AbstractPossible heteromultimer formation between Kv- and Kir-type K+ channels was investigated, in connection with the known functional diversity of K+ channels in vivo. Voltage-clamp experiments were performed on Xenopus oocytes, either injected with concatenated Kir2.1-Kv1.1 mRNA, or co-injected with Kv1.1 and Kir2.1 mRNA. K+ currents could be approximated by the algebraic sum of the 2 K+ current types alone. The tandem construct did not show functional expression, although it could be detected by Western blotting. We conclude that Kv1.1 and Kir2.1 α-subunit proteins fail to assemble and do not contribute functional diversity to K+ channels
AbstractThe inwardly-rectifying potassium channel subunit Kir5.1 selectively co-assembles with membe...
AbstractMembers of different voltage-gated K+ channel subfamilies usually do not form heteromultimer...
Potassium (K+) channel pore-forming (a) subunits are by far one of the most diverse groups of channe...
AbstractHeteromultimer formation between Kv potassium channel subfamilies with the production of a n...
Sequence similarity among and electrophysiological studies of known potassium channels, along with t...
K+ channel function is regulated through the assembly of channel subunit isoforms into either homo- ...
AbstractSingle K+ channels were recorded under the cell-attached mode in Xenopus oocytes injected wi...
AbstractThe ROMK1 (Kir 1.1a) channel is formed by a tetrameric complex of subunits, each characteriz...
Cloning and sequencing of cDNAs isolated from a rat cortex cDNA library reveals that a gene family e...
Four copies of the coding sequence for a voltage-dependent potassium channel (RBK1, rat Kv1.1) were ...
Four copies of the coding sequence for a voltage-dependent potassium channel (RBK1, rat Kv1.1) were ...
AbstractWe have cloned the human genes encoding the inwardly rectifying K+ (Kir) channel subunits, K...
AbstractInwardly rectifying potassium channels have an important role in determining the resting pot...
An important step towards understanding the molecular basis of the functional diversity of voltage-g...
An important step towards understanding the molecular basis of the functional diversity of voltage-g...
AbstractThe inwardly-rectifying potassium channel subunit Kir5.1 selectively co-assembles with membe...
AbstractMembers of different voltage-gated K+ channel subfamilies usually do not form heteromultimer...
Potassium (K+) channel pore-forming (a) subunits are by far one of the most diverse groups of channe...
AbstractHeteromultimer formation between Kv potassium channel subfamilies with the production of a n...
Sequence similarity among and electrophysiological studies of known potassium channels, along with t...
K+ channel function is regulated through the assembly of channel subunit isoforms into either homo- ...
AbstractSingle K+ channels were recorded under the cell-attached mode in Xenopus oocytes injected wi...
AbstractThe ROMK1 (Kir 1.1a) channel is formed by a tetrameric complex of subunits, each characteriz...
Cloning and sequencing of cDNAs isolated from a rat cortex cDNA library reveals that a gene family e...
Four copies of the coding sequence for a voltage-dependent potassium channel (RBK1, rat Kv1.1) were ...
Four copies of the coding sequence for a voltage-dependent potassium channel (RBK1, rat Kv1.1) were ...
AbstractWe have cloned the human genes encoding the inwardly rectifying K+ (Kir) channel subunits, K...
AbstractInwardly rectifying potassium channels have an important role in determining the resting pot...
An important step towards understanding the molecular basis of the functional diversity of voltage-g...
An important step towards understanding the molecular basis of the functional diversity of voltage-g...
AbstractThe inwardly-rectifying potassium channel subunit Kir5.1 selectively co-assembles with membe...
AbstractMembers of different voltage-gated K+ channel subfamilies usually do not form heteromultimer...
Potassium (K+) channel pore-forming (a) subunits are by far one of the most diverse groups of channe...