F
Flavio Meggio
Researcher at Health Science University
Publications - 16
Citations - 782
Flavio Meggio is an academic researcher from Health Science University. The author has contributed to research in topics: Phosphorylation & Casein kinase 2. The author has an hindex of 9, co-authored 16 publications receiving 754 citations. Previous affiliations of Flavio Meggio include University of Santiago de Compostela & University of Bologna.
Papers
More filters
Journal ArticleDOI
Optimization of protein kinase CK2 inhibitors derived from 4,5,6,7-tetrabromobenzimidazole.
Mario A. Pagano,Mariola Andrzejewska,Maria Ruzzene,Stefania Sarno,Luca Cesaro,Jenny Bain,Matthew Elliott,Flavio Meggio,Zygmunt Kazimierczuk,Lorenzo A. Pinna +9 more
TL;DR: It is proposed to adopt 2c as first choice CK2 inhibitor instead of TBB, especially for in cell studies, because 2c is even more susceptible than TBB to mutations of the unique hydrophobic residues V66 and/or I174 to alanine.
Journal ArticleDOI
Endogenous phosphate acceptor proteins for rat liver cytosolic casein kinases.
TL;DR: The electrophoretic mobilities of the 80,000, 49, thousands, and 25,000 phosphorylatable proteins are consistent with their identification as glycogen synthase, calsequestrin, and protein phosphatase inhibitor-1, respectively.
Journal ArticleDOI
Synthetic peptides including acidic clusters as substrates and inhibitors of rat liver casein kinase TS (type-2).
TL;DR: It is concluded that the minimum structural requirement of type-2 casein kinases consists of a phosphorylatable residue followed by an acidic cluster, whose length is critical for the binding to the enzyme.
Journal ArticleDOI
Coumarin as Attractive Casein Kinase 2 (CK2) Inhibitor Scaffold: An Integrate Approach To Elucidate the Putative Binding Motif and Explain Structure–Activity Relationships
Adriana Chilin,Roberto Battistutta,Andrea Bortolato,Giorgio Cozza,Samuele Zanatta,Giorgia Poletto,Marco Mazzorana,Giuseppe Zagotto,Eugenio Uriarte,A. Guiotto,Lorenzo A. Pinna,Flavio Meggio,Stefano Moro +12 more
TL;DR: It is discovered that coumarin moiety can be considered an attractive CK2 inhibitor scaffold and the most promising inhibitor, 3,8-dibromo-7-hydroxy-4-methylchromen-2-one (DBC), has been also crystallized in complex with CK2, and the experimental binding mode has been used to derive a linear interaction energy (LIE) model.
Journal ArticleDOI
The Regulatory β Subunit of Protein Kinase CK2 Contributes to the Recognition of the Substrate Consensus Sequence. A Study with an eIF2β-Derived Peptide†
Giorgia Poletto,Jordi Vilardell,Oriano Marin,Mario A. Pagano,Giorgio Cozza,Stefania Sarno,Antoni Falqués,Emilio Itarte,L. A. Pinna,Flavio Meggio +9 more
TL;DR: Results demonstrate that this peptide still displays phosphorylation features similar to full-length eIF2beta and the CK2 beta subunit also contributes to recognition of the protein substrate by establishing both polar and hydrophobic interactions with specificity determinants located downstream from the phosphoacceptor site.