Mattia Poletto
University of Udine
17 Papers
54 Citations
Mattia Poletto is an academic researcher from University of Udine. The author has contributed to research in topics: AP site & Nucleophosmin. The author has an hindex of 12, co-authored 15 publications. Previous affiliations of Mattia Poletto include University of Naples Federico II.
Chat about Author
Papers
Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions
Damiano Fantini,Carlo Vascotto,Daniela Marasco,Chiara D'Ambrosio,Milena Romanello,Luigi Vitagliano,Carlo Pedone,Mattia Poletto,Laura Cesaratto,Franco Quadrifoglio,Andrea Scaloni,J. Pablo Radicella,Gianluca Tell +12 more
TL;DR: Results suggest that protein–protein interactions and/or post-translational modifications involving APE1 N-terminal domain may play important in vivo roles, in better coordinating and fine-tuning protein BER activity and function on RNA metabolism.
Inhibitors of the apurinic/apyrimidinic endonuclease 1 (APE1)/nucleophosmin (NPM1) interaction that display anti-tumor properties.
Mattia Poletto,Matilde Clarissa Malfatti,Dorjbal Dorjsuren,Pasqualina Liana Scognamiglio,Daniela Marasco,Carlo Vascotto,Ajit Jadhav,David J. Maloney,David M. Wilson,Anton Simeonov,Gianluca Tell +10 more
TL;DR: A chemiluminescence‐based high‐throughput screening assay led to the identification of a set of bioactive compounds that impair the APE1/NPM1 association in living cells, and some of these molecules display anti‐proliferative activity and sensitize cells to therapeutically relevant genotoxins.
G-quadruplex DNA recognition by nucleophosmin: new insights from protein dissection.
Pasqualina Liana Scognamiglio,Pasqualina Liana Scognamiglio,Concetta Di Natale,Concetta Di Natale,Marilisa Leone,Mattia Poletto,Luigi Vitagliano,Gianluca Tell,Daniela Marasco +8 more
TL;DR: It is suggested that the tight binding of NPM1/B23 to the G-quadruplex is achieved through the cooperation of both folded and unfolded regions that are individually able to bind it.
57
Nucleophosmin modulates stability, activity, and nucleolar accumulation of base excision repair proteins. - eScholarship
David Wilson,Mattia Poletto,Lisa Lirussi,Denise Wilson,Gianluca Tell +4 more
- 01 May 2014
TL;DR: Nucleophosmin (NPM1) is a multifunctional protein that controls cell growth and genome stability via a mechanism that involves nucleolar-cytoplasmic shuttling.
43
Expression and Prognostic Significance of APE1/Ref-1 and NPM1 Proteins in High-Grade Ovarian Serous Cancer
Ambrogio P. Londero,Maria Orsaria,Gianluca Tell,Stefania Marzinotto,Valentina Capodicasa,Mattia Poletto,Carlo Vascotto,Cosimo Sacco,Laura Mariuzzi +8 more
TL;DR: A high NPM1 immunohistochemical expression was independently correlated with a shorter survival period and thus appears to be an important prognostic factor in high-grade ovarian serous cancer.