Evidence map›Paper›PMID 10993914›Full record

ArticleThe Journal of experimental medicine2000

The cysteine-rich regions of the regulatory domains of Raf and protein kinase C as retinoid receptors.

B Hoyos, A Imam, R Chua, C Swenson, G X Tong, E Levi, N Noy, U Hämmerling

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 80 citations in OpenAlex.

  1. Review
  2. The mitochondrial PKCδ/retinol signal complex exerts real-time control on energy homeostasis.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  3. Article
  4. Review
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  7. Two protein kinase C isoforms, δ and ε, regulate energy homeostasis in mitochondria by transmitting opposing signals to the pyruvate dehydrogenase complex.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012
    Article
  8. Article
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  11. Control of oxidative phosphorylation by vitamin A illuminates a fundamental role in mitochondrial energy homoeostasis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010
    Article
  12. Vitamin A depletion causes oxidative stress, mitochondrial dysfunction, and PARP-1-dependent energy deprivation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2008
    Article
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  15. Review
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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

8 authors at 2 institutions in 1 country.

B HoyosProgram in Immunology, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
A Imam
R Chua
C Swenson
G X Tong
E Levi
N Noy
U Hämmerling
Memorial Sloan Kettering Cancer Center · USCornell University · US

Funding

LIPID GROWTH FACTOR FOR NORMAL AND MALIGNANT B CELLSR01CA049933 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI HAMMERLING, ULRICH G · 1989 to 2004
$1.4M
VITAMIN A METABOLITES IN SIGNAL TRANSDUCTIONF32CA069718 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SWENSON, CHRISTINA D · 1996 to 1998
–
NCI NIH HHS CA49933NCI NIH HHS CA69718NCI NIH HHS F32 CA069718NCI NIH HHS R01 CA049933
6 · The paper itself

Abstract

Vitamin A and its biologically active derivatives, the retinoids, are recognized as key regulators of vertebrate development, cell growth, and differentiation. Although nuclear receptors have held the attention since their discovery a decade ago, we report here on serine/threonine kinases as a new class of retinoid receptors. The conserved cysteine-rich domain of the NH(2)-terminal regulatory domains of cRaf-1, as well as several select domains of the mammalian protein kinase C (PKC) isoforms alpha, delta, zeta, and mu, the Drosophila and yeast PKCs, were found to bind retinol with nanomolar affinity. The biological significance was revealed in the alternate redox activation pathway of these kinases. Retinol served as a cofactor to augment the activation of both cRaf and PKC alpha by reactive oxygen, whereas the classical receptor-mediated pathway was unaffected by the presence or absence of retinol. We propose that bound retinol, owing to its electron transfer capacity, functions as a tag to enable the efficient and directed redox activation of the cRaf and PKC families of kinases.

Indexed as

Cysteine3T3 CellsAmino Acid SequenceAnimalsBinding SitesDrosophilaHumansIsoenzymesKineticsMiceMolecular Sequence DataPeptide FragmentsProtein Kinase CProto-Oncogene Proteins c-rafReceptors, Retinoic AcidRetinoidsCysteineIsoenzymesPeptide FragmentsProtein Kinase CProto-Oncogene Proteins c-rafReceptors, Retinoic AcidRetinoids

Identifiers

PMID10993914
PMCPMC2193291
OpenAlexW2106368090

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.