Luigi Rossetti
Sapienza University of Rome
Network
Latest external collaboration on country level. Dive into details by clicking on the dots.
Publication
Featured researches published by Luigi Rossetti.
Biophysical Chemistry | 2000
Ilaria Filesi; Stefano Cacchione; Pasquale De Santis; Luigi Rossetti; Maria Savino
Using a competitive reconstitution assay, we measured the free energy spent in nucleosome formation of eight telomeric DNAs, differing in sequence and/or in length. The obtained values are in satisfactorily good agreement with those derived from a theoretical model that allows the calculation of the free energy of nucleosome formation on the basis of sequence-dependent DNA elasticity, using a statistical thermodynamic approach. Both theoretical and experimental evaluations show that telomeres are characterized by the highest free energies of nucleosome formation among all the DNA sequences so far studied. The free energy of nucleosome formation varies according to the different telomeric sequences and the length of the fragments. Theoretical analysis and experimental mapping by lambda exonuclease show that telomeric nucleosomes occupy multiple positions spaced every telomeric repeat. Sequence-dependent DNA elasticity appears as the main determinant of the stability of telomeric nucleosomes and their multiple translational positioning.
Biochimica et Biophysica Acta | 1997
Roberto Caneva; Alessandro De Simoni; Luciano Mayol; Luigi Rossetti; Maria Savino
Equilibrium binding properties of DAPI and Hoechst for prototype curved (CA4T4G)n and straight (CT4A4G)n DNAs were derived from fluorescence intensity. Both decamers display a single strong binding site for each ligand. Hoechst binds seven times stronger to curved than to straight DNA. An additional cooperative, much weaker binding site is found for DAPI.
Biochimica et Biophysica Acta | 1996
Roberto Caneva; Luigi Rossetti; Maria Savino
Equilibrium binding properties of DAPI for purified nucleosome cores were derived from fluorescence intensity enhancement. Both the affinity and the number of sites of the primary, minor groove binding are preserved with respect to the corresponding isolated DNA, suggesting that the capacity for specific interactions of the minor groove may well be exerted in chromatin.
Bioorganic & Medicinal Chemistry Letters | 2006
Marco Franceschin; Luigi Rossetti; Anna D'Ambrosio; Stefano Schirripa; Armandodoriano Bianco; Giancarlo Ortaggi; Maria Savino; Christoph Schultes; Stephen Neidle
Bioorganic & Medicinal Chemistry Letters | 2002
Luigi Rossetti; Marco Franceschin; Armandodoriano Bianco; Giancarlo Ortaggi; Maria Savino
Biochemistry | 1998
Luigi Rossetti; Stefano Cacchione; M. Fua; Maria Savino
Bioorganic & Medicinal Chemistry Letters | 2005
Luigi Rossetti; Marco Franceschin; Stefano Schirripa; Armandodoriano Bianco; Giancarlo Ortaggi; Maria Savino
Journal of Molecular Biology | 2001
Luigi Rossetti; Stefano Cacchione; Amanda De Menna; Lynda Chapman; Daniela Rhodes; Maria Savino
Journal of Molecular Biology | 2006
Alessandra Galati; Luigi Rossetti; Sabrina Pisano; Lynda Chapman; Daniela Rhodes; Maria Savino; Stefano Cacchione
Biophysical Chemistry | 2007
Luigi Rossetti; Giuliana D'Isa; Clementina Mauriello; Michela Varra; Pasquale De Santis; Luciano Mayol; Maria Savino