1H, 13C and 15N chemical shift assignments for the N-terminal domain of the voltage-gated potassium channel-hERG

2010 ◽  
Vol 4 (2) ◽  
pp. 211-213 ◽  
Author(s):  
Qingxin Li ◽  
Manfred Raida ◽  
CongBao Kang
2017 ◽  
Vol 11 (2) ◽  
pp. 137-141 ◽  
Author(s):  
Hanjun Li ◽  
Gaelle Spagnol ◽  
Tasha K. Pontifex ◽  
Janis M. Burt ◽  
Paul L. Sorgen

2017 ◽  
Vol 11 (2) ◽  
pp. 281-284 ◽  
Author(s):  
Ning Zhang ◽  
Wensu Yuan ◽  
Jing-Song Fan ◽  
Zhi Lin

Author(s):  
Yonghong Zhang ◽  
Johannes W. Hell ◽  
James B. Ames

AbstractPostsynaptic density protein-95 (PSD95) contributes to the postsynaptic architecture of neuronal synapses and plays an important role in controlling synaptic plasticity. The N-terminal domain of PSD95 (residues 1–71, called PSD95-NT) interacts with target proteins (calmodulin, α-actinin-1 and CDKL5), which regulate the Ca2+-dependent degradation of glutamate receptors. We report complete backbone NMR chemical shift assignments of PSD95-NT (BMRB No. 50752).


Author(s):  
Angelo Gallo ◽  
Aikaterini C. Tsika ◽  
Nikolaos K. Fourkiotis ◽  
Francesca Cantini ◽  
Lucia Banci ◽  
...  

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