Evidence map›Paper›PMID 9621019›Full record

ArticleJournal of virology1998

Persistent activation of RelA by respiratory syncytial virus involves protein kinase C, underphosphorylated IkappaBbeta, and sequestration of protein phosphatase 2A by the viral phosphoprotein.

V Bitko, S Barik

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 66 citations in OpenAlex.

  1. Regulatory role of microRNAs in virus-mediated inflammation.Journal of inflammation (London, England) · 2024
    Review
  2. Pathway expression analysis.Scientific reports · 2022
    Article
  3. Review
  4. Article
  5. Rescue from Stx2-Producing E. coli-Associated Encephalopathy by Intravenous Injection of Muse Cells in NOD-SCID Mice.Molecular therapy : the journal of the American Society of Gene Therapy · 2020
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
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  15. Review
  16. Respiratory syncytial virus induces insensitivity to beta-adrenergic agonists in mouse lung epithelium in vivo.American journal of physiology. Lung cellular and molecular physiology · 2007
    Article
  17. Article
  18. Article
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  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.

V BitkoDepartment of Biochemistry and Molecular Biology, College of Medicine, University of South Alabama, Mobile, Alabama 36688-0002, USA.
S Barik
University of South Alabama · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Respiratory syncytial virus (RSV) activated the RelA (p65) subunit of nuclear factor kappa B (NF-kappaB) over many hours postinfection. The initial activation coincided with phosphorylation and degradation of IkappaBalpha, the cytoplasmic inhibitor of RelA. During persistent activation of NF-kappaB at later times in infection, syntheses of inhibitors IkappaBalpha as well as IkappaBbeta were restored. However, the resynthesized IkappaBbeta was in an underphosphorylated state, which apparently prevented inhibition of NF-kappaB. Use of specific inhibitors suggested that the pathway leading to the persistent-but not the initial-activation of NF-kappaB involved signaling through protein kinase C (PKC) and reactive oxygen intermediates of nonmitochondrial origin, whereas phospholipase C or D played little or no role. Thus, RSV infection led to the activation of NF-kappaB by a biphasic mechanism: a transient or early activation involving phosphorylation of the inhibitor IkappaB polypeptides, and a persistent or long-term activation requiring PKC and the generation of hypophosphorylated IkappaBbeta. At least a part of the activation was through a novel mechanism in which the viral phosphoprotein P associated with but was not dephosphorylated by protein phosphatase 2A and thus sequestered and inhibited the latter. We postulate that this led to a net increase in the phosphorylation state of signaling proteins that are responsible for RelA activation.

Indexed as

HN ProteinI-kappa B ProteinsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesDNA-Binding ProteinsMolecular Sequence DataNF-kappa BPhosphoprotein PhosphatasesPhosphorylationProtein Kinase CProtein Phosphatase 2RabbitsRespiratory Syncytial Virus, HumanTranscription Factor RelAViral Envelope Proteinsattachment protein GCalcium-Calmodulin-Dependent Protein KinasesDNA-Binding ProteinsHN ProteinI kappa B beta proteinI-kappa B ProteinsNF-kappa BPhosphoprotein PhosphatasesProtein Kinase CProtein Phosphatase 2Transcription Factor RelAViral Envelope ProteinsViral Proteins

Identifiers

PMID9621019
PMCPMC110221
OpenAlexW2158608067

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.