Evidence map›Paper›PMID 1656454›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1991

The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase.

W Lorenz, J Inglese, K Palczewski, J J Onorato, M G Caron, R J Lefkowitz

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

40 citing papers in PubMed, 189 citations in OpenAlex.

  1. Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024
    Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Targeting G protein-coupled receptor kinases (GRKs) to G protein-coupled receptors.Current opinion in endocrine and metabolic research · 2021
    Article
  7. Review
  8. Review
  9. A Brief History of the β-Arrestins.Methods in molecular biology (Clifton, N.J.) · 2019
    Review
  10. Article
  11. Article
  12. Review
  13. Chemistry and biology of the initial steps in vision: the Friedenwald lecture.Investigative ophthalmology & visual science · 2014
    Article
  14. Article
  15. The functional cycle of visual arrestins in photoreceptor cells.Progress in retinal and eye research · 2011
    Review
  16. Introduction of Robert J. Lefkowitz.The Journal of clinical investigation · 2011
    Article
  17. Arrestin in ciliary invertebrate photoreceptors: molecular identification and functional analysis in vivo.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    Article
  18. Review
  19. Review
  20. 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.

W LorenzHoward Hughes Medical Institute, Department of Biochemistry, Duke University Medical Center, Durham, NC 27710.
J Inglese
K Palczewski
J J Onorato
M G Caron
R J Lefkowitz
Howard Hughes Medical Institute · US

Funding

Molecular Regulation of Cardiovascular 7 TM ReceptorsR01HL016037 · NHLBI · DUKE UNIVERSITY · PI ROBERT J LEFKOWITZ · 1985 to 2026
$14.5M
MOLECULAR PROPERTIES OF CARDIAC ADRENERGIC RECEPTORSR37HL016037 · NHLBI · DUKE UNIVERSITY · PI LEFKOWITZ, ROBERT J · 1986 to 1995
–
NEI NIH HHS EY0806NHLBI NIH HHS HL16037
6 · The paper itself

Abstract

Light-dependent deactivation of rhodopsin as well as homologous desensitization of beta-adrenergic receptors involves receptor phosphorylation that is mediated by the highly specific protein kinases rhodopsin kinase (RK) and beta-adrenergic receptor kinase (beta ARK), respectively. We report here the cloning of a complementary DNA for RK. The deduced amino acid sequence shows a high degree of homology to beta ARK. In a phylogenetic tree constructed by comparing the catalytic domains of several protein kinases, RK and beta ARK are located on a branch close to, but separate from the cyclic nucleotide-dependent protein kinase and protein kinase C subfamilies. From the common structural features we conclude that both RK and beta ARK are members of a newly delineated gene family of guanine nucleotide-binding protein (G protein)-coupled receptor kinases that may function in diverse pathways to regulate the function of such receptors.

Indexed as

Cyclic AMP-Dependent Protein KinasesEye ProteinsAmino Acid SequenceAnimalsBase Sequencebeta-Adrenergic Receptor KinasesBlotting, NorthernCattleCloning, MolecularGene ExpressionG-Protein-Coupled Receptor Kinase 1Molecular Sequence DataOligonucleotidesPhylogenyPolymerase Chain ReactionProtein Kinasesbeta-Adrenergic Receptor KinasesCyclic AMP-Dependent Protein KinasesEye ProteinsG-Protein-Coupled Receptor Kinase 1OligonucleotidesProtein KinasesReceptors, Adrenergic, betaRhodopsinRNA, Messenger

Identifiers

PMID1656454
PMCPMC52580
OpenAlexW2071132058

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.