Evidence map›Paper›PMID 17661083›Full record

ReviewJournal of cancer research and clinical oncology2007

Protein kinase C family: on the crossroads of cell signaling in skin and tumor epithelium.

D Breitkreutz, L Braiman-Wiksman, N Daum, M F Denning, T Tennenbaum

Open access · greenAbstract readReview
In one paragraph

Review in Journal of cancer research and clinical oncology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.1field-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

63 citing papers in PubMed, 143 citations in OpenAlex.

  1. The PKC inhibitor AEB071 may be a therapeutic option for psoriasis.The Journal of clinical investigation · 2008
    Trial
  2. Cannabinoid tolerance relies on CBProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
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  9. Alcohol in Psoriasis-From Bench to Bedside.International journal of molecular sciences · 2021
    Review
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  11. Review
  12. Review
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3 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 3 countries.

D BreitkreutzDivision of Differentiation and Carcinogenesis (A080/A110), German Cancer Research Center (DKFZ), POB 101949, Im Neuenheimer Feld 280, 69009, Heidelberg, Germany. d.breitkreutz@dkfz.de
L Braiman-Wiksman
N Daum
M F Denning
T Tennenbaum
German Cancer Research Center · DEBar-Ilan University · ILLoyola University Chicago · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein kinase C (PKC) family represents a large group of phospholipid dependent enzymes catalyzing the covalent transfer of phosphate from ATP to serine and threonine residues of proteins. Phosphorylation of the substrate proteins induces a conformational change resulting in modification of their functional properties. The PKC family consists of at least ten members, divided into three subgroups: classical PKCs (alpha, betaI, betaII, gamma), novel PKCs (delta, epsilon, eta, theta), and atypical PKCs (zeta, iota/lambda). The specific cofactor requirements, tissue distribution, and cellular compartmentalization suggest differential functions and fine tuning of specific signaling cascades for each isoform. Thus, specific stimuli can lead to differential responses via isoform specific PKC signaling regulated by their expression, localization, and phosphorylation status in particular biological settings. PKC isoforms are activated by a variety of extracellular signals and, in turn, modify the activities of cellular proteins including receptors, enzymes, cytoskeletal proteins, and transcription factors. Accordingly, the PKC family plays a central role in cellular signal processing. Accumulating data suggest that various PKC isoforms participate in the regulation of cell proliferation, differentiation, survival and death. These findings have enabled identification of abnormalities in PKC isoform function, as they occur in several cancers. Specifically, the initiation of squamous cell carcinoma formation and progression to the malignant phenotype was found to be associated with distinct changes in PKC expression, activation, distribution, and phosphorylation. These studies were recently further extended to transgenic and knockout animals, which allowed a more direct analysis of individual PKC functions. Accordingly, this review is focused on the involvement of PKC in physiology and pathology of the skin.

Indexed as

AnimalsEpitheliumHumansIsoenzymesProtein Kinase CSignal TransductionSkinSkin NeoplasmsIsoenzymesProtein Kinase C

Identifiers

PMID17661083
PMCPMC12160839
OpenAlexW1988649727

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.