Evidence map›Paper›PMID 28328744›Full record

ReviewJournal of cardiovascular pharmacology2017

Noncanonical Roles of G Protein-coupled Receptor Kinases in Cardiovascular Signaling.

Sarah M Schumacher, Walter J Koch

Open access · greenAbstract readReview
In one paragraph

Review in Journal of cardiovascular pharmacology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Location-specific and Kinase-Independent GRK5 Function in Heart.JACC. Basic to translational science · 2022
    Article
  7. Article
  8. Targeting GRK5 for Treating Chronic Degenerative Diseases.International journal of molecular sciences · 2021
    Review
  9. Review
  10. Differential Regulation of GPCRs-Are GRK Expression Levels the Key?Frontiers in cell and developmental biology · 2021
    Review
  11. The Roles of GRKs in Hemostasis and Thrombosis.International journal of molecular sciences · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
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 1 institution in 1 country.

Sarah M Schumacher*Department of Pharmacology, Center for Translational Medicine, Lewis Katz School of Medicine at Temple University, Philadelphia, PA; and †Department of Pharmacology, Lewis Katz School of Medicine at Temple University, Philadelphia, PA.
Walter J Koch
Temple University · US

Funding

Regulation of Beta-Adrenergic Receptor Signaling by S-NitrosylationP01HL075443 · NHLBI · DUKE UNIVERSITY · PI ROCKMAN, HOWARD A · 2004 to 2019
$26.1M
Targeted Cancer Therapeutics and Heart Failure: Mechanisms and Post-injury RepairP01HL091799 · NHLBI · THOMAS JEFFERSON UNIVERSITY · PI KOCH, WALTER J. · 2008 to 2018
$23.1M
PKC alpha as a translational target in Heart FailureP01HL108806 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI RABINOWITZ, JOSEPH E · 2012 to 2016
$11.3M
Structure, function, and inhibition of G protein-coupled receptor kinasesR01HL071818 · NHLBI · UNIVERSITY OF TEXAS AUSTIN · PI TESMER, JOHN · 2004 to 2023
$7.1M
Targeting GRK2 in the HeartR01HL061690 · NHLBI · THOMAS JEFFERSON UNIVERSITY · PI KOCH, WALTER J. · 1998 to 2022
$4.2M
Targeting GRK2 (BARK1) in Heart FailureR37HL061690 · NHLBI · THOMAS JEFFERSON UNIVERSITY · PI KOCH, WALTER J. · 2009 to 2018
$3.9M
GRK and b-Arrestin Signaling in Cardiac RegenerationR01HL085503 · NHLBI · THOMAS JEFFERSON UNIVERSITY · PI KOCH, WALTER J. · 2007 to 2015
$3.0M
Unique Domain Features of GRK2 and Roles in Cardiovascular DiseaseK99HL132882 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI SCHUMACHER, SARAH MARIE · 2016 to 2017
$229k
NHLBI NIH HHS K99 HL132882NHLBI NIH HHS P01 HL075443NHLBI NIH HHS P01 HL091799NHLBI NIH HHS P01 HL108806NHLBI NIH HHS R01 HL061690NHLBI NIH HHS R01 HL071818NHLBI NIH HHS R01 HL085503NHLBI NIH HHS R37 HL061690
6 · The paper itself

Abstract

G protein-coupled receptor kinases (GRKs) are classically known for their role in regulating the activity of the largest known class of membrane receptors, which influence diverse biological processes in every cell type in the human body. As researchers have tried to uncover how this family of kinases, containing only 7 members, achieves selective and coordinated control of receptors, they have uncovered a growing number of noncanonical activities for these kinases. These activities include phosphorylation of nonreceptor targets and kinase-independent molecular interactions. In particular, GRK2, GRK3, and GRK5 are the predominant members expressed in the heart. Their canonical and noncanonical actions within cardiac and other tissues have significant implications for cardiovascular function in healthy animals and for the development and progression of disease. This review summarizes what is currently known regarding the activity of these kinases, and particularly the role of GRK2 and GRK5 in the molecular alterations that occur during heart failure. This review further highlights areas of GRK regulation that remain poorly understood and how they may represent novel targets for therapeutic development.

Indexed as

AnimalsCardiovascular DiseasesG-Protein-Coupled Receptor Kinase 2G-Protein-Coupled Receptor Kinase 5G-Protein-Coupled Receptor KinasesHumansSignal TransductionG-Protein-Coupled Receptor Kinase 2G-Protein-Coupled Receptor Kinase 5G-Protein-Coupled Receptor KinasesGRK2 protein, humanGRK5 protein, human

Identifiers

PMID28328744
PMCPMC5591054
OpenAlexW2599997917

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.