Evidence map›Paper›PMID 22645331›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

BclAF1 restriction factor is neutralized by proteasomal degradation and microRNA repression during human cytomegalovirus infection.

Song Hee Lee, Robert F Kalejta, Julie Kerry, Oliver John Semmes, Christine M O'Connor, Zia Khan, Benjamin A Garcia, Thomas Shenk, Eain Murphy

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

54 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Function of BCLAF1 in human disease.Oncology letters · 2022
    Review
  7. Review
  8. Article
  9. Article
  10. Human Cytomegalovirus miR-UL70-3p Downregulates the HInternational journal of molecular sciences · 2021
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Impact of Natural OccurringInternational journal of molecular sciences · 2020
    Review
  18. Article
  19. Review
  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

9 authors at 3 institutions in 1 country.

Song Hee LeeInstitute for Molecular Virology and McArdle Laboratory for Cancer Research, University of Wisconsin, Madison, WI 53706, USA.
Robert F Kalejta
Julie Kerry
Oliver John Semmes
Christine M O'Connor
Zia Khan
Benjamin A Garcia
Thomas Shenk
Eain Murphy
Princeton University · USEastern Virginia Medical School · USUniversity of Wisconsin–Madison · US

Funding

Spatial Patterning During DevelopmentP50GM071508 · NIGMS · PRINCETON UNIVERSITY · PI POWELL, SUSAN M · 2004 to 2013
$30.6M
HUMAN CYTOMEGALOVIRUS TEGUMENT PROTEINSR01CA082396 · NCI · PRINCETON UNIVERSITY · PI SHENK, THOMAS E · 1999 to 2013
$5.0M
Role of Daxx degradation by pp71 during the Human Cytomegalovirus life cycleR01AI074984 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI KALEJTA, ROBERT F · 2008 to 2018
$3.5M
HTLV-I TAX MEDIATED DEREGULATION OF CELL STATER01CA076595 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI SEMMES, OLIVER JOHN · 1999 to 2016
$2.9M
Mechanisms of Human Cytomegalovirus LatencyR01AI101080 · NIAID · EVRYS BIO, LLC · PI MURPHY, EAIN A · 2013 to 2016
$1.6M
Regulation and Function of the HCMV pp71 Tegument ProteinR03AI074800 · NIAID · EASTERN VIRGINIA MEDICAL SCHOOL · PI KERRY, JULIE A · 2008 to 2009
$206k
NCI NIH HHS CA082396NCI NIH HHS R01 CA076595NCI NIH HHS R01 CA082396NIAID NIH HHS AI074800NIAID NIH HHS AI074984NIAID NIH HHS R01 AI074984NIAID NIH HHS R01 AI101080NIAID NIH HHS R03 AI074800NIGMS NIH HHS GM071508NIGMS NIH HHS P50 GM071508
6 · The paper itself

Abstract

Cell proteins can restrict the replication of viruses. Here, we identify the cellular BclAF1 protein as a human cytomegalovirus restriction factor and describe two independent mechanisms the virus uses to decrease its steady-state levels. Immediately following infection, the viral pp71 and UL35 proteins, which are delivered to cells within virions, direct the proteasomal degradation of BclAF1. Although BclAF1 reaccumulates through the middle stages of infection, it is subsequently down-regulated at late times by miR-UL112-1, a virus-encoded microRNA. In the absence of BclAF1 neutralization, viral gene expression and replication are inhibited. These data identify two temporally and mechanistically distinct functions used by human cytomegalovirus to down-regulate a cellular antiviral protein.

Indexed as

CytomegalovirusCytomegalovirus InfectionsGenes, Immediate-EarlyHumansHydrolysisMicroRNAsProteasome Endopeptidase ComplexRepressor ProteinsTumor Suppressor ProteinsBCLAF1 protein, humanMicroRNAsProteasome Endopeptidase ComplexRepressor ProteinsTumor Suppressor Proteins

Identifiers

PMID22645331
PMCPMC3386064
OpenAlexW2043486017

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.