Evidence map›Paper›PMID 9177178›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Casein kinase II is a selective target of HIV-1 transcriptional inhibitors.

J W Critchfield, J E Coligan, T M Folks, S T Butera

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
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  10. Crystal structure of human CK2α at 1.06 Å resolution.Journal of synchrotron radiation · 2013
    Article
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  14. Inhibition of Thr-55 phosphorylation restores p53 nuclear localization and sensitizes cancer cells to DNA damage.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
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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

4 authors at 3 institutions in 1 country.

J W CritchfieldRetrovirus Diseases Branch, Division of Acquired Immunodeficiency Syndrome, Sexually Transmitted Diseases, and Tuberculosis Laboratory Research, Centers for Disease Control and Prevention, Atlanta, GA 30333, USA. jkc6@cdc.gov
J E Coligan
T M Folks
S T Butera
National Institute of Allergy and Infectious Diseases · USCenters for Disease Control and Prevention · USNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The identification of cellular factors that are required to complete various steps of the HIV-1 life cycle may lead to the development of new therapeutics. One key step, transcription from the integrated provirus, is inhibited by members of two distinct classes of compounds, the flavonoids and the benzothiophenes, via an unknown mechanism, possibly involving a cellular factor. A marked specificity toward inhibiting HIV-1 transcription is evidenced by the ability of drug-treated cells to retain their proliferative and differentiation capabilities. In addition, the compounds do not impede the activation and function of the transcriptional factor NF-kappaB. Here we report on the identification of several cellular proteins that mediate the HIV-1 transcriptional inhibitory property of the flavonoid chrysin. Chemical and immunologic analyses identified these cellular proteins as the individual subunits of casein kinase II (CKII). Though structurally unrelated to chrysin, an HIV-1 inhibitory benzothiophene also bound selectively to CKII. Both chrysin and the benzothiophenes inhibited human recombinant CKII enzymatic activity and showed competitive kinetics with respect to ATP, analogous to the classic CKII inhibitor 5, 6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB). Moreover, DRB potently inhibited HIV-1 expression in chronically infected cells. CKII may regulate HIV-1 transcription by phosphorylating cellular proteins involved in HIV-1 transactivation that contain multiple CKII phosphorylation consensus sequences.

Indexed as

Transcription, GeneticVirus IntegrationAnti-HIV AgentsCarrier ProteinsCasein Kinase IICatechinCell LineChamomileChromatography, AffinityFlavonoidsHesperidinHIV-1HL-60 CellsHumansKineticsNF-kappa BAnti-HIV AgentsbenzothiopheneCarrier ProteinsCasein Kinase IICatechinchrysinFlavonoidsHesperidinNF-kappa BOils, VolatileProtein Serine-Threonine KinasesRecombinant ProteinsThiophenes

Identifiers

PMID9177178
PMCPMC21010
OpenAlexW2168506538

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.