergruber, Karin
Fragment docking to s100 proteins reveals a wide diversity of weak interaction sites
2007 Y. Arendt; A. Bhaumik; R. Del Conte; C. Luchinat; M. Mori; M. Porcu
Fragmenting the S100B–p53 Interaction: CombinedVirtual/Biophysical Screening Approaches to IdentifyLigands
2010 M.Agamennone; L.Cesari; D.Lalli; E.Turlizzi; R. Del Conte; P. Turano; S. Mangani; A. Padova
Impact of lipid binding on the tertiary structure and allergenic potential of Jug r 3, the non-specificlipid transfer protein from walnut
2019 Pawel Dubiela, Rebecca Del Conte, Francesca Cantini, Tomasz Borowski, Roberta Aina, Christian Radauer, Merima Bublin, Karin Hoffmann-Sommergruber, Stefano Alessandri
NMR as a tool to target protein-protein interactions
2013 R. Del Conte; D. Lalli; P. Turano
NMR quality control of fragment libraries for screening
2020 Sreeramulu S.; Richter C.; Kuehn T.; Azzaoui K.; Blommers M.J.J.; Del Conte R.; Fragai M.; Trieloff N.; Schmieder P.; Nazare M.; Specker E.; Ivanov V.; Oschkinat H.; Banci L.; Schwalbe H.
Redox equilibria of manganese peroxidase from Phanerochaetes chrysosporium: functional role of residues on the proximal side of the haem pocket
2000 R. Santucci; C. Bongiovanni; S. Marini; R. Del Conte; M. Tien; L. Banci; M. Coletta
Solution structure and backbone dynamics of the Cu(I) and apo forms of the second metal-binding domain of the Menkes protein ATP7A
2004 L.Banci; I.Bertini; R.Del Conte; M.D'Onofrio; A.Rosato
Solution structure of apo CopZ from Bacillus subtilis: Further analysis of the changes associated with the presence of copper
2003 L. BANCI; I. BERTINI; R. DEL CONTE
Solution structure of apo Cu,Zn superoxide dismutase: the role of metal ions in protein folding
2003 L. BANCI; I. BERTINI; F. CRAMARO; R. DEL CONTE; M.S. VIEZZOLI
Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase. Why is SOD a dimeric enzyme?
1998 BANCI L.; BENEDETTO M.; I. BERTINI; DEL CONTE R.; PICCIOLI M.; VIEZZOLI M.S.
Spectroscopic characterization of active mutants of manganese peroxidase: mutations on the proximal side effect calcium binding on the distal side
1999 BANCI L.; I. BERTINI; CAPANNOLI C.; DEL CONTE R.; TIEN M.