Ilda D'Annessa
University of Rome Tor Vergata
49 Papers
310 Citations
Ilda D'Annessa is an academic researcher from University of Rome Tor Vergata. The author has contributed to research in topics: Topoisomerase & Camptothecin. The author has an hindex of 16, co-authored 48 publications. Previous affiliations of Ilda D'Annessa include Indian Institute of Chemical Biology.
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Papers
Allosteric Modulators of HSP90 and HSP70: Dynamics Meets Function through Structure-Based Drug Design.
Mariarosaria Ferraro,Ilda D'Annessa,Elisabetta Moroni,Giulia Morra,Antonella Paladino,Silvia Rinaldi,Federica Compostella,Giorgio Colombo +7 more
TL;DR: In this article, the authors review advances in the design of HSP90 and HSP70 allosteric modulators and discuss these compounds as probes to decipher the complexity of the chapero...
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Computational Analysis of Dengue Virus Envelope Protein (E) Reveals an Epitope with Flavivirus Immunodiagnostic Potential in Peptide Microarrays.
Greta Bergamaschi,Enrico M.A. Fassi,Alessandro Romanato,Ilda D'Annessa,Maria Teresa Odinolfi,Dario Brambilla,Francesco Damin,Marcella Chiari,Alessandro Gori,Giorgio Colombo,Marina Cretich +10 more
TL;DR: A synthetic epitope probe synthesized as a linear peptide, modified for chemoselective immobilization on microarrays and used in a serological assay to discriminate Dengue-infected individuals from healthy controls showed a diagnostic performance comparable to that of the full antigen in terms of specificity and sensitivity.
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Thr729 in human topoisomerase I modulates anti-cancer drug resistance by altering protein domain communications as suggested by molecular dynamics simulations.
Giovanni Chillemi,Ilda D'Annessa,Paola Fiorani,Carmen Losasso,Piero Benedetti,Alessandro Desideri +5 more
TL;DR: The role of Thr729 in modulating the enzymatic function of human topoisomerase I has been characterized by molecular dynamics simulation and the complete abolishment, in the Thr729Lys mutant, of the protein communications between the C-terminal domain and the linker domain is shown, thus explaining the distributive mode of action displayed by this mutant.
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Interaction between natural compounds and human topoisomerase I.
Silvia Castelli,Andrea Coletta,Ilda D'Annessa,Paola Fiorani,Cinzia Tesauro,Alessandro Desideri +5 more
TL;DR: This review points out the interaction between human Top1 and some natural compounds, such us terpenoids, flavonoids, stilbenes and fatty acids, and different assays that can be used to identify the catalytic step of the enzyme inhibited by different natural compounds.
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Ligand Binding, Unbinding, and Allosteric Effects: Deciphering Small-Molecule Modulation of HSP90.
Ilda D'Annessa,Stefano Raniolo,Vittorio Limongelli,Vittorio Limongelli,Daniele Di Marino,Giorgio Colombo +5 more
TL;DR: This work for the first time explicitly correlates HSP90 responses to binding/unbinding of an allosteric ligand to the modulation of functionally oriented protein motions, and shows that different binding poses induce different dynamics states.
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