Evidence map›Paper›PMID 25821234›Full record

ReviewJournal of lipid research2015

Phosphoinositide-specific phospholipase C in health and disease.

Lucio Cocco, Matilde Y Follo, Lucia Manzoli, Pann-Ghill Suh

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of lipid research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

69 citing papers in PubMed, 172 citations in OpenAlex.

  1. Article
  2. Article
  3. Inhibitors of Phosphatidylinositol-specific Phospholipase C wit hMedicinal chemistry (Shariqah (United Arab Emirates)) · 2026
    Article
  4. Article
  5. Article
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  8. Phospholipases: Paving the Way for a New Life.Reproductive sciences (Thousand Oaks, Calif.) · 2025
    Review
  9. Review
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  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
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  20. Review

9 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 2 countries.

Lucio CoccoCellular Signalling Laboratory, Department of Biomedical and Neuromotor Sciences, University of Bologna, 40126 Bologna, Italy.
Matilde Y FolloCellular Signalling Laboratory, Department of Biomedical and Neuromotor Sciences, University of Bologna, 40126 Bologna, Italy.
Lucia ManzoliCellular Signalling Laboratory, Department of Biomedical and Neuromotor Sciences, University of Bologna, 40126 Bologna, Italy.
Pann-Ghill SuhDepartment of Biological Sciences, Ulsan National Institute of Science and Technology, Ulsan 689-798, Korea.
University of Bologna · ITUlsan National Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phospholipases are widely occurring and can be found in several different organisms, including bacteria, yeast, plants, animals, and viruses. Phospholipase C (PLC) is a class of phospholipases that cleaves phospholipids on the diacylglycerol (DAG) side of the phosphodiester bond producing DAGs and phosphomonoesters. Among PLCs, phosphoinositide-specific PLC (PI-PLC) constitutes an important step in the inositide signaling pathways. The structures of PI-PLC isozymes show conserved domains as well as regulatory specific domains. This is important, as most PI-PLCs share a common mechanism, but each of them has a peculiar role and can have a specific cell distribution that is linked to a specific function. More importantly, the regulation of PLC isozymes is fundamental in health and disease, as there are several PLC-dependent molecular mechanisms that are associated with the activation or inhibition of important physiopathological processes. Moreover, PI-PLC alternative splicing variants can play important roles in complex signaling networks, not only in cancer but also in other diseases. That is why PI-PLC isozymes are now considered as important molecules that are essential for better understanding the molecular mechanisms underlying both physiology and pathogenesis, and are also potential molecular targets useful for the development of innovative therapeutic strategies.

Indexed as

Alternative SplicingAnimalsDiglyceridesEnzyme ActivationHumansPhosphatidylinositolsPhosphoinositide Phospholipase CSignal TransductionDiglyceridesPhosphatidylinositolsPhosphoinositide Phospholipase Cenzyme regulationfunctionsignal transduction

Identifiers

PMID25821234
PMCPMC4583093
OpenAlexW1799359705

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.