Evidence map›Paper›PMID 10947947›Full record

ReviewThe Biochemical journal2000

Sac phosphatase domain proteins.

W E Hughes, F T Cooke, P J Parker

Open access · bronzeAbstract readReview
In one paragraph

Review in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

62 citing papers in PubMed, 135 citations in OpenAlex.

  1. Roles in physiology and disease of the inositol phosphatase synaptojanin 1.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2026
    Review
  2. Article
  3. Sur7 mediates a novel pathway for PIMolecular biology of the cell · 2024
    Article
  4. Review
  5. Review
  6. Genomic identification of cottonFrontiers in plant science · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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  19. Article
  20. SAC phosphoinositide phosphatases at the tonoplast mediate vacuolar function in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article

2 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

3 authors at 1 institution in 1 country.

W E HughesProtein Phosphorylation Laboratory, Imperial Cancer Research Fund, 44, Lincoln's Inn Fields, London WC2A 3PX, UK.
F T Cooke
P J Parker
The Honourable Society of Lincoln's Inn · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Advances in our understanding of the roles of phosphatidylinositol phosphates in controlling cellular functions such as endocytosis, exocytosis and the actin cytoskeleton have included new insights into the phosphatases that are responsible for the interconversion of these lipids. One of these is an entirely novel class of phosphatase domain found in a number of well characterized proteins. Proteins containing this Sac phosphatase domain include the yeast Saccharomyces cerevisiae proteins Sac1p and Fig4p. The Sac phosphatase domain is also found within the mammalian phosphoinositide 5-phosphatase synaptojanin and the yeast synaptojanin homologues Inp51p, Inp52p and Inp53p. These proteins therefore contain both Sac phosphatase and 5-phosphatase domains. This review describes the Sac phosphatase domain-containing proteins and their actions, with particular reference to the genetic and biochemical insights provided by study of the yeast Saccharomyces cerevisiae.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceFlavoproteinsFungal ProteinsMembrane ProteinsModels, BiologicalModels, ChemicalMolecular Sequence DataNerve Tissue ProteinsPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesProtein Structure, TertiarySaccharomyces cerevisiaeSequence Homology, Amino AcidFIG4 protein, S cerevisiaeFlavoproteinsFungal ProteinsMembrane ProteinsNerve Tissue ProteinsPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesSAC1 protein, S cerevisiaeSaccharomyces cerevisiae Proteinssynaptojanin

Identifiers

PMID10947947
PMCPMC1221260
OpenAlexW2068831015

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.