Evidence map›Paper›PMID 19056296›Full record

ReviewTrends in endocrinology and metabolism: TEM2009

Rationally designed peptide regulators of protein kinase C.

Eric N Churchill, Nir Qvit, Daria Mochly-Rosen

Open access · greenAbstract readReview
In one paragraph

Review in Trends in endocrinology and metabolism: TEM, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

53 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Current Challenges and Future Directions in Peptidomics.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. PKC and PKN in heart disease.Journal of molecular and cellular cardiology · 2019
    Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Protein kinase C mechanisms that contribute to cardiac remodelling.Clinical science (London, England : 1979) · 2016
    Review
  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

3 authors at 1 institution in 1 country.

Eric N ChurchillDepartment of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Nir Qvit
Daria Mochly-Rosen
Stanford University · US

Funding

Protein Kinase C Isozymes in Ischemic HeartR01HL052141 · NHLBI · STANFORD UNIVERSITY · PI MOCHLY-ROSEN, DARIA · 1996 to 2021
$8.5M
MECHANISMS OF ETHANOL-INDUCED CARDIAC PROTECTIONR01AA011147 · NIAAA · STANFORD UNIVERSITY · PI DARIA MOCHLY-ROSEN · 1996 to 2026
$8.2M
Mechanisms of Ethanol-Induced Cardiac ProtectionR37AA011147 · NIAAA · STANFORD UNIVERSITY · PI MOCHLY-ROSEN, DARIA · 2009 to 2018
$5.3M
MAP Kinase and AKT Signaling in Congestive Heart FailureR01HL076670 · NHLBI · WASHINGTON UNIVERSITY · PI MUSLIN, ANTHONY JUSTIN · 2005 to 2009
$1.7M
NHLBI NIH HHS HL52141NHLBI NIH HHS HL76670NHLBI NIH HHS R01 HL052141NHLBI NIH HHS R01 HL076670NIAAA NIH HHS AA11147NIAAA NIH HHS R01 AA011147NIAAA NIH HHS R37 AA011147
6 · The paper itself

Abstract

Protein-protein interactions sequester enzymes close to their substrates. Protein kinase C (PKC) is one example of a ubiquitous signaling molecule with effects that are dependent upon localization. Short peptides derived from interaction sites between each PKC isozyme and its receptor for activated C kinase act as highly specific inhibitors and have become available as selective drugs in basic research and animal models of human diseases, such as myocardial infarction and hyperglycemia. Whereas the earlier inhibitory peptides are highly specific, we believe that peptides targeting additional interactions between PKC and selective substrates will generate even more selective tools that regulate different functions of individual isozymes. Here, we discuss the methodologies and applications for identifying selective regulators of PKC.

Indexed as

Drug DesignAmino Acid SequenceAnimalsEnzyme ActivationEnzyme ActivatorsEnzyme InhibitorsHumansModels, BiologicalModels, MolecularMolecular Sequence DataPeptide FragmentsProtein BindingProtein Kinase CEnzyme ActivatorsEnzyme InhibitorsPeptide FragmentsProtein Kinase C

Identifiers

PMID19056296
PMCPMC2714361
OpenAlexW2016184567

What OpenQuestion 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 OpenQuestion graph.