Evidence map›Paper›PMID 25264170›Full record

ReviewBiochimica et biophysica acta2015

The structure of phosphoinositide phosphatases: Insights into substrate specificity and catalysis.

FoSheng Hsu, Yuxin Mao

Abstract 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. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

44 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
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  3. Review
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  7. Review
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  9. Article
  10. Review
  11. Article
  12. Article
  13. Host Cell Signatures of the Envelopment Site within Beta-Herpes Virions.International journal of molecular sciences · 2022
    Review
  14. Article
  15. Article
  16. Modification of phosphoinositides by theFrontiers in cellular and infection microbiology · 2022
    Review
  17. Fat of the Gut: Epithelial Phospholipids in Inflammatory Bowel Diseases.International journal of molecular sciences · 2021
    Review
  18. ACS infectious diseases · 2021
    Review
  19. Striking a balance: PIPExploration of neuroprotective therapy · 2021
    Article
  20. Article
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

2 authors at 1 institution in 1 country.

FoSheng HsuWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Yuxin MaoWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA. Electronic address: ym253@cornell.edu.
Cornell University · US

Funding

PREDOCTORAL TRAINING IN CELLULAR AND MOLECULAR BIOLOGYT32GM007273 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BRETSCHER, ANTHONY P. · 1985 to 2019
$11.6M
Structural and Functional Studies of the Sac Family Phosphoinositide PhosphatasesR01GM094347 · NIGMS · CORNELL UNIVERSITY · PI MAO, YUXIN · 2011 to 2015
$1.4M
NIGMS NIH HHS R01 GM094347NIGMS NIH HHS R01-GM094347NIGMS NIH HHS T32 GM007273
6 · The paper itself

Abstract

Phosphoinositides (PIs) are a group of key signaling and structural lipid molecules involved in a myriad of cellular processes. PI phosphatases, together with PI kinases, are responsible for the conversion of PIs between distinctive phosphorylation states. PI phosphatases are a large collection of enzymes that are evolved from at least two disparate ancestors. One group is distantly related to endonucleases, which apply divalent metal ions for phosphoryl transfer. The other group is related to protein tyrosine phosphatases, which contain a highly conserved active site motif Cys-X5-Arg (CX5R). In this review, we focus on structural insights to illustrate current understandings of the molecular mechanisms of each PI phosphatase family, with emphasis on their structural basis for substrate specificity determinants and catalytic mechanisms. This article is part of a Special Issue entitled Phosphoinositides.

Indexed as

BacteriaBacterial ProteinsBiocatalysisCell MembraneCrystallography, X-RayGenetic Diseases, X-LinkedHumansInositol Polyphosphate 5-PhosphatasesIsoenzymesMembrane ProteinsModels, MolecularNephrolithiasisOculocerebrorenal SyndromePhosphatidylinositolsPhosphoric Monoester HydrolasesProtein Tyrosine Phosphatases, Non-ReceptorBacterial ProteinsInositol Polyphosphate 5-PhosphatasesIsoenzymesMembrane ProteinsmyotubularinPhosphatidylinositolsPhosphoric Monoester HydrolasesProtein Tyrosine Phosphatases, Non-ReceptorPTEN PhosphohydrolaseSac1 protein, mammalianLowe syndromeMyotubularinOCRLPTENSac1

Identifiers

PMID25264170
PMCPMC4377127
OpenAlexW2052021870

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.