Influence of Amino-Terminal Structures on Kinetic Transitions between Several Closed and Open States in Human erg K+ Channels

@article{GmezVarela2002InfluenceOA,
  title={Influence of Amino-Terminal Structures on Kinetic Transitions between Several Closed and Open States in Human erg K+ Channels},
  author={David G{\'o}mez-Varela and P Garc{\'i}a de la Pe{\~n}a and Juan Garc{\'i}a and Teresa Giraldez and Francisco Barros},
  journal={The Journal of Membrane Biology},
  year={2002},
  volume={187},
  pages={117-133}
}
Gating kinetics of human ether-a-go-go (eag)-related gene (HERG) K+ channel expressed in Xenopus oocytes was studied using non-inactivating channel variants carrying different structural modifications in the amino terminus. A kinetics model was elaborated to describe the behavior of full-length channels, that includes at least three open states besides the three closed states previously proposed. Deletion of the HERG-specific proximal domain (HERG D138-373) accelerated all individual forward… CONTINUE READING
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