RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/7890764http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7890764http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7890764http://www.w3.org/2000/01/rdf-schema#comment"Voltage-gated potassium channel beta subunits are cytoplasmic proteins that co-purify with the pore-forming alpha subunits. One of these subunits, Kv beta 1 from rat brain, was previously demonstrated to increase the rate of inactivation of Kv1.1 and Kv1.4 when co-expressed in Xenopus oocytes. We have cloned and characterized a novel voltage-gated K+ channel beta subunit. The cDNA, designated Kv beta 3, has a 408-amino acid open reading frame. It possesses a unique 79-amino acid N-terminal leader, but is identical with rat Kv beta 1 over the 329 C-terminal amino acids. The Kv beta 3 transcript was found in many tissues, but was most abundant in aorta and left ventricle of the heart. Co-expression of Kv beta 3 with K+ channel alpha subunits shows that this beta subunit can increase the rate of inactivation from 4-to 7-fold in a Kv1.4 or Shaker B channel. Kv beta 3 had no effect on Kv1.1, unlike Kv beta 1 which can increase rate of inactivation of this alpha subunit more than 100-fold. Other kinetic parameters were unaffected. This study shows that voltage-gated K+ channel beta subunits are present outside the central nervous system, and that at least one member of this family selectively modulates inactivation of K+ channel alpha subunits."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.11.6272"xsd:string
http://purl.uniprot.org/citations/7890764http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.11.6272"xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/author"Morales M.J."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/author"Morales M.J."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/author"Castellino R.C."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/author"Castellino R.C."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/author"Crews A.L."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/author"Crews A.L."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/author"Rasmusson R.L."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/author"Rasmusson R.L."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/author"Strauss H.C."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/author"Strauss H.C."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/pages"6272-6277"xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/pages"6272-6277"xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/title"A novel beta subunit increases rate of inactivation of specific voltage-gated potassium channel alpha subunits."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/title"A novel beta subunit increases rate of inactivation of specific voltage-gated potassium channel alpha subunits."xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/7890764http://purl.uniprot.org/core/volume"270"xsd:string