D
Daniel O. Cicero
Researcher at University of Rome Tor Vergata
Publications - 114
Citations - 2202
Daniel O. Cicero is an academic researcher from University of Rome Tor Vergata. The author has contributed to research in topics: Corrole & Protein structure. The author has an hindex of 24, co-authored 105 publications receiving 1995 citations. Previous affiliations of Daniel O. Cicero include Fundación Instituto Leloir & International School for Advanced Studies.
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NMR Analysis of Molecular Flexibility in Solution: A New Method for the Study of Complex Distributions of Rapidly Exchanging Conformations. Application to a 13-Residue Peptide with an 8-Residue Loop
TL;DR: In this article, a new methodology, called NAMFIS (NMR analysis of molecular flexibility in solution), is described for the analysis of flexible molecules in solution, which allows for the examination of the occurrence and relevance of arbitrary elements of secondary structure.
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Sensitivity enhancement of a two-dimensional experiment for the measurement of heteronuclear long-range coupling constants, by a new scheme of coherence selection by gradients.
TL;DR: A new pulse sequence for the measurement of long-range heteronuclear coupling constants in which the optimization of coherence selection by pulsed field gradients offers a net increase in sensitivity.
Journal ArticleDOI
The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism.
Gaetano Barbato,Daniel O. Cicero,Maria Chiara Nardi,Christian Steinkühler,R. Cortese,R. De Francesco,Renzo Bazzo +6 more
TL;DR: The solution structure of the hepatitis C virus (BK strain) NS3 protein N-terminal domain (186 residues) has been solved by NMR spectroscopy and allows the formulation of a model in which, in addition to the NS4A cofactor, the substrate plays an important role in the activation of the catalytic mechanism.
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The Structure of the Elicitor Cerato-platanin (CP), the First Member of the CP Fungal Protein Family, Reveals a Double ψβ-Barrel Fold and Carbohydrate Binding
Aline L. de Oliveira,Mariana Gallo,Luigia Pazzagli,Celso Eduardo Benedetti,Gianni Cappugi,Aniello Scala,Barbara Pantera,Alberto Spisni,Thelma A. Pertinhez,Daniel O. Cicero +9 more
TL;DR: The results suggest that CP might be involved in polysaccharide recognition and that the double ψβ-barrel fold is widespread in distantly related organisms, where it is often involved in host-microbe interactions.
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Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain
Gaetano Barbato,Daniel O. Cicero,Florence Cordier,Frank Narjes,Benjamin Gerlach,Sonia Sambucini,Stephan Grzesiek,Stephan Grzesiek,V.G. Matassa,R. De Francesco,Renzo Bazzo +10 more
TL;DR: The data suggest that natural substrates of this serine protease could contribute to the enzyme activation by a similar induced‐fit mechanism, and the high degree of similarity at the His–Asp catalytic site region between HCV NS3 and other viral serines suggests that this behaviour could be a more general feature for this category of viral enzymes.