Evidence map›Paper›PMID 25452496›Full record

ArticleThe EMBO journal2015

Receptor guanylyl cyclase-G is a novel thermosensory protein activated by cool temperatures.

Ying-Chi Chao, Chih-Cheng Chen, Yuh-Charn Lin, Heinz Breer, Joerg Fleischer, Ruey-Bing Yang

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Ion channels of cold transduction and transmission.The Journal of general physiology · 2024
    Review
  5. Early life oxytocin treatment improves thermo-sensory reactivity and maternal behavior in neonates lacking the autism-associated gene Magel2.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2022
    Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. The Impact of Cold Storage on Adenosine Diphosphate-Mediated Platelet Responsiveness.TH open : companion journal to thrombosis and haemostasis · 2020
    Article
  14. Article
  15. HowGenetics · 2019
    Review
  16. The extraordinary AFD thermosensor of C. elegans.Pflugers Archiv : European journal of physiology · 2018
    Review
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Ying-Chi ChaoMolecular Medicine Program, Taiwan International Graduate Program, Academia Sinica, Taipei, Taiwan Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
Chih-Cheng ChenInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
Yuh-Charn LinInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
Heinz BreerInstitute of Physiology, University of Hohenheim, Stuttgart, Germany.
Joerg FleischerInstitute of Physiology, University of Hohenheim, Stuttgart, Germany joergf@uni-hohenheim.de rbyang@ibms.sinica.edu.tw.
Ruey-Bing YangMolecular Medicine Program, Taiwan International Graduate Program, Academia Sinica, Taipei, Taiwan Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan Institute of Pharmacology, School of Medicine, National Yang-Ming University, Taipei, Taiwan joergf@uni-hohenheim.de rbyang@ibms.sinica.edu.tw.
Institute of Biomedical Sciences, Academia Sinica · TWUniversity of Hohenheim · DENational Taipei University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transmembrane guanylyl cyclases (GCs), with activity regulated by peptide ligands and/or calcium-binding proteins, are essential for various physiological and sensory processes. The mode of activation of the GC subtype GC-G, which is expressed in neurons of the Grueneberg ganglion that respond to cool temperatures, has been elusive. In searching for appropriate stimuli to activate GC-G, we found that its enzymatic activity is directly stimulated by cool temperatures. In this context, it was observed that dimerization/oligomerization of GC-G, a process generally considered as critical for enzymatic activity of GCs, is strongly enhanced by coolness. Moreover, heterologous expression of GC-G in cultured cells rendered these cells responsive to coolness; thus, the protein might be a sensor for cool temperatures. This concept is supported by the observation of substantially reduced coolness-induced response of Grueneberg ganglion neurons and coolness-evoked ultrasonic vocalization in GC-G-deficient mouse pups. GC-G may be a novel thermosensory protein with functional implications for the Grueneberg ganglion, a sensory organ responding to cool temperatures.

Indexed as

Cold TemperatureAnimalsCalcium-Binding ProteinsGuanylate CyclaseHEK293 CellsHumansMembrane ProteinsMiceMice, KnockoutNeuronsProtein MultimerizationCalcium-Binding ProteinsGC-G protein, mouseGuanylate CyclaseMembrane Proteinschemosensorycyclic guanosine monophosphateGrueneberg gangliontransmembrane guanylyl cyclase GC‐Gultrasound vocalization

Identifiers

PMID25452496
PMCPMC4339118
OpenAlexW2139817648

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.