Evidence map›Paper›PMID 19008230›Full record

ArticleThe Journal of biological chemistry2009

Stimulation of mammalian G-protein-responsive adenylyl cyclases by carbon dioxide.

Philip D Townsend, Phillip M Holliday, Stepan Fenyk, Kenneth C Hess, Michael A Gray, David R W Hodgson, Martin J Cann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 18% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 49 citations in OpenAlex.

  1. Pooled it
  2. Carbon dioxide is a triple vasodilator.Cardiovascular research · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Stomatal COScience advances · 2022
    Article
  9. Structure ofeLife · 2022
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Carbon dioxide-sensing in organisms and its implications for human disease.Cellular and molecular life sciences : CMLS · 2014
    Review
  19. Revisiting cAMP signaling in the carotid body.Frontiers in physiology · 2014
    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

7 authors at 4 institutions in 3 countries.

Philip D TownsendSchool of Biological and Biomedical Sciences, Durham University, Durham, UK.
Phillip M Holliday
Stepan Fenyk
Kenneth C Hess
Michael A Gray
David R W Hodgson
Martin J Cann
Durham University · GBDepartment of Biological Sciences · RUCornell University · USNewcastle University · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust
6 · The paper itself

Abstract

Carbon dioxide is fundamental to the physiology of all organisms. There is considerable interest in the precise molecular mechanisms that organisms use to directly sense CO(2). Here we demonstrate that a mammalian recombinant G-protein-activated adenylyl cyclase and the related Rv1625c adenylyl cyclase of Mycobacterium tuberculosis are specifically stimulated by CO(2). Stimulation occurred at physiological concentrations of CO(2) through increased k(cat). CO(2) increased the affinity of enzyme for metal co-factor, but contact with metal was not necessary as CO(2) interacted directly with apoenzyme. CO(2) stimulated the activity of both G-protein-regulated adenylyl cyclases and Rv1625c in vivo. Activation of G-protein regulated adenylyl cyclases by CO(2) gave a corresponding increase in cAMP-response element-binding protein (CREB) phosphorylation. Comparison of the responses of the G-protein regulated adenylyl cyclases and the molecularly, and biochemically distinct mammalian soluble adenylyl cyclase revealed that whereas G-protein-regulated enzymes are responsive to CO(2), the soluble adenylyl cyclase is responsive to both CO(2) and bicarbonate ion. We have, thus, identified a signaling enzyme by which eukaryotes can directly detect and respond to fluctuating CO(2).

Indexed as

Adenylyl CyclasesAmino Acid SequenceAnimalsCarbon DioxideCell LineGene Expression RegulationGTP-Binding ProteinsHumansIsoenzymesKineticsMolecular Sequence DataRatsSequence AlignmentAdenylyl CyclasesCarbon DioxideGTP-Binding ProteinsIsoenzymes

Identifiers

PMID19008230
PMCPMC2613629
OpenAlexW2142094277

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.