Evidence map›Paper›PMID 25732852›Full record

ReviewBiochimica et biophysica acta2015

Polyphosphoinositide binding domains: Key to inositol lipid biology.

Gerald R V Hammond, Tamas Balla

Erratum issuedOpen access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 143 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
143citing papers in PubMed, 2 pooled it
13.7field-weighted citation impact, top 1% 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

143 citing papers in PubMed, 2 syntheses or guidelines pooled it, 254 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
  4. Distinct impact of PI(4)P flux on PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Phosphatidylinositol 4-phosphate; A minor lipid with multiple personalities.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  11. Review
  12. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Gerald R V HammondDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA. ghammond@pitt.edu
Tamas BallaSection on Molecular Signal Transduction, Eunice Shriver Kennedy National Institute for Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA. Electronic address: ballat@mail.nih.gov.
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USUniversity of Pittsburgh · US

Funding

Phosphoinositide-calcium Signaling In Cell RegulationZIAHD000196 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BALLA, TAMAS · 2009 to 2025
$26.3M
Intramural NIH HHS ZIA HD000196
6 · The paper itself

Abstract

Polyphosphoinositides (PPIn) are an important family of phospholipids located on the cytoplasmic leaflet of eukaryotic cell membranes. Collectively, they are critical for the regulation of many aspects of membrane homeostasis and signaling, with notable relevance to human physiology and disease. This regulation is achieved through the selective interaction of these lipids with hundreds of cellular proteins, and thus the capability to study these localized interactions is crucial to understanding their functions. In this review, we discuss current knowledge of the principle types of PPIn-protein interactions, focusing on specific lipid-binding domains. We then discuss how these domains have been re-tasked by biologists as molecular probes for these lipids in living cells. Finally, we describe how the knowledge gained with these probes, when combined with other techniques, has led to the current view of the lipids' localization and function in eukaryotes, focusing mainly on animal cells. This article is part of a Special Issue entitled Phosphoinositides.

Indexed as

Biosensing TechniquesAdaptor Proteins, Signal TransducingAnimalsCell MembraneGreen Fluorescent ProteinsGuanine Nucleotide Exchange FactorsHumansMolecular ImagingMolecular ProbesPhosphatidylinositolsProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsSignal TransductionTacrolimus Binding ProteinsType C PhospholipasesAdaptor Proteins, Signal TransducingFGD5 protein, humanGreen Fluorescent ProteinsGuanine Nucleotide Exchange FactorsMolecular ProbesPhosphatidylinositolsPLEKHA3 protein, humanRecombinant Fusion ProteinsTacrolimus Binding ProteinsType C PhospholipasesFluorescence imagingMembranePH-domainPhosphoinositidePhospholipase CPX-domain

Identifiers

PMID25732852
PMCPMC4380703
OpenAlexW2044409787

What OpenQuestion holds

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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.