Evidence map›Paper›PMID 31936296›Full record

ReviewInternational journal of molecular sciences2020

Protein Phosphatases in G1 Regulation.

Ruth Martín, Vilte Stonyte, Sandra Lopez-Aviles

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. 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

3 authors at 1 institution in 1 country.

Ruth MartínNorwegian Centre for Molecular Medicine (NCMM), University of Oslo. Gaustalleen 21, 0349 Oslo, Norway.
Vilte StonyteNorwegian Centre for Molecular Medicine (NCMM), University of Oslo. Gaustalleen 21, 0349 Oslo, Norway.
Sandra Lopez-AvilesNorwegian Centre for Molecular Medicine (NCMM), University of Oslo. Gaustalleen 21, 0349 Oslo, Norway.
University of Oslo · NO

Funding

Norges Forskningsråd 251321
6 · The paper itself

Abstract

Eukaryotic cells make the decision to proliferate, to differentiate or to cease dividing during G1, before passage through the restriction point or Start. Keeping cyclin-dependent kinase (CDK) activity low during this period restricts commitment to a new cell cycle and is essential to provide the adequate timeframe for the sensing of environmental signals. Here, we review the role of protein phosphatases in the modulation of CDK activity and as the counteracting force for CDK-dependent substrate phosphorylation, in budding and fission yeast. Moreover, we discuss recent findings that place protein phosphatases in the interface between nutritional signalling pathways and the cell cycle machinery.

Indexed as

Cell ProliferationCyclin-Dependent KinasesG1 PhasePhosphoprotein PhosphatasesPhosphorylationSaccharomyces cerevisiaeSignal TransductionCyclin-Dependent KinasesPhosphoprotein PhosphatasesCDK-counteracting phosphatasesG1 controlGreatwall-ENSAStart

Identifiers

PMID31936296
PMCPMC7013402
OpenAlexW3000699800

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.