The significance of transmembrane segment of EGF-receptor in transduction of hormone signal

Author(s):  
Mária Ficková ◽  
Štefan Zorad ◽  
Gerard Cremel
2004 ◽  
Vol 171 (4S) ◽  
pp. 251-251
Author(s):  
Kazunori Hattori ◽  
Katsuyuki Iida ◽  
Akira Johraku ◽  
Sadamu Tsukamoto ◽  
Taeko Asano ◽  
...  

2009 ◽  
Vol 138 (3) ◽  
pp. 604-604
Author(s):  
Natalia Jura ◽  
Nicholas F. Endres ◽  
Kate Engel ◽  
Sebastian Deindl ◽  
Rahul Das ◽  
...  

2009 ◽  
Vol 138 (33) ◽  
pp. 604-604
Author(s):  
Natalia Jura ◽  
Nicholas F. Endres ◽  
Kate Engel ◽  
Sebastian Deindl ◽  
Rahul Das ◽  
...  

2019 ◽  
Author(s):  
Alisher M Kariev ◽  
Michael Green

Quantum calculations on 976 atoms of the voltage sensing domain of the K<sub>v</sub>1.2 channel, with protons in several positions, give energy, charge transfer, and other properties. Motion of the S4 transmembrane segment that accounts for gating current in standard models is shown not to occur; there is H<sup>+ </sup>transfer instead. The potential at which two proton positions cross in energy approximately corresponds to the gating potential for the channel. The charge displacement seems approximately correct for the gating current. Two mutations are accounted for (Y266F, R300cit, cit =citrulline). The primary conclusion is that voltage sensing depends on H<sup>+</sup> transfer, not motion of arginine charges.


Sign in / Sign up

Export Citation Format

Share Document