AbstractWe have cloned the human genes encoding the inwardly rectifying K+ (Kir) channel subunits, Kir2.2 (hKir2.2) and its variant, termed hKir2.2v. When expressed in Xenopus oocytes, hKir2.2 produced strong inwardly rectifying K+ currents, whereas the expression of hKir2.2v did not elicit significant currents. Coexpression of hKir2.2v with hKir2.2 showed an hKir2.2v inhibition of hKir2.2 K+ currents, indicating that it acts as a negative regulator of hKir2.2 channel activity. Mutational analysis of hKir2.2v and studies of chimeras between hKir2.2 and hKir2.2v suggest that the intracellular C-terminal region of hKir2.2v participates in the negative regulation of the hKir2.2v channel activity
AbstractThe ROMK1 (Kir 1.1a) channel is formed by a tetrameric complex of subunits, each characteriz...
Abstract: Inwardly rectifying potassium channels (Kir) are a special subset of potassium selective i...
The superfamily of prokaryotic inwardly rectifying (KirBac) potassium channels is homologous to mamm...
AbstractWe have cloned the human genes encoding the inwardly rectifying K+ (Kir) channel subunits, K...
AbstractWe have identified several cDNAs for the human Kir5.1 subunit of inwardly rectifying K+ chan...
AbstractArginine residue at position 285 (R285) in the intracellular C-terminal domain of inward rec...
AbstractA new member of the two transmembrane domain potassium (K+) channel family was identified an...
AbstractPossible heteromultimer formation between Kv- and Kir-type K+ channels was investigated, in ...
AbstractWe have identified several cDNAs for the human Kir5.1 subunit of inwardly rectifying K+ chan...
Kir channels display voltage-dependent block by cytosolic cations such as Mg2+ and polyamines that c...
Kir channels display voltage-dependent block by cytosolic cations such as Mg2+ and polyamines that c...
AbstractInwardly rectifying K+ (Kir) channels are important regulators of resting membrane potential...
AbstractInwardly rectifying potassium channels (Kir), comprising four subunits each with two transme...
AbstractArginine residue at position 285 (R285) in the intracellular C-terminal domain of inward rec...
Inward rectifying potassium: Kir) channels are important in regulating cellular excitability in orga...
AbstractThe ROMK1 (Kir 1.1a) channel is formed by a tetrameric complex of subunits, each characteriz...
Abstract: Inwardly rectifying potassium channels (Kir) are a special subset of potassium selective i...
The superfamily of prokaryotic inwardly rectifying (KirBac) potassium channels is homologous to mamm...
AbstractWe have cloned the human genes encoding the inwardly rectifying K+ (Kir) channel subunits, K...
AbstractWe have identified several cDNAs for the human Kir5.1 subunit of inwardly rectifying K+ chan...
AbstractArginine residue at position 285 (R285) in the intracellular C-terminal domain of inward rec...
AbstractA new member of the two transmembrane domain potassium (K+) channel family was identified an...
AbstractPossible heteromultimer formation between Kv- and Kir-type K+ channels was investigated, in ...
AbstractWe have identified several cDNAs for the human Kir5.1 subunit of inwardly rectifying K+ chan...
Kir channels display voltage-dependent block by cytosolic cations such as Mg2+ and polyamines that c...
Kir channels display voltage-dependent block by cytosolic cations such as Mg2+ and polyamines that c...
AbstractInwardly rectifying K+ (Kir) channels are important regulators of resting membrane potential...
AbstractInwardly rectifying potassium channels (Kir), comprising four subunits each with two transme...
AbstractArginine residue at position 285 (R285) in the intracellular C-terminal domain of inward rec...
Inward rectifying potassium: Kir) channels are important in regulating cellular excitability in orga...
AbstractThe ROMK1 (Kir 1.1a) channel is formed by a tetrameric complex of subunits, each characteriz...
Abstract: Inwardly rectifying potassium channels (Kir) are a special subset of potassium selective i...
The superfamily of prokaryotic inwardly rectifying (KirBac) potassium channels is homologous to mamm...