Evidence map›Paper›PMID 29983916›Full record

ReviewF1000Research2018

aPKC: the Kinase that Phosphorylates Cell Polarity.

Yang Hong

Open access · goldAbstract readReview
In one paragraph

Review in F1000Research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.5field-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

45 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. LGL-1 and the RhoGAP protein PAC-1 redundantly polarize thebioRxiv : the preprint server for biology · 2026
    Article
  3. Review
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  7. Review
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  14. A PDZ-kinase allosteric relay mediates Par complex regulator exchange.bioRxiv : the preprint server for biology · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

1 author at 1 institution in 1 country.

Yang HongDepartment of Cell Biology, University of Pittsburgh School of Medicine, S325 BST, 3500 Terrace Street, Pittsburgh, PA 15261, USA.ORCID https://orcid.org/0000-0003-2252-0798
University of Pittsburgh · US

Funding

Plasma Membrane Targeting and Retargeting of Polarity ProteinsR01GM121534 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HONG, YANG · 2017 to 2025
$2.5M
NIGMS NIH HHS R01 GM121534
6 · The paper itself

Abstract

Establishing and maintaining cell polarity are dynamic processes that necessitate complicated but highly regulated protein interactions. Phosphorylation is a powerful mechanism for cells to control the function and subcellular localization of a target protein, and multiple kinases have played critical roles in cell polarity. Among them, atypical protein kinase C (aPKC) is likely the most studied kinase in cell polarity and has the largest number of downstream substrates characterized so far. More than half of the polarity proteins that are essential for regulating cell polarity have been identified as aPKC substrates. This review covers mainly studies of aPKC in regulating anterior-posterior polarity in the worm one-cell embryo and apical-basal polarity in epithelial cells and asymmetrically dividing cells (for example,

Indexed as

anterior-posterior polarityapical-basal polarityaPKCC. elegansDrosophilaepithelial cellsone-cell embryoPar-3Par-6polybasic domain

Identifiers

PMID29983916
PMCPMC6020718
OpenAlexW2810043503

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.