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Science 26 October 1990: Vol. 250. no. 4980, pp. 533 - 538 DOI: 10.1126/science.2122519
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Articles
Science, Vol 250, Issue 4980, 533-538
Copyright © 1990 by American Association for the Advancement of Science
Biophysical and molecular mechanisms of Shaker potassium channel inactivation
T Hoshi,
WN Zagotta,
and
RW Aldrich
Department of Molecular and Cellular Physiology, Stanford University, School of Medicine, CA 94305.
The potassium channels encoded by the Drosophila Shaker gene activate and inactivate rapidly when the membrane potential becomes more positive. Site-directed mutagenesis and single-channel patch-clamp recording were used to explore the molecular transitions that underlie inactivation in Shaker potassium channels expressed in Xenopus oocytes. A region near the amino terminus with an important role in inactivation has now been identified. The results suggest a model where this region forms a cytoplasmic domain that interacts with the open channel to cause inactivation.
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- External TEA Block of Shaker K+ Channels Is Coupled to the Movement of K+ Ions within the Selectivity Filter.
- J. Thompson and T. Begenisich (2003)
J. Gen. Physiol.
122, 239-246
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- Differential Modulation of Cardiac Ca2+ Channel Gating by {beta}-Subunits.
- I. Dzhura and A. Neely (2003)
Biophys. J.
85, 274-289
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- Voltage-Gated K Channels.
- C. M. Armstrong (2003)
Sci. STKE
2003, re10
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- Two Components of Voltage-Dependent Inactivation in Cav1.2 Channels Revealed by Its Gating Currents.
- G. Ferreira, E. Rios, and N. Reyes (2003)
Biophys. J.
84, 3662-3678
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