Evidence map›Paper›PMID 20012469›Full record

ReviewMolecular and cellular biochemistry2010

New insight into the functioning of nitric oxide-receptive guanylyl cyclase: physiological and pharmacological implications.

John Garthwaite

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular and cellular biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 101 citations in OpenAlex.

  1. NO rapidly mobilizes cellular heme to trigger assembly of its own receptor.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  2. Review
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  13. Signaling and stress: The redox landscape in NOS2 biology.Free radical biology & medicine · 2015
    Review
  14. Review
  15. Motion of proximal histidine and structural allosteric transition in soluble guanylate cyclase.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  16. Review
  17. Article
  18. Role of angiotensin modulation in primary headaches.Current pain and headache reports · 2014
    Review
  19. Article
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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 2 countries.

John GarthwaiteWolfson Institute for Biomedical Research, University College London, Gower Street, London WC1E 6BT, UK. john.garthwaite@ucl.ac.uk
University College London · GB

Funding

Wellcome Trust 081512/Z/06/Z
6 · The paper itself

Abstract

The cellular counterpart of the "soluble" guanylyl cyclase found in tissue homogenates over 30 years ago is now recognized as the physiological receptor for nitric oxide (NO). The ligand-binding site is a prosthetic haem group that, when occupied by NO, induces a conformational change in the protein that propagates to the catalytic site, triggering conversion of GTP into cGMP. This review focuses on recent research that takes this basic information forward to the beginnings of a quantitative depiction of NO signal transduction, analogous to that achieved for other major transmitters. At its foundation is an explicit enzyme-linked receptor mechanism for NO-activated guanylyl cyclase that replicates all its main properties. In cells, NO signal transduction is subject to additional, activity-dependent modifications, notably through receptor desensitization and changes in the activity of cGMP-hydrolyzing phosphodiesterases. The measurement of these parameters under varying conditions in rat platelets has made it possible to formulate a cellular model of NO-cGMP signaling. The model helps explain cellular responses to NO and their modification by therapeutic agents acting on the guanylyl cyclase or phosphodiesterase limbs of the pathway.

Indexed as

Signal TransductionAnimalsCyclic GMPGuanylate CyclaseRatsReceptors, Cytoplasmic and NuclearSoluble Guanylyl CyclaseCyclic GMPGuanylate CyclaseReceptors, Cytoplasmic and NuclearSoluble Guanylyl Cyclase

Identifiers

PMID20012469
OpenAlexW2006132439

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.