Evidence map›Paper›PMID 7510407›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

K+ currents expressed from the guinea pig cardiac IsK protein are enhanced by activators of protein kinase C.

Z J Zhang, N K Jurkiewicz, K Folander, E Lazarides, J J Salata, R Swanson

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Article
  6. Article
  7. O-glycosylation of the cardiac I(Ks) complex.The Journal of physiology · 2011
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
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  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Z J ZhangDepartment of Pharmacology, Merck Research Laboratories, West Point, PA 19486.
N K Jurkiewicz
K Folander
E Lazarides
J J Salata
R Swanson
United States Military Academy · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have isolated cardiac cDNA and genomic clones encoding the guinea pig IsK protein. The deduced amino acid sequence is approximately 78% identical to the rat, mouse, and human variants of this channel, and the structure of the gene encoding the protein is also similar to that in other species. For example, the gene is present only once in the haploid genome, the protein-coding sequence is present on a single uninterrupted exon, an intron exists in the 5' untranslated domain, and multiple alternative polyadenylation sites are used in processing the transcript. Expression of the guinea pig protein in Xenopus oocytes results in a slowly activating, voltage-dependent K+ current, IsK, similar to those expressed previously from the rat, mouse, and human genes. However, in sharp contrast to the rat and mouse currents, activation of protein kinase C with phorbol esters increases the amplitude of the guinea pig IsK current, analogous to its effects on the endogenous IKs current in guinea pig cardiac myocytes. Mutagenesis of the guinea pig cDNA to alter four cytoplasmic amino acid residues alters the phenotype of the current response to protein kinase C from enhancement to inhibition, mimicking that of rat and mouse IsK currents. This mutation is consistent with reports that phosphorylation of Ser-102 by protein kinase C decreases the current amplitude. These data explain previously reported differences in the regulatory properties between recombinant rat or mouse IsK channels and native guinea pig IKs channels and provide further evidence that the IsK protein forms the channels that underlie the IKs current in the heart.

Indexed as

Potassium ChannelsPotassium Channels, Voltage-GatedAmino Acid SequenceAnimalsBase SequenceCloning, MolecularDNA, ComplementaryEnzyme ActivationFemaleGuinea PigsHumansIon ChannelsMembrane ProteinsMiceMolecular Sequence DataMutagenesis, Site-DirectedDNA, ComplementaryIon ChannelsMembrane ProteinsPotassiumpotassium channel protein I(sk)Potassium ChannelsPotassium Channels, Voltage-GatedProtein Kinase C

Identifiers

PMID7510407
PMCPMC43244
OpenAlexW2142133653

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.