Evidence map›Paper›PMID 24667605›Full record

ArticleBiochemical and biophysical research communications2014

PTK2b function during fertilization of the mouse oocyte.

Jinping Luo, Lynda K McGinnis, Carol Carlton, Hilary E Beggs, William H Kinsey

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.3field-weighted citation impact, top 17% 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

5 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Role of focal adhesion kinase in oocyte-follicle communication.Molecular reproduction and development · 2015
    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

5 authors at 2 institutions in 1 country.

Jinping LuoDepartment of Anatomy & Cell Biology, University of Kansas Medical Center, Kansas City, KS 66160, United States.
Lynda K McGinnisDepartment of Molecular & Integrative Physiology, University of Kansas Medical Center, Kansas City, KS 66160, United States.
Carol CarltonDepartment of Anatomy & Cell Biology, University of Kansas Medical Center, Kansas City, KS 66160, United States.
Hilary E BeggsDepartment of Ophthalmology, University of California, San Francisco, CA, United States.
William H KinseyDepartment of Anatomy & Cell Biology, University of Kansas Medical Center, Kansas City, KS 66160, United States. Electronic address: wkinsey@kumc.edu.
University of Kansas Medical Center · USUniversity of California, San Francisco · US

Funding

PYK2 function during fertilizationR01HD062860 · NICHD · UNIVERSITY OF KANSAS MEDICAL CENTER · PI KINSEY, WILLIAM H. · 2010 to 2020
$2.9M
NICHD NIH HHS HD062860NICHD NIH HHS R01 HD062860
6 · The paper itself

Abstract

Fertilization triggers rapid changes in intracellular free calcium that serve to activate multiple signaling events critical to the initiation of successful development. Among the pathways downstream of the fertilization-induced calcium transient is the calcium-calmodulin dependent protein tyrosine kinase PTK2b or PYK2 kinase. PTK2b plays an important role in fertilization of the zebrafish oocyte and the objective of the present study was to establish whether PTK2b also functions in mammalian fertilization. PTK2b was activated during the first few hours after fertilization of the mouse oocyte during the period when anaphase resumption was underway and prior to the pronuclear stage. Suppression of PTK2b kinase activity in oocytes blocked sperm incorporation and egg activation although sperm-oocyte binding was not affected. Oocytes that failed to incorporate sperm after inhibitor treatment showed no evidence of a calcium transient and no evidence of anaphase resumption suggesting that egg activation did not occur. The results indicate that PTK2b functions during the sperm-egg fusion process or during the physical incorporation of sperm into the egg cytoplasm and is therefore critical for successful development.

Indexed as

AnimalsCalcium SignalingEnzyme ActivationFemaleFertilizationFocal Adhesion Kinase 2MaleMiceMice, Inbred C57BLMice, KnockoutMice, TransgenicOocytesProtein Kinase InhibitorsSperm-Ovum InteractionsZygoteFocal Adhesion Kinase 2Protein Kinase InhibitorsPtk2b protein, mouseEgg activationFertilizationOocytePTK2bPYK2 kinase

Identifiers

PMID24667605
PMCPMC4133292
OpenAlexW2086534389

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.