L
L. Mugnaini
Researcher at University of Pisa
Publications - 7
Citations - 492
L. Mugnaini is an academic researcher from University of Pisa. The author has contributed to research in topics: Docking (molecular) & Adenosine. The author has an hindex of 7, co-authored 7 publications receiving 454 citations. Previous affiliations of L. Mugnaini include University of Florence.
Papers
More filters
Journal ArticleDOI
Pyrido[1,2-a]pyrimidin-4-one derivatives as a novel class of selective aldose reductase inhibitors exhibiting antioxidant activity.
Concettina La Motta,Stefania Sartini,L. Mugnaini,Francesca Simorini,Sabrina Taliani,Silvia Salerno,Anna Maria Marini,Federico Da Settimo,Antonio Lavecchia,Ettore Novellino,Miriam Cantore,Paola Failli,M. Ciuffi +12 more
TL;DR: The theoretical binding mode of the most active compounds obtained by docking simulations into the ALR2 crystal structure was fully consistent with the structure-activity relationships in the pyrido[1,2-a]pyrimidin-4-one series.
Journal ArticleDOI
Inhibition of Adenosine Deaminase Attenuates Inflammation in Experimental Colitis
Luca Antonioli,Matteo Fornai,Rocchina Colucci,Narcisa Ghisu,Federico Da Settimo,Gianfranco Natale,Olga Kastsiuchenka,Emiliano Duranti,Agostino Virdis,Cristina Vassalle,Concettina La Motta,L. Mugnaini,Maria Cristina Breschi,Corrado Blandizzi,Mario Del Taca +14 more
TL;DR: In conclusion, inhibition of adenosine deaminase results in a significant attenuation of intestinal inflammation and the novel compound APP is more effective than EHNA in reducing systemic and intestinal inflammatory alterations.
Journal ArticleDOI
Sampling protein motion and solvent effect during ligand binding
Vittorio Limongelli,Luciana Marinelli,Sandro Cosconati,Concettina La Motta,Stefania Sartini,L. Mugnaini,Federico Da Settimo,Ettore Novellino,Michele Parrinello +8 more
TL;DR: The mechanism of binding of a new series of potent inhibitors of Adenosine Deaminase is developed and revealed and the lowest energy binding modes of the most potent compound of the series, 4-decyl-pyrazolo[1,5-a]pyrimidin-7-one are identified.
Journal ArticleDOI
Novel N2-substituted pyrazolo[3,4-d]pyrimidine adenosine A3 receptor antagonists: inhibition of A3-mediated human glioblastoma cell proliferation.
Sabrina Taliani,Concettina La Motta,L. Mugnaini,Francesca Simorini,Silvia Salerno,Anna Maria Marini,Federico Da Settimo,Sandro Cosconati,Barbara Cosimelli,Giovanni Greco,Vittorio Limongelli,Luciana Marinelli,Ettore Novellino,Osele Ciampi,Simona Daniele,Maria Letizia Trincavelli,Claudia Martini +16 more
TL;DR: A novel series of N(2)-substituted pyrazolo[3,4-d]pyrimidines 2a-u was developed as highly potent and selective A(3) AR antagonists and the antiproliferative activity of the new compounds was demonstrated to be mediated by the block of A( 3) AR agonist activation of intracellular kinases ERK 1/2.
Journal ArticleDOI
Novel, highly potent adenosine deaminase inhibitors containing the pyrazolo[3,4-d]pyrimidine ring system. Synthesis, structure-activity relationships, and molecular modeling studies.
Federico Da Settimo,Giampaolo Primofiore,Concettina La Motta,Sabrina Taliani,Francesca Simorini,Anna Maria Marini,L. Mugnaini,Antonio Lavecchia,Ettore Novellino,D. Tuscano,Claudia Martini +10 more
TL;DR: The synthesis of a number of 1- and 2-alkyl derivatives of the 4-aminopyrazolo[3,4-d-d]pyrimidine nucleus and their evaluation as inhibitors of ADA from bovine spleen proved to be potent inhibitors, most of them exhibiting K(i) values in the nanomolar/subnanomolar range.