The family of human Na+K+‐ATPase genes

@article{Ovchinnikov1991TheFO,
  title={The family of human Na+K+‐ATPase genes},
  author={Yu. A. Ovchinnikov and Galina Sergeevna Monastyrskaya and Natalia E. Broude and Rando Allikmets and Yuri A Ushkaryov and A M Melkov and Yu.V. Smirnov and I. V. Malyshev and Irina Dulubova and K. E. Petrukhin and A.V. Gryshin and Vladimir E. Sverdlov and Nikita Kiyatkin and Maria B Kostina and Nikolai N. Modyanov and Eugene D. Sverdlov},
  journal={FEBS Letters},
  year={1991},
  volume={213}
}
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The family of human Na,K‐ATPase genesATP1AL1 gene is transcriptionally competent and probably encodes the related ion transport ATPase
Human Na+, K+ ‐ATPase genes
Family of human Na+,K+‐ATPase genes Structure of the putative regulatory region of the α+‐gene
Cloning and characterization of the entire cDNA encoded by ATP1AL1 — a member of the human Na,K/H,K‐ATPase gene family
Structure of the α1 subunit of horse Na,K‐ATPase gene
Advances in Na+,K+‐ATPase studies: from protein to gene and back to protein
Stability of Na(+)-K(+)-ATPase alpha-subunit isoforms in evolution.
TLDR
Encoding DNA for alpha 2- and alpha 3-isoforms of the alpha-subunit of the chicken Na(+)-K(+-ATPase have been cloned, and their nucleotide sequences and deduced amino acid sequences are reported, making possible an assessment of alpha- subunit isoform diversity among vertebrates.
Control region and gastric specific transcription of the rat H+,K+‐ATPase α subunit gene
Mechanisms of urinary K+ and H+ excretion: primary structure and functional expression of a novel H,K-ATPase
TLDR
The findings indicate that the bladder ATPase is a member of a new ion motive P-ATPase subfamily, which may be one of the molecules involved in H+ and K+ homeostasis, mediating the transport of these ions across urinary epithelia and therefore regulating their urinary excretion.
Human nongastric H-K-ATPase : transport properties of ATP 1 al 1 assembled with different-subunits
TLDR
Control trypsinolysis reveals that -isoforms influence the protease sensitivity of AL1 and 1 and that AL1/ complexes, similar to the Na K -ATPase, can undergo distinct K -Na and ouabain-dependent conformational changes.
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References

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Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence.
TLDR
Total genomic Southern hybridization indicated the existence of at most two copies, possibly only one, of the gene encoding the Na,K-ATPase alpha-subunit in the human genome.
Primary structure of the α-subunit of Torpedo californica (Na+ + K+)ATPase deduced from cDNA sequence
TLDR
Cloned and sequenced DNA complementary to the Torpedo californica electroplax messenger RNA encoding the α-subunit of (Na+ + K+)ATPase is cloned and deduced the complete ammo-acid sequence of the polypeptide.
Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA
TLDR
A complementary DNA for the catalytic subunit of the sheep kidney sodium / potassium-dependent ATPase is isolated and characterized and is linked to the phosphorylation site by a 60-amino-acid conserved sequence that may be a major channel for energy transduction.
Two Ca2+ ATPase genes: Homologies and mechanistic implications of deduced amino acid sequences
The catalytic subunits of the (Na+,K+)-ATPase α and α(+) isozymes are the products of different genes
The active site structure of Na+/K+-transporting ATPase: location of the 5'-(p-fluorosulfonyl)benzoyladenosine binding site and soluble peptides released by trypsin.
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    Proceedings of the National Academy of Sciences of the United States of America
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TLDR
To establish any regions of the enzyme protruding from the membrane, the native Na+/K+-transporting ATPase from the electric ray, Torpedo californica, was treated with trypsin; and four peptides, which were released into the water phase, were purified and sequenced.
Possible Functional Differences between the Two Na,K-ATPases of the Brain
Pig kidney Na+,K+‐ATPase
DNA sequencing with chain-terminating inhibitors.
TLDR
A new method for determining nucleotide sequences in DNA is described, which makes use of the 2',3'-dideoxy and arabinon nucleoside analogues of the normal deoxynucleoside triphosphates, which act as specific chain-terminating inhibitors of DNA polymerase.
Nucleotide sequence analysis of DNA. I. Partial sequence of the cohesive ends of bacteriophage lambda and 186 DNA.
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