Evidence map›Paper›PMID 24098283›Full record

ReviewFrontiers in pharmacology2013

Unique catalytic activities and scaffolding of p21 activated kinase-1 in cardiovascular signaling.

Yunbo Ke, Ming Lei, Xin Wang, R John Solaro

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in pharmacology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.3field-weighted citation impact, top 37% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Regulation of cardiac gap junctions by protein phosphatases.Journal of molecular and cellular cardiology · 2017
    Review
  6. 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 2 institutions in 2 countries.

Yunbo KeDepartment of Physiology and Biophysics, University of Illinois at Chicago Chicago, IL, USA ; Center for Cardiovascular Research, College of Medicine, University of Illinois at Chicago Chicago, IL, USA.
Ming Lei
Xin Wang
R John Solaro
University of Illinois Chicago · USUniversity of Manchester · GB

Funding

British Heart Foundation PG/11/59/29006
6 · The paper itself

Abstract

P21 activated kinase-1 (Pak1) has diverse functions in mammalian cells. Although a large number of phosphoproteins have been designated as Pak1 substrates from in vitro studies, emerging evidence has indicated that Pak1 may function as a signaling molecule through a unique molecular mechanism - scaffolding. By scaffolding, Pak1 delivers signals through an auto-phosphorylation-induced conformational change without transfer of a phosphate group to its immediate downstream effector(s). Here we review evidence for this regulatory mechanism based on structural and functional studies of Pak1 in different cell types and research models as well as in vitro biochemical assays. We also discuss the implications of Pak1 scaffolding in disease-related signaling processes and the potential in cardiovascular drug development.

Indexed as

auto-phosphorylationcardiovascular diseasescytoskeletal reorganizationFTY720scaffolding

Identifiers

PMID24098283
PMCPMC3784770
OpenAlexW2114194778

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.