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Publikováno v:
Pflügers Archiv - European Journal of Physiology. 474:721-732
KCNQ channels participate in the physiology of several cell types. In neurons of the central nervous system, the primary subunits are KCNQ2, 3, and 5. Activation of these channels silence the neurons, limiting action potential duration and preventing
Autor:
Draheim, Teliha
Publikováno v:
Surface Design; Fall2008, Vol. 33 Issue 1, p42-44, 3p
Autor:
Juan Jose Romero-Tovar, Alejandro Rafael Medina-Vilchis, Adrian Rivera-Ruedas, Victor De la Rosa
Publikováno v:
Biophysical Journal. 122:512a
Autor:
Alexander B. Taylor, Victor De la Rosa, Benjamin T. Enslow, Akash Bhattacharya, Mark S. Shapiro, Crystal R. Archer
Publikováno v:
Journal of Biological Chemistry. 294:6094-6112
Calmodulin (CaM) conveys intracellular Ca2+ signals to KCNQ (Kv7, “M-type”) K+ channels and many other ion channels. Whether this “calmodulation” involves a dramatic structural rearrangement or only slight perturbations of the CaM/KCNQ comple
Publikováno v:
Journal of Biological Chemistry. 293:19411-19428
Phosphatidylinositol 4,5-bisphosphate (PIP2) in the plasma membrane regulates the function of many ion channels, including M-type (potassium voltage-gated channel subfamily Q member (KCNQ), Kv7) K+ channels; however, the molecular mechanisms involved
Autor:
Victor De La Rosa, Ian Scott Ramsey
Publikováno v:
Biophysical Journal. 114:2844-2854
The Hv1 proton channel shares striking structural homology with fourth transmembrane helical segment-type voltage-sensor (VS) domains but manifests distinctive functional properties, including a proton-selective “aqueous” conductance and alloster
Publikováno v:
The Journal of General Physiology
Hv1 proteins form a voltage-gated proton channel that is inhibited by extracellular Zn2+. De La Rosa et al find that extracellular Zn2+ is octahedrally coordinated by specific protein atoms and that Zn2+ occupancy modulates voltage sensor activation
Autor:
Victor De la Rosa, Mark S. Shapiro
Publikováno v:
Biophysical Journal. 118:588a-589a
Autor:
Crystal R, Archer, Benjamin T, Enslow, Alexander B, Taylor, Victor, De la Rosa, Akash, Bhattacharya, Mark S, Shapiro
Publikováno v:
The Journal of biological chemistry. 294(15)
Calmodulin (CaM) conveys intracellular Ca(2+) signals to KCNQ (Kv7, “M-type”) K(+) channels and many other ion channels. Whether this “calmodulation” involves a dramatic structural rearrangement or only slight perturbations of the CaM/KCNQ co