Evidence map›Paper›PMID 15126679›Full record

ReviewMolecular neurobiology2004

Invertebrates yield a plethora of atypical guanylyl cyclases.

David B Morton

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

33 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. A FRET-based cGMP biosensor inmicroPublication biology · 2023
    Article
  3. Article
  4. Article
  5. Oxygen sensing in crustaceans: functions and mechanisms.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2021
    Review
  6. Compartmentalized cGMP Responses of Olfactory Sensory Neurons inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Receptor Guanylyl Cyclases in Sensory Processing.Frontiers in endocrinology · 2016
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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.

David B MortonDepartment of Integrative Biosciences, Oregon Health and Science University, Portland, OR, USA. mortonda@ohsu.edu
Oregon Health & Science University · US

Funding

REGULATION AND FUNCTION OF CYCLIC GMP IN THE CNSR01NS029740 · NINDS · UNIVERSITY OF ARIZONA · PI MORTON, DAVID B · 1996 to 2011
$2.8M
STEROID REGULATION OF PEPTIDE SENSITIVITY IN THE CNSR29NS029740 · NINDS · UNIVERSITY OF ARIZONA · PI MORTON, DAVID B · 1991 to 1995
–
NINDS NIH HHS NS29740
6 · The paper itself

Abstract

Invertebrate model systems have a long history of generating new insights into neuronal signaling systems. This review focuses on cyclic GMP signaling and describes recent advances in understanding the properties and functions of guanylyl cyclases in invertebrates. The sequencing of three invertebrate genomes has provided a complete catalog of the guanylyl cyclases in C. elegans, Drosophila, and the mosquito Anopheles gambiae. Using this data and that from cloned guanylyl cyclases in Manduca sexta, C. elegans, and Drosophila, plus predictions and models from vertebrate guanylyl cyclases, evidence is presented that there is a much broader array of properties for these enzymes than previously realized. In addition to the classic homodimeric receptor guanylyl cyclases, C. elegans has at least two receptor guanylyl cyclases that are predicted to require heterodimer formation for activity. Soluble guanylyl cyclases are generally recognized as being obligate heterodimers that are activated by nitric oxide (NO). Some of the soluble guanylyl cyclases in C. elegans may heterodimeric, but all appear to be insensitive to NO. The beta2 soluble guanylyl cyclase subunit in mammals and similar ones in Manduca and Drosophila are active in the absence of additional subunits and there is evidence that Drosophila and Anopheles also express an additional subunit that enhances this activity.

Indexed as

Amino Acid SequenceAnimalsCaenorhabditis elegansDrosophilaGuanylate CyclaseManducaMolecular Sequence DataGuanylate Cyclase

Identifiers

PMID15126679
OpenAlexW2089624873

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.