Evidence map›Paper›PMID 21618529›Full record

ArticleJournal of cellular physiology2011

Voltage sensitive phosphoinositide phosphatases of Xenopus: their tissue distribution and voltage dependence.

William J Ratzan, Alexei V Evsikov, Yasushi Okamura, Laurinda A Jaffe

Open access · greenAbstract read
In one paragraph

Article in Journal of cellular physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.3field-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

28 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Voltage sensors.Molecular pharmacology · 2025
    Review
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  13. Discovery and functional characterization of a neomorphic PTEN mutation.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
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  16. Review
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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 3 institutions in 2 countries.

William J RatzanDepartment of Cell Biology, University of Connecticut Health Center, Farmington, Connecticut 06032, USA.
Alexei V Evsikov
Yasushi Okamura
Laurinda A Jaffe
UConn Health · USJackson Laboratory · USOsaka University · JP

Funding

Function of a voltage-sensitive phosphatase in the regulation of sperm-egg fusionR21HD067017 · NICHD · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI JAFFE, LAURINDA A. · 2010 to 2011
$396k
NICHD NIH HHS R21 HD067017NICHD NIH HHS R21HD067017
6 · The paper itself

Abstract

Voltage-sensitive phosphatases (VSPs) are unique proteins in which membrane potential controls enzyme activity. They are comprised of the voltage sensor domain of an ion channel coupled to a lipid phosphatase specific for phosphoinositides, and for ascidian and zebrafish VSPs, the phosphatase activity has been found to be activated by membrane depolarization. The physiological functions of these proteins are unknown, but their expression in testis and embryos suggests a role in fertilization or development. Here we investigate the expression pattern and voltage dependence of VSPs in two frog species, Xenopus laevis and Xenopus tropicalis, that are well suited for experimental studies of these possible functions. X. laevis has two VSP genes (Xl-VSP1 and Xl-VSP2), whereas X. tropicalis has only one gene (Xt-VSP). The highest expression of these genes was observed in testis, ovary, liver, and kidney. Our results show that while Xl-VSP2 activates only at positive membrane potentials outside of the physiological range, Xl-VSP1 and Xt-VSP phosphatase activity is regulated in the voltage range that regulates sperm-egg fusion at fertilization.

Indexed as

Amino Acid SequenceAnimalsFemaleGene ExpressionKidneyLiverMaleMembrane PotentialsMolecular Sequence DataOvaryPhosphoinositide 5-PhosphatasesPhosphoric Monoester HydrolasesTestisTissue DistributionXenopus laevisXenopus ProteinsPhosphoinositide 5-PhosphatasesPhosphoric Monoester HydrolasesXenopus Proteins

Identifiers

PMID21618529
PMCPMC3181042
OpenAlexW2147429783

What OpenQuestion 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 OpenQuestion graph.