Evidence map›Paper›PMID 29623276›Full record

ReviewFrontiers in cell and developmental biology2018

Coordination of Protein Kinase and Phosphoprotein Phosphatase Activities in Mitosis.

Isha Nasa, Arminja N Kettenbach

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in cell and developmental biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 79 citations in OpenAlex.

  1. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Optimized chemical structure extends silencing duration of therapeutic siRNAs in dividing cancer and immune cells.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Targeting PRL phosphatases in hematological malignancies.Expert opinion on therapeutic targets · 2024
    Review
  13. Article
  14. Review
  15. Article
  16. Inducible degradation-coupled phosphoproteomics identifies PP2AFrontiers in cell and developmental biology · 2024
    Article
  17. Article
  18. Article
  19. Review
  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 2 institutions in 1 country.

Isha NasaDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, United States.
Arminja N KettenbachDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, United States.
Cotton (United States) · USDartmouth College · US

Funding

Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MADDEN, DEAN R · 2016 to 2025
$25.9M
Phosphorylation Signaling by Phosphoprotein PhosphatasesR35GM119455 · NIGMS · DARTMOUTH COLLEGE · PI Arminja Nadine Kettenbach · 2016 to 2026
$5.1M
NIGMS NIH HHS P20 GM113132NIGMS NIH HHS R35 GM119455
6 · The paper itself

Abstract

Dynamic changes in protein phosphorylation govern the transitions between different phases of the cell division cycle. A "tug of war" between highly conserved protein kinases and the family of phosphoprotein phosphatases (PPP) establishes the phosphorylation state of proteins, which controls their function. More than three-quarters of all proteins are phosphorylated at one or more sites in human cells, with the highest occupancy of phosphorylation sites seen in mitosis. Spatial and temporal regulation of opposing kinase and PPP activities is crucial for accurate execution of the mitotic program. The role of mitotic kinases has been the focus of many studies, while the contribution of PPPs was for a long time underappreciated and is just emerging. Misconceptions regarding the specificity and activity of protein phosphatases led to the belief that protein kinases are the primary determinants of mitotic regulation, leaving PPPs out of the limelight. Recent studies have shown that protein phosphatases are specific and selective enzymes, and that their activity is tightly regulated. In this review, we discuss the emerging roles of PPPs in mitosis and their regulation of and by mitotic kinases, as well as mechanisms that determine PPP substrate recognition and specificity.

Indexed as

kinases and phosphatasemass spectrometrymitosisphosphatasesprotoemics

Identifiers

PMID29623276
PMCPMC5874294
OpenAlexW2790171528

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.