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Gap Junctional Coupling in Lenses from α8 Connexin Knockout Mice

George J. Baldo,Xiaohua Gong,Francisco J. Martinez-Wittinghan,Nalin M. Kumar,Norton B. Gilula,Richard T. Mathias
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Gating Kinetics of the α1i T-Type Calcium Channel

Charles J. Frazier,Jose R. Serrano,Eric G. George,Xiaofeng Yu,Ahalya Viswanathan,Edward Perez-Reyes,Stephen W. Jones
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The Number of Subunits Comprising the Channel Formed by the T Domain of Diphtheria Toxin

Michael Gordon,Alan Finkelstein
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Prolonged Residence Time of a Noncovalent Molecular Adapter, β-Cyclodextrin, within the Lumen of Mutant α-Hemolysin Pores

Li-Qun Gu,Stephen Cheley,Hagan Bayley
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Potentiation of the Cardiac L-Type Ca2+ Channel (α1C) by Dihydropyridine Agonist and Strong Depolarization Occur via Distinct Mechanisms

Christina M. Wilkens,Manfred Grabner,Kurt G. Beam
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Permeant Ion-Dependent Changes in Gating of Kir2.1 Inward Rectifier Potassium Channels

Tao Lu,Li Wu,Jun Xiao,Jian Yang
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Efficient Coupling of Ligand Binding to Channel Opening by the Binding Domain of a Modulatory (β) Subunit of the Olfactory Cyclic Nucleotide-Gated Channel

Edgar C. Young,Daniel M. Sciubba,Steven A. Siegelbaum
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Hidden Markov Model Analysis of Intermediate Gating Steps Associated with the Pore Gate of Shaker Potassium Channels

Jie Zheng,Lalitha Vankataramanan,Fred J. Sigworth
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Functional Properties of Human Nicotinic Achrs Expressed by Imr-32 Neuroblastoma Cells Resemble Those of α3β4 Achrs Expressed in Permanently Transfected Hek Cells

Mark E. Nelson,Fan Wang,Alexander Kuryatov,Catherine H. Choi,Volodymyr Gerzanich,Jon Lindstrom
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Intracellular Mg2+ Enhances the Function of Bk-Type Ca2+-Activated K+ Channels

Jingyi Shi,Jianmin Cui
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Allosteric Regulation of Bk Channel Gating by Ca2+ and Mg2+ through a Nonselective, Low Affinity Divalent Cation Site

X. Zhang,C.R. Solaro,C.J. Lingle
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Commentary

Kinetic Gating Mechanisms for Bk Channels : When Complexity Leads to Simplicity

Karl L. Magleby
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Correction

Due to an Editorial Error the Words “Which Is” Were Inadvertently Included. the Corrected Sentence Appears below:

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