Evidence map›Paper›PMID 8799166›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Phosphorylation by protein kinase C of serine-23 of the alpha-1 subunit of rat Na+,K(+)-ATPase affects its conformational equilibrium.

N S Logvinenko, I Dulubova, N Fedosova, S H Larsson, A C Nairn, M Esmann, P Greengard, A Aperia

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Identification of a Primary Renal ATCirculation research · 2020
    Article
  3. Defective Renal Angiotensin III and ATJournal of the American Heart Association · 2019
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. 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

8 authors at 2 institutions in 3 countries.

N S LogvinenkoDepartment of Woman and Child Health, Karolinska Institute, Stockholm, Sweden.
I Dulubova
N Fedosova
S H Larsson
A C Nairn
M Esmann
P Greengard
A Aperia
Karolinska Institutet · SERockefeller University · US

Funding

REGION-SPECIFIC PHOSPHOPROTEINS IN THE BASAL GANGLIAP01MH040899 · NIMH · ROCKEFELLER UNIVERSITY · PI GREENGARD, PAUL · 1985 to 2004
$7.0M
NIMH NIH HHS MH 40899
6 · The paper itself

Abstract

Phosphorylation of the alpha-1 subunit of rat Na+,K(+)-ATPase by protein kinase C has been shown previously to decrease the activity of the enzyme in vitro. We have now undertaken an investigation of the mechanism by which this inhibition occurs. Analysis of the phosphorylation of recombinant glutathione S-transferase fusion proteins containing putative cytoplasmic domains of the protein, site-directed mutagenesis, and two-dimensional peptide mapping indicated that protein kinase C phosphorylated the alpha-1 subunit of the rat Na+,K(+)-ATPase within the extreme NH2-terminal domain, on serine-23. The phosphorylation of this residue resulted in a shift in the equilibrium toward the E1 form, as measured by eosin fluorescence studies, and this was associated with a decrease in the apparent K+ affinity of the enzyme, as measured by ATPase activity assays. The rate of transition from E2 to E1 was apparently unaffected by phosphorylation by protein kinase C. These results, together with previous studies that examined the effects of tryptic digestion of Na+,K(+)-ATPase, suggest that the NH2-terminal domain of the alpha-1 subunit, including serine-23, is involved in regulating the activity of the enzyme.

Indexed as

Amino Acid SequenceAnimalsBase SequenceEnzyme InhibitorsEosine Yellowish-(YS)Fluorescent DyesMolecular ProbesMolecular Sequence DataPeptide FragmentsPeptide MappingPhosphopeptidesPhosphoric Monoester HydrolasesPhosphorylationProtein ConformationProtein Kinase CRatsEnzyme InhibitorsEosine Yellowish-(YS)Fluorescent DyesMolecular ProbesPeptide FragmentsPhosphopeptidesPhosphoric Monoester HydrolasesProtein Kinase CRecombinant Fusion ProteinsSerineSodium-Potassium-Exchanging ATPase

Identifiers

PMID8799166
PMCPMC38607
OpenAlexW2146020890

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.