Evidence map›Paper›PMID 25855792›Full record

ReviewThe Journal of biological chemistry2015

Signaling, Regulation, and Specificity of the Type II p21-activated Kinases.

Byung Hak Ha, Elizabeth M Morse, Benjamin E Turk, Titus J Boggon

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2015. 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
3.3field-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, 59 citations in OpenAlex.

  1. An Integrated Proteomics and Genomics Approach to Identify Essential Protein Kinases During Human Trophoblast Development.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Regulation and signaling of the LIM domain kinases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  10. Review
  11. Article
  12. Article
  13. Rho family GTPase signaling through type II p21-activated kinases.Cellular and molecular life sciences : CMLS · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  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

4 authors at 1 institution in 1 country.

Byung Hak HaFrom the Departments of Pharmacology and.
Elizabeth M MorseCell Biology, Yale University School of Medicine, New Haven, Connecticut 06520.
Benjamin E TurkFrom the Departments of Pharmacology and.
Titus J BoggonFrom the Departments of Pharmacology and titus.boggon@yale.edu.
Yale University · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
Structure-directed investigations into the regulation of Ste20 kinasesR01GM102262 · NIGMS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON · 2012 to 2025
$4.2M
NIGMS NIH HHS R01 GM102262NIGMS NIH HHS R01GM102262NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

The p21-activated kinases (PAKs) are a family of six serine/threonine kinases that act as key effectors of RHO family GTPases in mammalian cells. PAKs are subdivided into two groups: type I PAKs (PAK1, PAK2, and PAK3) and type II PAKs (PAK4, PAK5, and PAK6). Although these groups are involved in common signaling pathways, recent work indicates that the two groups have distinct modes of regulation and have both unique and common substrates. Here, we review recent insights into the molecular level details that govern regulation of type II PAK signaling. We also consider mechanisms by which signal transduction is regulated at the level of substrate specificity. Finally, we discuss the implications of these studies for clinical targeting of these kinases.

Indexed as

Gene Expression Regulation, EnzymologicSignal TransductionAnimalsHumansp21-Activated KinasesPhosphorylationSubstrate Specificityp21-Activated KinasesCDC42protein structureRas-related C3 botulinum toxin substrate 1 (Rac1)serine/threonine protein kinasesignal transduction

Identifiers

PMID25855792
PMCPMC4505552
OpenAlexW2088895162

What OpenQuestion holds

Textmetadata
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.