| Title : Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3 - Wood_2012_Biomol.NMR.Assign_6_15 |
| Author(s) : Wood K , Paz A , Dijkstra K , Scheek RM , Otten R , Silman I , Sussman JL , Mulder FA |
| Ref : Biomol NMR Assign , 6 :15 , 2012 |
|
Abstract :
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we report the backbone and side chain (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3. |
| PubMedSearch : Wood_2012_Biomol.NMR.Assign_6_15 |
| PubMedID: 21647611 |
Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA (2012)
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
Biomol NMR Assign
6 :15
Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA (2012)
Biomol NMR Assign
6 :15