Evidence map›Paper›PMID 20441790›Full record

ArticleFree radical biology & medicine2010

Accumulation of oxidized proteins in Herpesvirus infected cells.

Shomita S Mathew, Patrick W Bryant, April D Burch

Abstract read
In one paragraph

Article in Free radical biology & medicine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 45 citations in OpenAlex.

  1. Therapeutic Potential of Biochanin A in Herpes Simplex Keratitis.Pharmaceuticals (Basel, Switzerland) · 2023
    Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. A Polyphenol Rich Extract fromMolecules (Basel, Switzerland) · 2018
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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  18. Article
  19. Article
  20. Review
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

3 authors at 2 institutions in 1 country.

Shomita S MathewThe David Axelrod Institute, Wadsworth Center, New York State Department of Health, 120 New Scotland Avenue, USA.
Patrick W Bryant
April D Burch
New York State Department of Health · USWadsworth Center · US

Funding

Defining the role of Hsp90 during HSV-1 infection.K22AI062991 · NIAID · WADSWORTH CENTER · PI BURCH, APRIL DAWN · 2006 to 2007
$270k
NIAID NIH HHS K22 AI062991NIAID NIH HHS K22AI062991
6 · The paper itself

Abstract

Oxidative stress gives rise to an environment that can be highly damaging to proteins, lipids, and DNA. Previous studies indicate that Herpesvirus infections cause oxidative stress in cells and in tissues. The biological consequences of virus-induced oxidative stress have not been characterized. Studies from many groups indicate that proteins which have been damaged through oxidative imbalances are either degraded by the 20S proteasome in a ubiquitin-independent fashion or form aggregates that are resistant to proteolysis. We have previously shown that herpes simplex virus type 1 (HSV-1) replication was significantly enhanced in the presence of the cellular antioxidant chaperone Hsp27, indicating a possible role for this protein in managing virus-induced oxidative stress. Here we show that oxidized proteins accumulate during infections with two distantly related herpesviruses, HSV-1 and Rhesus Rhadinovirus (RRV), a close relative of the Kaposi's sarcoma-associated herpesvirus (KSHV). The presence of oxidized proteins was not entirely unexpected as oxidative stress during herpesvirus infection has been previously documented. Unexpectedly, some oxidized proteins are removed in a proteasome-dependent fashion throughout infection and others resist degradation. Oxidized proteins that resist proteolysis become sequestered in foci within the nucleus and are not associated with virus-induced chaperone enriched domains (VICE), active centers of protein quality control, but rather coincide with Hsp27-enriched foci that were previously described by our laboratory. Experiments also indicate that the accumulation of oxidized proteins is more pronounced in cells depleted for Hsp27. We propose that Hsp27 may facilitate oxidized protein turnover at VICE domains in the nucleus during infection. Hsp27 may also buffer toxic effects of highly-carbonylated, defective proteins that resist proteolysis by promoting their aggregation in the nucleus. These roles of Hsp27 during virus infection are most likely not mutually exclusive.

Indexed as

Oxidative StressAnimalsChlorocebus aethiopsHeLa CellsHerpesviridae InfectionsHerpesvirus 1, HumanHSP27 Heat-Shock ProteinsHumansMolecular ChaperonesOxidation-ReductionProteasome Endopeptidase ComplexProtein CarbonylationProtein DenaturationProteinsRhadinovirusTumor Virus InfectionsHSP27 Heat-Shock ProteinsMolecular ChaperonesProteasome Endopeptidase ComplexProteins

Identifiers

PMID20441790
PMCPMC3206308
OpenAlexW2061405112

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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.