LIMITS OF KINETIC SCHEMES FOR EXCITON REACTIONS

1985 ◽  
Vol 46 (C7) ◽  
pp. C7-3-C7-8
Author(s):  
A. Blumen ◽  
G. Zumofen ◽  
J. Klafter
Keyword(s):  
2003 ◽  
Vol 192 (2) ◽  
pp. 695-726 ◽  
Author(s):  
Matthias Kunik ◽  
Shamsul Qamar ◽  
Gerald Warnecke

2019 ◽  
Vol 141 ◽  
pp. 234-247
Author(s):  
Corrado Lattanzio ◽  
Corrado Mascia ◽  
Ramón G. Plaza ◽  
Chiara Simeoni

2003 ◽  
Vol 43 (9) ◽  
pp. 1081-1098
Author(s):  
H. S. R. Reksoprodjo ◽  
R. K. Agarwal

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Christian Sattler ◽  
Thomas Eick ◽  
Sabine Hummert ◽  
Eckhard Schulz ◽  
Ralf Schmauder ◽  
...  

AbstractIonotropic purinergic (P2X) receptors are trimeric channels that are activated by the binding of ATP. They are involved in multiple physiological functions, including synaptic transmission, pain and inflammation. The mechanism of activation is still elusive. Here we kinetically unraveled and quantified subunit activation in P2X2 receptors by an extensive global fit approach with four complex and intimately coupled kinetic schemes to currents obtained from wild type and mutated receptors using ATP and its fluorescent derivative 2-[DY-547P1]-AET-ATP (fATP). We show that the steep concentration-activation relationship in wild type channels is caused by a subunit flip reaction with strong positive cooperativity, overbalancing a pronounced negative cooperativity for the three ATP binding steps, that the net probability fluxes in the model generate a marked hysteresis in the activation-deactivation cycle, and that the predicted fATP binding matches the binding measured by fluorescence. Our results shed light into the intricate activation process of P2X channels.


Sign in / Sign up

Export Citation Format

Share Document