Evidence map›Paper›PMID 17580120›Full record

ReviewPharmacological research2007

Insight into intra- and inter-molecular interactions of PKC: design of specific modulators of kinase function.

Viktoria Kheifets, Daria Mochly-Rosen

Open access · greenAbstract readReview
In one paragraph

Review in Pharmacological research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. PKC regulation of ion channels: The involvement of PIPThe Journal of biological chemistry · 2022
    Review
  6. Article
  7. Review
  8. Classical Protein Kinase C: a novel kinase target in breast cancer.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2019
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Engineered Substrate-Specific Delta PKC Antagonists to Enhance Cardiac Therapeutics.Angewandte Chemie (International ed. in English) · 2016
    Article
  14. Regulation of pulmonary endothelial barrier function by kinases.American journal of physiology. Lung cellular and molecular physiology · 2016
    Review
  15. Article
  16. Review
  17. 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

2 authors at 1 institution in 1 country.

Viktoria KheifetsDepartment of Chemical and Systems Biology, Stanford University School of Medicine, CCSR, Rm 3145A, 269 Campus Drive, Stanford, CA 94305-5174, USA.
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
NHLBI NIH HHS R01 HL052141
6 · The paper itself

Abstract

Protein kinase C (PKC) is a family of kinases that are critical in many cellular events. These enzymes are activated by lipid-derived second messengers, are dependent on binding to negatively charged phospholipids and some members also require calcium to attain full activation. The interaction with lipids and calcium activators is mediated by binding to the regulatory domains C1 and C2. In addition, many protein-protein interactions between PKC and other proteins have been described. These include interactions with adaptor proteins, substrates and cytoskeletal elements. Regulation of the interactions between PKC, small molecules and other proteins is essential for signal transduction to occur. Finally, a number of auto-inhibitory intra-molecular protein-protein interactions have also been identified in PKC. This chapter focuses on mapping the sites for many of these inter- and intra-molecular interactions and how this information may be used to generate selective inhibitors and activators of PKC signaling.

Indexed as

AnimalsBinding SitesCalciumEnzyme ActivationPhospholipidsProtein BindingProtein ConformationProtein Interaction MappingProtein Kinase CProtein Structure, TertiarySignal TransductionCalciumPhospholipidsProtein Kinase C

Identifiers

PMID17580120
PMCPMC2834269
OpenAlexW1985415000

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.