Evidence map›Paper›PMID 38491249›Full record

ReviewThe protein journal2024

An update on Glycerophosphodiester Phosphodiesterases; From Bacteria to Human.

Seyyedeh Mina Hejazian, Saeed Pirmoradi, Sepideh Zununi Vahed, Ripon Kumar Roy, Seyed Mahdi Hosseiniyan Khatibi

Abstract readReview
PubMed Publisher
In one paragraph

Review in The protein journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
10.2field-weighted citation impact, top 2% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. UrinaryJournal of cellular immunology · 2025
    Article
  8. Review
  9. Article
  10. 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

5 authors at 3 institutions in 2 countries.

Seyyedeh Mina HejazianKidney Research Center, Tabriz University of Medical Sciences, Tabriz, Iran.
Saeed PirmoradiClinical Research Development Unit of Tabriz Valiasr Hospital, Tabriz University of Medical Sciences, Tabriz, Iran.
Sepideh Zununi VahedKidney Research Center, Tabriz University of Medical Sciences, Tabriz, Iran.
Ripon Kumar RoyBangladesh Rice Research Institute, Dhaka, Bangladesh.
Seyed Mahdi Hosseiniyan KhatibiKidney Research Center, Tabriz University of Medical Sciences, Tabriz, Iran. s.mahdi.h.khatibi@gmail.com.
Tabriz University of Medical Sciences · IRBangladesh Rice Research Institute · BDK.N.Toosi University of Technology · IR

Funding

Tabriz University of Medical Sciences 74063
6 · The paper itself

Abstract

The hydrolysis of deacylated glycerophospholipids into sn-glycerol 3-phosphate and alcohol is facilitated by evolutionarily conserved proteins known as glycerophosphodiester phosphodiesterases (GDPDs). These proteins are crucial for the pathogenicity of bacteria and for bioremediation processes aimed at degrading organophosphorus esters that pose a hazard to both humans and the environment. Additionally, GDPDs are enzymes that respond to multiple nutrients and could potentially serve as candidate genes for addressing deficiencies in zinc, iron, potassium, and especially phosphate in important plants like rice. In mammals, glycerophosphodiesterases (GDEs) play a role in regulating osmolytes, facilitating the biosynthesis of anandamine, contributing to the development of skeletal muscle, promoting the differentiation of neurons and osteoblasts, and influencing pathological states. Due to their capacity to enhance a plant's ability to tolerate various nutrient deficiencies and their potential as pharmaceutical targets in humans, GDPDs have received increased attention in recent times. This review provides an overview of the functions of GDPD families as vital and resilient enzymes that regulate various pathways in bacteria, plants, and humans.

Indexed as

BacteriaPhosphoric Diester HydrolasesAnimalsBacterial ProteinsHumansBacterial Proteinsglycerophosphodiester phosphodiesterasePhosphoric Diester HydrolasesGlycerophosphodiesterase (GDE)Glycerophosphodiester phosphodiesterase (GDPD)Phosphodiesterase

Identifiers

PMID38491249
OpenAlexW4394763181

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.