Inhibition of Eph/ephrin interaction with the small molecule UniPR500 improves glucose tolerance in healthy and insulin-resistant mice

Autor: Giorgio, C., Incerti, M., Pala, D., Russo, S., Chiodelli, P., Rusnati, M., Cantoni, A.M., Di Lecce, R., Barocelli, E., Bertoni, S., Ravassard, P., Manenti, F., Piemonti, L., Ferlenghi, F., Lodola, A., Tognolini, M.

Publikováno v: In Pharmacological Research March 2019 141:319-330

Functionalization of gold surfaces with copoly(DMA-NAS-MAPS) by dip coating: Surface characterization and hybridization tests

Autor: Petti, D., Torti, A., Damin, F., Sola, L., Rusnati, M., Albisetti, E., Bugatti, A., Bertacco, R., Chiari, M.

Publikováno v: In Sensors & Actuators: B. Chemical January 2014 190:234-242

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The fd phage and a peptide derived from its p8 coat protein interact with the HIV-1 Tat-NLS and inhibit its biological functions

Autor: Krichevsky, A. ^*, Rusnati, M., Bugatti, A., Waigmann, E., Shohat, S., Loyter, A.

Publikováno v: In Antiviral Research 2005 66(1):67-78

Exploitation of a novel biosensor based on the full-length human F508de1-CFTR with computational studies, biochemical and biological assays for the characterization of a new Lumacaftor/Tezacaftor analogue

Autor: D'Ursi P., Uggeri M., Urbinati C., Millo E., Paiardi G., Milanesi L., Ford R. C., Clews J., Meng X., Bergese P., Ridolfi A., Pedemonte N., Fossa P., Orro A., Rusnati M.

Publikováno v: Sensors and actuators. B, Chemical
301 (2019). doi:10.1016/j.snb.2019.127131
info:cnr-pdr/source/autori:D'Ursi P.; Uggeri M.; Urbinati C.; Millo E.; Paiardi G.; Milanesi L.; Ford R. C.; Clews J.; Meng X.; Bergese P.; Ridolfi A.; Pedemonte N.; Fossa P.; Orro A.; Rusnati M./titolo:Exploitation of a novel biosensor based on the full-length human F508de1-CFTR with computational studies, biochemical and biological assays for the characterization of a new Lumacaftor%2FTezacaftor analogue/doi:10.1016%2Fj.snb.2019.127131/rivista:Sensors and actuators. B, Chemical (Print)/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume:301

Cystic fibrosis (CF) is mainly caused by the mutation F508del of the cystic fibrosis transmembrane conductance regulator (CFTR) that is thus retained in the endoplasmic reticulum and degraded. New drugs able to rescue F508del-CFTR trafficking and act

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::5386c3fdc84e2f5e8eb461edbff8f624
http://www.cnr.it/prodotto/i/408373