Get well prune: The C-terminal third domain of h-prune is largely unfolded and involved in relevant protein-protein interactions, particularly with Nm23-H1 (see figure), GSK-3β and gelsolin. This study shows that protein functions mediated by protein-protein interactions can be accurately followed in cell lysates by using fast NMR spectroscopy, which could be easily used for a very efficient NMR drug-discovery strategy.

Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates / Diana, Donatella; Giovanni, Smaldone; Pasquale, De?antonellis; Luciano, Pirone; Marianeve, Carotenuto; Alessandro, Alonzi; Sonia, Di?gaetano; Zollo, Massimo; Pedone, EMILIA MARIA; Roberto, Fattorusso. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - 19:(2013), pp. 12217-12220. [10.1002/chem.201302168]

Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates

Donatella Diana;ZOLLO, MASSIMO;PEDONE, EMILIA MARIA;
2013

Abstract

Get well prune: The C-terminal third domain of h-prune is largely unfolded and involved in relevant protein-protein interactions, particularly with Nm23-H1 (see figure), GSK-3β and gelsolin. This study shows that protein functions mediated by protein-protein interactions can be accurately followed in cell lysates by using fast NMR spectroscopy, which could be easily used for a very efficient NMR drug-discovery strategy.
2013
Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates / Diana, Donatella; Giovanni, Smaldone; Pasquale, De?antonellis; Luciano, Pirone; Marianeve, Carotenuto; Alessandro, Alonzi; Sonia, Di?gaetano; Zollo, Massimo; Pedone, EMILIA MARIA; Roberto, Fattorusso. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - 19:(2013), pp. 12217-12220. [10.1002/chem.201302168]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/577668
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