Evidence map›Paper›PMID 11952096›Full record

ReviewMolecular and cellular biochemistry2002

Natriuretic peptide receptor: structure and signaling.

Kunio S Misono

Abstract readReview
PubMed
In one paragraph

Review in Molecular and cellular biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
40.8field-weighted citation impact, top 1% 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

21 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Reversal of the detrimental effects of social isolation on ischemic cerebral injury and stroke-associated pneumonia by inhibiting small intestinalJournal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2023
    Article
  4. Review
  5. Review
  6. Article
  7. Is Atrial Natriuretic Peptide (ANP) and Natriuretic Peptide Receptor-A (NPR-A) Expression in Human Placenta and Decidua Normal?Medical science monitor : international medical journal of experimental and clinical research · 2019
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Inhibition of inflammatory pain by activating B-type natriuretic peptide signal pathway in nociceptive sensory neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    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

1 author at 1 institution in 1 country.

Kunio S MisonoDepartment of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic Foundation, OH 44195, USA. misonok@ccf.org
Cleveland Clinic · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ANP receptor is a single-transmembrane sequence receptor coupled to guanylate cyclase (GCase). It belongs to a family of GCase-coupled receptors that share a common overall molecular configuration. Collectively, theses GCase-coupled receptors belong to a larger family of single-transmembrane sequence receptors that include growth hormone and cytokine receptors. The signal transduction mechanism of these receptors has not been thoroughly understood. Receptor dimerization (or oligomerization) has been suggested as the mechanism. However, at least for the ANP receptor, dimerization has been seen to occur in the absence of the ligand, suggesting that an additional, as yet unknown effect of hormone binding is responsible for receptor activation. To understand the signaling mechanism, some of the functions and subsites of the ANP receptor critical for signaling have been identified, including the binding stoichiometry, receptor self-association, the juxtamembrane hinge structure containing a signature motif critical for GCase signaling, ANP-binding site residues, chloride-dependence of ANP binding, disulfide linkages, and glycosylation structures. These structures and the functional sites have been identified in the crystal structure of dimerized recombinant extracellular domain of the ANP receptor. The intracellular domain contains a kinase-homologous domain that regulates the activity of the GCase domain responding to ANP binding and also to binding of the allosteric effector ATP. Moreover, this regulatory role of the kinase-homologous domain is modulated by its own phosphorylated state. Although considerable data have been accumulated, the mechanism of ANP receptor signaling has not been well defined. Further studies are necessary to understand how ANP binds to the receptor, what conformational effect is caused by ANP binding, how this effect is transduced across the cell membrane, and how this transmembrane effect leads to stimulation of the GCase catalytic activity.

Indexed as

Signal TransductionAmino Acid SequenceAnimalsAtrial Natriuretic FactorBinding SitesCrystallography, X-RayDimerizationModels, MolecularMolecular Sequence DataProtein BindingProtein ConformationReceptors, Atrial Natriuretic FactorStructure-Activity RelationshipAtrial Natriuretic FactorReceptors, Atrial Natriuretic Factor

Identifiers

PMID11952096
OpenAlexW1557787993

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.