Evidence map›Paper›PMID 39273482›Full record

ReviewInternational journal of molecular sciences2024

Moonlighting Crypto-Enzymes and Domains as Ancient and Versatile Signaling Devices.

Ilona Turek, Aloysius Wong, Guido Domingo, Candida Vannini, Marcella Bracale, Helen Irving, Chris Gehring

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Abscisic acid binds to anFrontiers in plant science · 2026
    Article
  2. Review
  3. 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

7 authors.

Ilona TurekAustralian Centre for Disease Preparedness, Commonwealth Scientific and Industrial Research Organisation, East Geelong, VIC 3220, Australia.ORCID 0000-0001-6457-7456
Aloysius WongDepartment of Biology, College of Science, Mathematics and Technology, Wenzhou-Kean University, Wenzhou 325060, China.ORCID 0000-0002-9105-5845
Guido DomingoBiotechnology and Life Science Department, University of Insubria, 21100 Varese, Italy.
Candida VanniniBiotechnology and Life Science Department, University of Insubria, 21100 Varese, Italy.ORCID 0000-0002-5196-6142
Marcella BracaleBiotechnology and Life Science Department, University of Insubria, 21100 Varese, Italy.
Helen IrvingLa Trobe Institute of Molecular Sciences, La Trobe University, Bendigo, VIC 3552, Australia.ORCID 0000-0002-1514-0909
Chris GehringDepartment of Chemistry, Biology and Biotechnology, University of Perugia, 06121 Perugia, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Increasing numbers of reports have revealed novel catalytically active cryptic guanylate cyclases (GCs) and adenylate cyclases (ACs) operating within complex proteins in prokaryotes and eukaryotes. Here we review the structural and functional aspects of some of these cyclases and provide examples that illustrate their roles in the regulation of the intramolecular functions of complex proteins, such as the phytosulfokine receptor (PSKR), and reassess their contribution to signal generation and tuning. Another multidomain protein,

Indexed as

Signal TransductionAdenylyl CyclasesAnimalsArabidopsisArabidopsis ProteinsCatalytic DomainGuanylate CyclaseHumansProtein DomainsAdenylyl CyclasesArabidopsis ProteinsGuanylate Cyclaseabscisic acid (ABA)adenylate cyclasecrypto-domainscrypto-enzymesguanylate cyclaseheme-proteinsH-NOXphosphodiesteraseplant hormonesproteomes

Identifiers

PMID39273482
PMCPMC11394779

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.