Cui J , Cox DH , Aldrich RW .

MH 48108 NIMH NIH HHS

	Scheme I.
	Figure 2. Activation of mslo currents. (A–E) Current traces from a single membrane patch recorded after a series of depolarizations to increasingly more positive membrane voltages. [Ca]i were as indicated (top to bottom) 0.84, 1.7, 10.2, 124, and 1,000 μM. Each series displayed is the average of 4 series recorded consecutively under identical conditions. Depolarizations were for 20 ms. Repolarizations were to −80 mV. In the left panels complete series are displayed. The voltage increment is 10 mV. In the middle panels a subset of traces have been expanded and fitted with single exponential functions (dashed curves). The voltage increment is 20 mV. In the right panels are shown plots of activation time constants as a function of test potential. The later portions of these curves are fitted with the function τ = Ae−qFV/RT + b (solid curves). (A) 0.84 μM [Ca]i, Vhold = −50 mV: (left) depolarizations ranged from 0 to +200 mV. (middle) Depolarizations ranged from +80 to +160 mV; (right) fit parameters: range +130 to 200 mV, q = 0.77, b = 1.3 ms. (B) 1.7 μM [Ca]i, Vhold = −80 mV: (left) depolarizations ranged from −40 to +200 mV in 10-mV increments; (middle) depolarizations ranged from +60 to +140 mV; (right) fit parameters: range +120 to 200 mV, q = 0.76, b = 0.76 ms. (C) 10.2 μM [Ca]i, Vhold = −100 mV: (left) depolarizations ranged from −80 to +150 mV; (middle) depolarizations ranged from +30 to +110 mV; (right) fit parameters: range +90 to +150 mV, q = 0.63, b = 0.16 ms (D) 124 μM [Ca]i, Vhold = −120 mV: (left) depolarizations ranged from −120 to +110 mV; (middle) depolarizations ranged from +10 to +110 mV; (right) fit parameters: range −10 to +110 mV, q = 0.52, b = 0.01 ms. (E) 1,000 μM [Ca]i, Vhold = −180 mV: (left) depolarizations ranged from −180 to +100 mV; (middle) depolarizations ranged from +20 to +100 mV; (right) fit parameters: range −10 to +100 mV q = 0.64, b = 0.23 ms.
	Figure 3. Deactivation of mslo currents. (A–E) Tail current families recorded from a single membrane patch. [Ca]i were as indicated (top to bottom): 0.84, 1.7, 10.2, 124, and 1,000 μM. Each family displayed is the average of 4 series recorded consecutively under identical conditions. Depolarizations are for 20 ms. Repolarizations are for 10 ms. In the left panels complete series are displayed. The voltage increment is 10 mV. In the middle panels subsets of traces from the left have been expanded and fitted with single exponential functions (dashed curves). The voltage increment is 20 mV. In the right panels are displayed plots of the deactivation time constant as a function of test potential. The most hyperpolarized portions of these curves are fitted with the function τ = Ae  qF   V/RT+ b (solid curves). (A) 0.84 μM [Ca2+]i: prepulse potential: 180 mV. Test potentials: −50 to 100 mV, q = 0.62, b = 0.069. (B) 1.7 μM [Ca2+]i: prepulse potential: 160 mV. Test potentials: −80 to 70 mV, q = 0.74, b = 0.223. (C) 10.2 μM [Ca2+]i: prepulse potential: 100 mV. Test potentials: −130 to 30 mV, q = 0.67, b = 0.176. (D) 124 μM [Ca2+]i: prepulse potential: 80 mV. Test potentials: −150 to 20 mV, q = 0.68, b = 0.226. (E) 1,000 μM [Ca2+]i: prepulse potential: 50 mV. Test potentials: −200 to −50 mV, q = 0.67, b = 0.163.
	Figure 4. Mean activation and deactivation time constant as a function of both voltage and [Ca]i. Displayed are semi-log plots of activation (A) and deactivation (B) time constants. Each curve represents the mean of between 4 and 10 experiments. Error bars indicate standard errors of the mean. Solid lines represent fits to the function τ = Ae−qFV/RT. Fits were done by eye. Fit parameters: (A) [Ca]i = 0.84 μM (•), n = 4, q = 0.46; [Ca]i = 1.7 μM (*), n = 10, q = 0.44; [Ca]i = 4.5 μM (□), n = 9, q = 0.51; [Ca]i = 10.2 μM (▪), n = 7, q = 0.50; [Ca]i = 124 μM (▴), n = 7, q = 0.45; [Ca]i = 1,000 μM (▸◂), n = 5, q = 0.45. (B) [Ca]i = 0.84 μM (•), n = 7, q = −0.48; [Ca]i = 1.7 μM (*), n = 6, q = −0.46; [Ca]i = 4.5 μM (□), n = 7, q = −0.42; [Ca]i = 10.2 μM (▪), n = 10, q = −0.46; [Ca]i = 124 μM (▴), n = 9, q = −0.43; [Ca]i = 1,000 μM (▸◂), n = 10, q = −0.38.
	Figure 5. Normalized conductance vs. voltage relations from a single membrane patch (A) and the average of several patches (B) are displayed for the following [Ca]i: 0.84 (•), 1.7 (*), 4.6 (□), 10.2 (▪), 65 (▵), 124 (▴), 490 (▿), 1,000 μM (▸◂). Relative conductance was determined for each test potential by measuring the tail current amplitude 200 μs after repolarization to −80 mV. The data were fitted (solid curve) with the Boltzmann function G = Gmax(1/(1+e−(V−V1/2)zF/RT)) and then normalized to the maximum of the fit. Curves plotted with filled symbols represent approximately 10-fold increases in [Ca]i, as do curves plotted with open symbols. (C) Plot of the voltage at half maximal activation V1/2 vs. [Ca]i as determined from fits to the data in A (•). Also plotted are the mean V1/2 values from several individual experiments (□). Error bars represent standard error of the mean with n = 11, 13, 11, 16, 10, 15 14, 13 for [Ca]i = 0.84, 1.7, 4.6, 10.2, 65, 124, 490, 1,000 μM, respectively. In A and B the parameters of the fits were as follows: (A) [Ca]i = 0.84 μM, V1/2 = 99.0 mV, z = 1.8; [Ca]i = 1.7 μM, V1/2 = 85.6 mV, z = 1.88; [Ca]i = 4.6 μM, V1/2 = 49.4 mV, z = 1.62; [Ca]i = 10.2 μM, V1/2 = 28.2 mV, z = 1.44; [Ca]i = 65 μM, V1/2 = −6.2 mV, z = 1.27; [Ca]i = 124 μM, V1/2 = −16.7 mV, z = 1.27; [Ca]i = 490 μM, V1/2 = −32.7, z = 1.13; [Ca]i = 1,000 μM, V1/2 = −41.8 mV, z = 1.18. (B) [Ca]i = 0.84 μM, V1/2 = 107 mV, z = 1.52, n = 5; [Ca]i = 1.7 μM, V1/2 = 81.5 mV, z = 1.56, n = 10; [Ca]i = 4.6 μM, V1/2 = 49.6 mV, z = 1.44, n = 9; [Ca]i = 10.2 μM, V1/2 = 32.0 mV, z = 1.27, n = 7; [Ca]i = 65 μM, V1/2 = −2.7 mV, z = 1.24, n = 8; [Ca]i = 124 μM, V1/2 = −11.8 mV, z = 1.20, n = 7; [Ca]i = 490 μM, V1/2 = −19.4, z = 1.09, n = 8; [Ca]i = 1,000 μM, V1/2 = −38.9 mV, z = 1.08, n = 5.
	Figure 6. Ca dependence of mslo currents. (A) Current traces recorded during 20-ms depolarizations to +70 mV at a series of [Ca]i. [Ca]i are, in alphabetical order: 0.84, 1.7, 4.5, 10.2, 124, 1,000 μM. In (B) several of the currents from A have been normalized to their maximum and superimposed for comparison. Also displayed are single exponential fits to the time course of activation (dashed lines). (C) Tail currents were recorded at −80 mV after 20-ms voltage steps to +100 mV. These currents were then normalized to their minimums and superimposed. [Ca]i are as indicated. Also displayed are single exponential fits to the time course of deactivation (dashed lines). In (D) the fraction of channels activated in A is plotted as a function of [Ca]i. Normalized conductances (G/Gmax) were derived from conductance-voltage relations determined at each [Ca]i from tail current measurements as described for Fig. 5. The data are fitted (solid curve) to the equation: G/Gmax = Amp(1/{1+(KD/[Ca])n}) with the following parameters (Amp = 0.99, KD = 1.44 μM, n = 3.08). In E and F the macroscopic rate constants for current activation E and deactivation F, as determined from single exponential fits, are plotted as a function of [Ca]i. In E the data are fitted with two functions. The solid curve represents a fit to Eq. 3 with α = 2.88 ms−1, k−1/k1 = 20.8 μM, and β = 0. The dashed curve represents a fit to Eq. 4 with α = 2.89 ms−1, k−1/k1 = 20 μM, β = 0.3, and k−3/k3 = 10 μM. In F the data are fitted with Eq. 4 with α = 0.74 ms−1, k−1/k1 = 20 μM, β = 3.40, and k−3/k3 = 10 μM.
	Scheme II.
	Scheme III.
	Scheme IV.
	Figure 7. (A) The mslo macroscopic activation rate constant (1/ time constant) is plotted as a function of [Ca]i for several different membrane voltages. Data are from a single membrane patch. Macroscopic rate constants were determined from exponential fits to the time course of activation. Voltages descend from top to bottom as indicated. Alternating open and closed markers have been used for ease of distinguishing data at differing voltages. Each data set has been fitted (solid curve) with the function 1/τ = Amp/{1+(KD/ [Ca]i)}. To minimize the effects of outlying points an absolute, sum of squares criteria was used in fitting. The parameters from these fits, Amp (maximum macroscopic rate constant), and KD (apparent Ca2+ dissociation constant) are plotted as a function of membrane voltage in B and C (•). Also included in B and C are mean values from 5 experiments (○). Error bars represent standard errors of the mean.
	Figure 8. mslo currents at very low [Ca]i. (A) Currents were elicited with depolarizing steps to test potentials ranging from +60 to +200 mV in 20-mV increments. Vhold = −50 mV. Included in the internal solution was 5 mM EGTA. No HEDTA or Ca2+ was added. The calculated free [Ca]i in this solution was ∼0.5 nM assuming contaminant Ca2+ of 10 to 20 μM (see materials and methods). The traces displayed are the average from 5 series recorded consecutively. (B) Peak current values from the data in A are plotted as a function of membrane voltage (•). Also included is the peak current measured from the same patch with a step to +200 mV while the patch was superfused with 124 μM [Ca]i (▴).
	Figure 9. Currents recorded at high voltage and very low [Ca]i are passing through mslo channels. (A) Control currents recorded from an oocyte not injected with RNA. Currents shown were elicited with 50-ms voltage steps to potentials ranging from +60 to +200 mV in 20-mV increments. Vhold = −50 mV. (B) Correlation between the amplitudes of mslo currents recorded from the same patches with ∼0.5 nM (ordinate) or 124 μM (abscissa) [Ca]i. Each symbol represents an individual experiment. Amplitudes were measured at the end of 50-ms depolarizations to +200 mV. Vhold = −50 mV (0.5 nM [Ca]i); Vhold = −120 mV (124 μM [Ca]i). (C) Current traces recorded from an outside out membrane patch with voltage steps to from −50 to +200 mV before (control), during (3 mM TEA), and after (recovery) exposure of the external surface of the patch to 3 mM TEA. In the lower panel the time course of TEA block is displayed. Data points were recorded at 2-s intervals. (D) Single channel current traces recorded from inside out membrane patches pulled from oocytes injected with a low concentration of mslo RNA, at ∼2 and 10.2 μM [Ca]i. Voltage steps were to +180 mV.
	Figure 10. Rapid activation of mslo currents at very low [Ca]i. The two current traces displayed were recorded from the same membrane patch with 10.2 μM and ∼0.5 nM [Ca]i (5 mM EGTA no added Ca2+) as indicated. The traces shown represent the average of 5 (10.2 μM [Ca]i) and 8 (∼0.5 nM [Ca]i) traces recorded in consecutive current families. Voltage steps were from −100 to +170 mV at 10.2 μM [Ca]i, and from 0 to +250 mV at ∼0.5 nM [Ca]i. The ∼0.5 nM [Ca]i trace was fitted with a single exponential function with a time constant of 1.15 ms. The fit is superimposed on the data (dashed line).
	Figure 11. mslo currents are insensitive to changes in [Ca]i in the low nanomolar range. (A) mslo currents recorded from a single membrane patch at the indicated [Ca]i. Internal solutions were prepared from the standard solution as follows: 0.5 nM (no added Ca2+, 5 mM EGTA), 2 nM (no added Ca2+, 1 mM EGTA), 10 nM (0.28 mM added CaCl2, 5 mM EGTA), 50 nM (1.18 mM added CaCl2, 5 mM EGTA). The order of solution presentation was as follows 2 nM (*), 0.5 nM (○), 10 nM (□), 50 nM (▵), 0.5 nM again (•), 2 nM again (#). (B) Time constants of activation for currents in A are plotted as a function [Ca]i. Each symbol represents data from a different test potential as indicated. The data points at +200 mV have been connected (solid line). Time constants were determined by fitting the time course of activation with a single exponential function.
	Figure 12. (A) mslo current families recorded from the same membrane patch at 10.2 μM and ∼0.5 nM [Ca]i. Each family displayed is the average of 5 (10.2 μM) and 8 (∼0.5 nM) families recorded in succession. (B) Mean mslo G-V curves recorded from 6 membrane patches with 10.2 μM [Ca]i before (▪) and after (□) superfusion with ∼0.5 nM [Ca]i (•). In three patches current families were determined with ∼0.5 nM [Ca]i with voltages up to +280 mV (○). Error bars represent standard errors of the mean. G-V curves were fit with the Boltzmann function G = Gmax(1/ {1+e−(V−V1/2)zF/RT}) and then normalized to the maximum of the fit. Fit parameters were as follows: (▪) V1/2 = 36 mV, z = 1.18; (□) V1/2 = 50 mV, z = 1.19; (•) V1/2 = 195 mV, z = 0.87; (○) V1/2 = 197 mV, z = 0.83.
	Figure 13. Ca-dependence of mslo currents. (A) Conductance vs. voltage (G-V) relations at the following [Ca]i: 0.84, 1.7, 4.5, 10.2, 65, 124, 490, 1,000 μM where constructed from tail current amplitudes measured 0.2-ms after repolarization from the appropriate test potential to −80 mV. Each G-V curve was then fitted with a Boltzmann function and normalized to the maximum of the fit. These data were transformed to dose-response form for each voltage and displayed in A. Smooth curves represent fits to the Hill equation G/Gmax = Amp/{1+(KD/[Ca])n}, were n = Hill coefficient, and KD = apparent Ca2+ dissociation constant. Voltages descend from left to right starting at +90 mV and ending at −50 mV in 20-mV increments. Alternating open and closed markers have been used for ease of distinguishing data at differing voltages. The data are from the same membrane patch. In (B ) the amplitudes of each fit in A are plotted as a function of voltage. In (C) Hill coefficients, and in (D) apparent dissociation constants determined from the curves in A are also plotted as a function of voltage. In B, C, and D closed circles represent parameters determined from the fits in A. Open circles represent the mean values from 5 experiments. The mean data in D have been fitted (solid line) with the function KD(V) = KD(0)e−zFV/RT with KD(0) = 35.2 μM and z = 1.18. Error bars indicate standard errors of the mean.
	Figure 14. mslo G-V relations fitted with Boltzmann functions raised to powers between 1 and 4. Displayed are semi-log plots of the mslo G-V relation determined with 0.84 (A), 10.2 (B), and 124 (C) μM [Ca]i. Each data set represents the mean of from 5 to 8 experiments. These data are the same as that displayed in Fig. 5 B. Each curve has been fitted with the function G/Gmax = A[1/ (1+e−(V−V1/2)zF/RT)]n. Curves corresponding to the best fit with n = 1, 2, 3, and 4 have been superimposed on the data. For each [Ca]i a fit with n varying freely is also displayed. The line type indicating n, as well as the fit parameter z, are as indicated on the figure.
	Scheme VI.
	Scheme V.

Adelman, Calcium-activated potassium channels expressed from cloned complementary DNAs. 1992, Pubmed, Xenbase

Adelman, Calcium-activated potassium channels expressed from cloned complementary DNAs. 1992, Pubmed , Xenbase
Aggarwal, Contribution of the S4 segment to gating charge in the Shaker K+ channel. 1996, Pubmed , Xenbase
Art, The calcium-activated potassium channels of turtle hair cells. 1995, Pubmed
Atkinson, A component of calcium-activated potassium channels encoded by the Drosophila slo locus. 1991, Pubmed
Barrett, Properties of single calcium-activated potassium channels in cultured rat muscle. 1982, Pubmed
Blair, Developmental acquisition of Ca2+-sensitivity by K+ channels in spinal neurones. , Pubmed , Xenbase
Butler, mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels. 1993, Pubmed , Xenbase
Chandler, The effect of changing the internal solution on sodium inactivation and related phenomena in giant axons. 1965, Pubmed
Cornejo, Modification of Ca2+-activated K+ channels in cultured medullary thick ascending limb cells by N-bromoacetamide. 1987, Pubmed
Cox, Separation of gating properties from permeation and block in mslo large conductance Ca-activated K+ channels. 1997, Pubmed
DiChiara, Distinct effects of Ca2+ and voltage on the activation and deactivation of cloned Ca(2+)-activated K+ channels. 1995, Pubmed , Xenbase
Diaz, Interaction of internal Ba2+ with a cloned Ca(2+)-dependent K+ (hslo) channel from smooth muscle. 1996, Pubmed , Xenbase
FRANKENHAEUSER, The action of calcium on the electrical properties of squid axons. 1957, Pubmed
Fabiato, Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. 1979, Pubmed
Findlay, High-conductance K+ channel in pancreatic islet cells can be activated and inactivated by internal calcium. 1985, Pubmed
Getzoff, Faster superoxide dismutase mutants designed by enhancing electrostatic guidance. 1992, Pubmed
Giangiacomo, Functional reconstitution of the large-conductance, calcium-activated potassium channel purified from bovine aortic smooth muscle. 1995, Pubmed
Golowasch, Allosteric effects of Mg2+ on the gating of Ca2+-activated K+ channels from mammalian skeletal muscle. 1986, Pubmed
Grissmer, Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. 1994, Pubmed
Heginbotham, A functional connection between the pores of distantly related ion channels as revealed by mutant K+ channels. 1992, Pubmed , Xenbase
Heginbotham, Mutations in the K+ channel signature sequence. 1994, Pubmed , Xenbase
Hille, Negative surface charge near sodium channels of nerve: divalent ions, monovalent ions, and pH. 1975, Pubmed
Hudspeth, A model for electrical resonance and frequency tuning in saccular hair cells of the bull-frog, Rana catesbeiana. 1988, Pubmed
Hudspeth, Kinetic analysis of voltage- and ion-dependent conductances in saccular hair cells of the bull-frog, Rana catesbeiana. 1988, Pubmed
Karpen, Gating kinetics of the cyclic-GMP-activated channel of retinal rods: flash photolysis and voltage-jump studies. 1988, Pubmed
Kaupp, Primary structure and functional expression from complementary DNA of the rod photoreceptor cyclic GMP-gated channel. 1989, Pubmed , Xenbase
Lagrutta, Functional differences among alternatively spliced variants of Slowpoke, a Drosophila calcium-activated potassium channel. 1994, Pubmed
Larsson, Transmembrane movement of the shaker K+ channel S4. 1996, Pubmed , Xenbase
Latorre, Reconstitution in planar lipid bilayers of a Ca2+-dependent K+ channel from transverse tubule membranes isolated from rabbit skeletal muscle. 1982, Pubmed
Latorre, Varieties of calcium-activated potassium channels. 1989, Pubmed
Liman, Voltage-sensing residues in the S4 region of a mammalian K+ channel. 1991, Pubmed , Xenbase
Logothetis, Gating charge differences between two voltage-gated K+ channels are due to the specific charge content of their respective S4 regions. 1993, Pubmed , Xenbase
Lopez, Hydrophobic substitution mutations in the S4 sequence alter voltage-dependent gating in Shaker K+ channels. 1991, Pubmed , Xenbase
Lux, Single channel activity associated with the calcium dependent outward current in Helix pomatia. 1981, Pubmed
MacKinnon, Mutations affecting TEA blockade and ion permeation in voltage-activated K+ channels. 1990, Pubmed
Mannuzzu, Direct physical measure of conformational rearrangement underlying potassium channel gating. 1996, Pubmed , Xenbase
Markwardt, Gating of maxi K+ channels studied by Ca2+ concentration jumps in excised inside-out multi-channel patches (myocytes from guinea pig urinary bladder). 1992, Pubmed
Marty, Ca-dependent K channels with large unitary conductance in chromaffin cell membranes. 1981, Pubmed
Marty, The physiological role of calcium-dependent channels. 1989, Pubmed
McCobb, A human calcium-activated potassium channel gene expressed in vascular smooth muscle. 1995, Pubmed , Xenbase
McManus, Accounting for the Ca(2+)-dependent kinetics of single large-conductance Ca(2+)-activated K+ channels in rat skeletal muscle. 1991, Pubmed
McManus, Calcium-activated potassium channels: regulation by calcium. 1991, Pubmed
McManus, Functional role of the beta subunit of high conductance calcium-activated potassium channels. 1995, Pubmed , Xenbase
McManus, Kinetic states and modes of single large-conductance calcium-activated potassium channels in cultured rat skeletal muscle. 1988, Pubmed
McManus, Inverse relationship of the durations of adjacent open and shut intervals for C1 and K channels. , Pubmed
Meera, A calcium switch for the functional coupling between alpha (hslo) and beta subunits (KV,Ca beta) of maxi K channels. 1996, Pubmed , Xenbase
Methfessel, The gating of single calcium-dependent potassium channels is described by an activation/blockade mechanism. 1982, Pubmed
Moczydlowski, Gating kinetics of Ca2+-activated K+ channels from rat muscle incorporated into planar lipid bilayers. Evidence for two voltage-dependent Ca2+ binding reactions. 1983, Pubmed
Neyton, A Ba2+ chelator suppresses long shut events in fully activated high-conductance Ca(2+)-dependent K+ channels. 1996, Pubmed
Oberhauser, Activation by divalent cations of a Ca2+-activated K+ channel from skeletal muscle membrane. 1988, Pubmed
Pak, A mouse brain homolog of the Drosophila Shab K+ channel with conserved delayed-rectifier properties. 1991, Pubmed , Xenbase
Pallotta, N-bromoacetamide removes a calcium-dependent component of channel opening from calcium-activated potassium channels in rat skeletal muscle. 1985, Pubmed
Pallotta, Single channel recordings of Ca2+-activated K+ currents in rat muscle cell culture. 1981, Pubmed
Pallotta, Calcium-activated potassium channels in rat muscle inactivate from a short-duration open state. 1985, Pubmed
Pallotta, Single channel recordings from calcium-activated potassium channels in cultured rat muscle. 1983, Pubmed
Papazian, Alteration of voltage-dependence of Shaker potassium channel by mutations in the S4 sequence. 1991, Pubmed , Xenbase
Perozo, S4 mutations alter gating currents of Shaker K channels. 1994, Pubmed , Xenbase
Pérez, Reconstitution of expressed KCa channels from Xenopus oocytes to lipid bilayers. 1994, Pubmed , Xenbase
Salomao, Effect of trypsin on a Ca(2+)-activated K+ channel reconstituted into planar phospholipid bilayers. 1992, Pubmed
Schoppa, The size of gating charge in wild-type and mutant Shaker potassium channels. 1992, Pubmed
Seoh, Voltage-sensing residues in the S2 and S4 segments of the Shaker K+ channel. 1996, Pubmed , Xenbase
Shen, Tetraethylammonium block of Slowpoke calcium-activated potassium channels expressed in Xenopus oocytes: evidence for tetrameric channel formation. 1994, Pubmed , Xenbase
Sigworth, Voltage gating of ion channels. 1994, Pubmed
Singer, Characterization of calcium-activated potassium channels in single smooth muscle cells using the patch-clamp technique. 1987, Pubmed
Stevens, Interactions between intrinsic membrane protein and electric field. An approach to studying nerve excitability. 1978, Pubmed
Stühmer, Structural parts involved in activation and inactivation of the sodium channel. 1989, Pubmed , Xenbase
Tseng-Crank, Cloning, expression, and distribution of functionally distinct Ca(2+)-activated K+ channel isoforms from human brain. 1994, Pubmed , Xenbase
Wallner, Characterization of and modulation by a beta-subunit of a human maxi KCa channel cloned from myometrium. 1995, Pubmed , Xenbase
Wallner, Determinant for beta-subunit regulation in high-conductance voltage-activated and Ca(2+)-sensitive K+ channels: an additional transmembrane region at the N terminus. 1996, Pubmed
Wei, Calcium sensitivity of BK-type KCa channels determined by a separable domain. 1994, Pubmed
Wei, Occult Drosophila calcium channels and twinning of calcium and voltage-activated potassium channels. 1986, Pubmed
Wong, Single calcium-dependent potassium channels in clonal anterior pituitary cells. 1982, Pubmed
Woodhull, Ionic blockage of sodium channels in nerve. 1973, Pubmed
Wu, A kinetic description of the calcium-activated potassium channel and its application to electrical tuning of hair cells. 1995, Pubmed
Yang, Molecular basis of charge movement in voltage-gated sodium channels. 1996, Pubmed
Yang, Evidence for voltage-dependent S4 movement in sodium channels. 1995, Pubmed
Yellen, Mutations affecting internal TEA blockade identify the probable pore-forming region of a K+ channel. 1991, Pubmed
Yool, Alteration of ionic selectivity of a K+ channel by mutation of the H5 region. 1991, Pubmed , Xenbase
Zagotta, Shaker potassium channel gating. III: Evaluation of kinetic models for activation. 1994, Pubmed , Xenbase
Zagotta, Shaker potassium channel gating. II: Transitions in the activation pathway. 1994, Pubmed , Xenbase