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Katiuscia Pagano
Researcher at University of Udine
Publications - 34
Citations - 688
Katiuscia Pagano is an academic researcher from University of Udine. The author has contributed to research in topics: Fibroblast growth factor & Bile acid binding. The author has an hindex of 12, co-authored 30 publications receiving 532 citations. Previous affiliations of Katiuscia Pagano include University of Padua.
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Journal ArticleDOI
Effect of Tetracyclines on the Dynamics of Formation and Destructuration of β2-Microglobulin Amyloid Fibrils
Sofia Giorgetti,Sara Raimondi,Katiuscia Pagano,Annalisa Relini,Monica Bucciantini,Alessandra Corazza,Federico Fogolari,Luca Codutti,Mario Salmona,Palma Mangione,Lino Colombo,Ada De Luigi,Riccardo Porcari,Alessandra Gliozzi,Massimo Stefani,Gennaro Esposito,Vittorio Bellotti,Monica Stoppini +17 more
TL;DR: NMR analysis showed that doxycycline inhibits β2-microglobulin self-association and stabilizes the native-like species through fast exchange interactions involving specific regions of the protein, further strengthening a possible in vivo therapeutic exploitation of this drug.
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Long-Pentraxin 3 Derivative as a Small-Molecule FGF Trap for Cancer Therapy
Roberto Ronca,Arianna Giacomini,Emanuela Di Salle,Daniela Coltrini,Katiuscia Pagano,Laura Ragona,Sara Matarazzo,Sara Rezzola,Daniele Maiolo,Rubben Torella,Elisabetta Moroni,Roberta Mazzieri,Giulia Escobar,Marco Mor,Giorgio Colombo,Marco Presta +15 more
TL;DR: Using pharmacophore modeling of the interaction of a minimal PTX3-derived FGF-binding pentapeptide with FGF2, a small-molecule chemical (NSC12) that acts as an extracellular FGF trap with significant implications in cancer therapy is identified.
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The study of transient protein-nanoparticle interactions by solution NMR spectroscopy
Michael Assfalg,Laura Ragona,Katiuscia Pagano,Mariapina D'Onofrio,Serena Zanzoni,Simona Tomaselli,Henriette Molinari +6 more
TL;DR: This review provides the first survey and critical assessment of the contributions from solution NMR spectroscopy to the study of transient interactions between proteins and both inorganic and organic nanoparticles.
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Natural Compounds as Inhibitors of Aβ Peptide Aggregation: Chemical Requirements and Molecular Mechanisms.
TL;DR: In this article, a review of natural compounds that interfere with amyloid-β (Aβ) aggregation by direct interaction with Aβ peptide and whose inhibitory mechanism has been investigated by means of biophysical and structural biology experimental approaches is presented.
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Structure, Conformational Stability, and Enzymatic Properties of Acylphosphatase from the Hyperthermophile Sulfolobus Solfataricus.
Alessandra Corazza,Camillo Rosano,Katiuscia Pagano,Vera Alverdi,Gennaro Esposito,Cristina Capanni,Francesco Bemporad,Georgia Plakoutsi,Massimo Stefani,Fabrizio Chiti,Simone Zuccotti,Martino Bolognesi,Martino Bolognesi,Paolo Viglino +13 more
TL;DR: The structure of Sulfolobus solfataricus (Sso AcP) was determined by H-NMR spectroscopy and X-ray crystallography in this article.