FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2038482806> ?p ?o ?g. }

• W2038482806 endingPage "593" @default.
• W2038482806 startingPage "586" @default.
• W2038482806 abstract "The DNA sequence encoding the rat brain inward rectifier-10 K+ channel was amplified from rat brain RNA using reverse transcription-polymerase chain reaction and used to clone the human homolog. Low stringency screening of a human kidney cDNA library and subsequent DNA sequence analysis identified two related K+ inward rectifier cDNAs, referred to as Kir1.2 and Kir1.3, which were derived from transcription of distinct human genes. Kir1.2 represents the human homolog of the rat BIRK-10 sequence, whereas Kir1.3 was unique compared with all available sequence data bases. The genes that encode Kir1.2 and Kir1.3 were mapped to human chromosomes 1 and 21, respectively. Both genes showed tissue-specific expression when analyzed by Northern blots. Kir1.2 was only detected in brain kidney and was detected at high levels in all brain regions examined. Kir1.3 was most readily detected in kidney and was also expressed in pancreas > lung. Comparative analysis of the predicted amino acid sequences for Kir1.2 and Kir1.3 revealed they were 62% identical. The most remarkable difference between the two polypeptides is that the Walker Type A consensus binding motif present in both Kir1.1 and Kir1.2 was not conserved in the Kir1.3 sequence. Expression of the Kir1.2 polypeptide in Xenopus oocytes resulted in the synthesis of a K+-selective channel that exhibited an inwardly rectifying current-voltage relationship and was inhibited by external Ba2+ and Cs+. Kir1.2 current amplitude was reduced by >85% when the pH was decreased from pH 7.4 to 5.9 using the membrane-permeant buffer acetate but was relatively unaffected when pH was similarly lowered using membrane-impermeant biphthalate. The inhibition by intracellular protons was voltage-independent with an IC50 of pH 6.2 and a Hill coefficient of 1.9, suggesting the cooperative binding of 2 protons to the intracellular face of the channel. In contrast, Kir1.3 expression in Xenopus oocytes was not detectable despite the fact that the cRNA efficiently directed the synthesis of a polypeptide of the expected Mr in an in vitro translation system. Co-expression of Kir1.3 with either Kir1.1 or Kir1.2 reduced currents resulting from expression of these inward-rectifier subunits alone, consistent with a dominant negative influence on Kir1.1 and Kir 1.2 expression. The DNA sequence encoding the rat brain inward rectifier-10 K+ channel was amplified from rat brain RNA using reverse transcription-polymerase chain reaction and used to clone the human homolog. Low stringency screening of a human kidney cDNA library and subsequent DNA sequence analysis identified two related K+ inward rectifier cDNAs, referred to as Kir1.2 and Kir1.3, which were derived from transcription of distinct human genes. Kir1.2 represents the human homolog of the rat BIRK-10 sequence, whereas Kir1.3 was unique compared with all available sequence data bases. The genes that encode Kir1.2 and Kir1.3 were mapped to human chromosomes 1 and 21, respectively. Both genes showed tissue-specific expression when analyzed by Northern blots. Kir1.2 was only detected in brain kidney and was detected at high levels in all brain regions examined. Kir1.3 was most readily detected in kidney and was also expressed in pancreas > lung. Comparative analysis of the predicted amino acid sequences for Kir1.2 and Kir1.3 revealed they were 62% identical. The most remarkable difference between the two polypeptides is that the Walker Type A consensus binding motif present in both Kir1.1 and Kir1.2 was not conserved in the Kir1.3 sequence. Expression of the Kir1.2 polypeptide in Xenopus oocytes resulted in the synthesis of a K+-selective channel that exhibited an inwardly rectifying current-voltage relationship and was inhibited by external Ba2+ and Cs+. Kir1.2 current amplitude was reduced by >85% when the pH was decreased from pH 7.4 to 5.9 using the membrane-permeant buffer acetate but was relatively unaffected when pH was similarly lowered using membrane-impermeant biphthalate. The inhibition by intracellular protons was voltage-independent with an IC50 of pH 6.2 and a Hill coefficient of 1.9, suggesting the cooperative binding of 2 protons to the intracellular face of the channel. In contrast, Kir1.3 expression in Xenopus oocytes was not detectable despite the fact that the cRNA efficiently directed the synthesis of a polypeptide of the expected Mr in an in vitro translation system. Co-expression of Kir1.3 with either Kir1.1 or Kir1.2 reduced currents resulting from expression of these inward-rectifier subunits alone, consistent with a dominant negative influence on Kir1.1 and Kir 1.2 expression." @default.
• W2038482806 created "2016-06-24" @default.
• W2038482806 creator A5032348579 @default.
• W2038482806 creator A5048027151 @default.
• W2038482806 creator A5053679944 @default.
• W2038482806 creator A5054663939 @default.
• W2038482806 creator A5085161936 @default.
• W2038482806 creator A5088417085 @default.
• W2038482806 date "1997-01-01" @default.
• W2038482806 modified "2023-09-27" @default.
• W2038482806 title "Cloning and Characterization of Two K+ Inward Rectifier (Kir) 1.1 Potassium Channel Homologs from Human Kidney (Kir1.2 and Kir1.3)" @default.
• W2038482806 cites W1544733266 @default.
• W2038482806 cites W1643229297 @default.
• W2038482806 cites W1969018357 @default.
• W2038482806 cites W1983231458 @default.
• W2038482806 cites W1996016170 @default.
• W2038482806 cites W1997883766 @default.
• W2038482806 cites W1999825844 @default.
• W2038482806 cites W2000023611 @default.
• W2038482806 cites W2002128406 @default.
• W2038482806 cites W2014899976 @default.
• W2038482806 cites W2015841601 @default.
• W2038482806 cites W2026846610 @default.
• W2038482806 cites W2028247996 @default.
• W2038482806 cites W2040834181 @default.
• W2038482806 cites W2040917453 @default.
• W2038482806 cites W2043327777 @default.
• W2038482806 cites W2044813037 @default.
• W2038482806 cites W2051729304 @default.
• W2038482806 cites W2055252729 @default.
• W2038482806 cites W2056257770 @default.
• W2038482806 cites W2056283223 @default.
• W2038482806 cites W2058606373 @default.
• W2038482806 cites W2059347766 @default.
• W2038482806 cites W2063840208 @default.
• W2038482806 cites W2067854932 @default.
• W2038482806 cites W2075834102 @default.
• W2038482806 cites W2082549404 @default.
• W2038482806 cites W2083584165 @default.
• W2038482806 cites W2091074829 @default.
• W2038482806 cites W2092552227 @default.
• W2038482806 cites W2092555510 @default.
• W2038482806 cites W2098567877 @default.
• W2038482806 cites W2108019757 @default.
• W2038482806 cites W2129110633 @default.
• W2038482806 cites W2133464980 @default.
• W2038482806 cites W2141400389 @default.
• W2038482806 cites W2147781053 @default.
• W2038482806 cites W2151570285 @default.
• W2038482806 cites W2155525842 @default.
• W2038482806 cites W2263205512 @default.
• W2038482806 cites W2420184510 @default.
• W2038482806 cites W4248147874 @default.
• W2038482806 doi "https://doi.org/10.1074/jbc.272.1.586" @default.
• W2038482806 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8995301" @default.
• W2038482806 hasPublicationYear "1997" @default.
• W2038482806 type Work @default.
• W2038482806 sameAs 2038482806 @default.
• W2038482806 citedByCount "95" @default.
• W2038482806 countsByYear W20384828062012 @default.
• W2038482806 countsByYear W20384828062013 @default.
• W2038482806 countsByYear W20384828062014 @default.
• W2038482806 countsByYear W20384828062015 @default.
• W2038482806 countsByYear W20384828062016 @default.
• W2038482806 countsByYear W20384828062017 @default.
• W2038482806 countsByYear W20384828062019 @default.
• W2038482806 countsByYear W20384828062020 @default.
• W2038482806 countsByYear W20384828062021 @default.
• W2038482806 countsByYear W20384828062022 @default.
• W2038482806 crossrefType "journal-article" @default.
• W2038482806 hasAuthorship W2038482806A5032348579 @default.
• W2038482806 hasAuthorship W2038482806A5048027151 @default.
• W2038482806 hasAuthorship W2038482806A5053679944 @default.
• W2038482806 hasAuthorship W2038482806A5054663939 @default.
• W2038482806 hasAuthorship W2038482806A5085161936 @default.
• W2038482806 hasAuthorship W2038482806A5088417085 @default.
• W2038482806 hasBestOaLocation W20384828061 @default.
• W2038482806 hasConcept C104317684 @default.
• W2038482806 hasConcept C153911025 @default.
• W2038482806 hasConcept C170493617 @default.
• W2038482806 hasConcept C187882448 @default.
• W2038482806 hasConcept C2779535977 @default.
• W2038482806 hasConcept C50254741 @default.
• W2038482806 hasConcept C54355233 @default.
• W2038482806 hasConcept C86803240 @default.
• W2038482806 hasConcept C94924445 @default.
• W2038482806 hasConceptScore W2038482806C104317684 @default.
• W2038482806 hasConceptScore W2038482806C153911025 @default.
• W2038482806 hasConceptScore W2038482806C170493617 @default.
• W2038482806 hasConceptScore W2038482806C187882448 @default.
• W2038482806 hasConceptScore W2038482806C2779535977 @default.
• W2038482806 hasConceptScore W2038482806C50254741 @default.
• W2038482806 hasConceptScore W2038482806C54355233 @default.
• W2038482806 hasConceptScore W2038482806C86803240 @default.
• W2038482806 hasConceptScore W2038482806C94924445 @default.
• W2038482806 hasIssue "1" @default.
• W2038482806 hasLocation W20384828061 @default.
• W2038482806 hasOpenAccess W2038482806 @default.

• next