Evidence map›Paper›PMID 27713345›Full record

ReviewPharmaceuticals (Basel, Switzerland)2010

Protein Kinases as Drug Development Targets for Heart Disease Therapy.

Naranjan S Dhalla, Alison L Müller

Open access · goldAbstract readReview
In one paragraph

Review in Pharmaceuticals (Basel, Switzerland), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.2field-weighted citation impact, top 40% 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

14 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Status of βReviews in cardiovascular medicine · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Synemin Redefined: Multiple Binding Partners Results in Multifunctionality.Frontiers in cell and developmental biology · 2020
    Review
  7. The Akt pathway in oncology therapy and beyond (Review).International journal of oncology · 2018
    Review
  8. Review
  9. Cyclic Nucleotide-Directed Protein Kinases in Cardiovascular Inflammation and Growth.Journal of cardiovascular development and disease · 2018
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. 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 2 institutions in 1 country.

Naranjan S DhallaInstitute of Cardiovascular Sciences, St. Boniface Hospital Research, and Department of Physiology, Faculty of Medicine, University of Manitoba, Winnipeg, MB R2H 2A6, Canada. nsdhalla@sbrc.ca.
Alison L MüllerInstitute of Cardiovascular Sciences, St. Boniface Hospital Research, and Department of Physiology, Faculty of Medicine, University of Manitoba, Winnipeg, MB R2H 2A6, Canada. amuller@sbrc.ca.
St. Boniface Hospital · CAUniversity of Manitoba · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinases are intimately integrated in different signal transduction pathways for the regulation of cardiac function in both health and disease. Protein kinase A (PKA), Ca²⁺-calmodulin-dependent protein kinase (CaMK), protein kinase C (PKC), phosphoinositide 3-kinase (PI3K) and mitogen-activated protein kinase (MAPK) are not only involved in the control of subcellular activities for maintaining cardiac function, but also participate in the development of cardiac dysfunction in cardiac hypertrophy, diabetic cardiomyopathy, myocardial infarction, and heart failure. Although all these kinases serve as signal transducing proteins by phosphorylating different sites in cardiomyocytes, some of their effects are cardioprotective whereas others are detrimental. Such opposing effects of each signal transduction pathway seem to depend upon the duration and intensity of stimulus as well as the type of kinase isoform for each kinase. In view of the fact that most of these kinases are activated in heart disease and their inhibition has been shown to improve cardiac function, it is suggested that these kinases form excellent targets for drug development for therapy of heart disease.

Indexed as

Ca2+ calmodulin protein kinasemitogen-activated protein kinasesphosphoinositide 3-kinaseprotein kinase Aprotein kinase C

Identifiers

PMID27713345
PMCPMC4036665
OpenAlexW2032690812

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.