Evidence map›Paper›PMID 27761507›Full record

ArticleData in brief2016

Mass spectrometry analysis of PPIP5K1 interactions and data on cell motility of PPIP5K1-deficient cells.

Gayane Machkalyan, Phan Trieu, Darlaine Pétrin, Terence E Hébert, Gregory J Miller

Open access · goldAbstract read
In one paragraph

Article in Data in brief, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 99% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Review
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 2 countries.

Gayane MachkalyanDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada.
Phan TrieuDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada.
Darlaine PétrinDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada.
Terence E HébertDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada.
Gregory J MillerDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada; Department of Chemistry, The Catholic University of America, Washington, DC, USA.
McGill University · CAUniversity of America · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inositol pyrophosphates are cellular signals that are created by the actions of inositol kinases and are degraded by highly active inositol phosphatases. The potent actions of these phosphatases suggest these signals must be created near their sites of action. To identify sites where the inositol kinase, PPIP5K1 acts, we performed affinity purification of PPIP5K1 from HEK293 cells and analyzed these samples using mass spectrometry to identify the proteins pesent (10.1016/j.cellsig.2016.02.002) [1]. We further decreased PPIP5K1 levels in HeLa cells and treated these with PPIP5K1 siRNA. We then monitored the motility of these cells in Scratch assays.

Identifiers

PMID27761507
PMCPMC5063796
OpenAlexW2314534292

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.