Evidence map›Paper›PMID 17622316›Full record

ArticleMolecular medicine (Cambridge, Mass.)

Anti-vpr activities of heat shock protein 27.

Dong Liang, Zsigmond Benko, Emmanuel Agbottah, Michael Bukrinsky, Richard Y Zhao

Open access · goldAbstract read
In one paragraph

Article in Molecular medicine (Cambridge, Mass.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

13 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Vpr-host interactions during HIV-1 viral life cycle.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2011
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

5 authors at 3 institutions in 1 country.

Dong LiangDepartment of Pathology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.
Zsigmond Benko
Emmanuel Agbottah
Michael Bukrinsky
Richard Y Zhao
George Washington University · USNorthwestern University · USUniversity of Maryland, Baltimore · US

Funding

VPR AND HIV1 NUCLEAR TRANSLOCATIONR01AI033776 · NIAID · PICOWER INSTITUTE FOR MEDICAL RESEARCH · PI BUKRINSKY, MICHAEL ILYA · 1998 to 2006
$2.0M
Effect of HIV-1 Vpr on Basic Cellular Functions (II)R01AI040891 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI ZHAO, RICHARD YUQI · 2003 to 2007
$1.4M
Cell Cycle G2/M Pathway Modulated by Viral Protein RR01GM063080 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI ZHAO, RICHARD YUQI · 2002 to 2006
$968k
Effect of HIV-1 Vpr on Basic Cellular FunctionsR21AI040891 · NIAID · CHILDREN'S MEMORIAL HOSPITAL (CHICAGO) · PI ZHAO, RICHARD YUQI · 2002 to 2002
$249k
Role of Vpr in HIV-1 Nuclear TranslocationR21AI033776 · NIAID · GEORGE WASHINGTON UNIVERSITY · PI BUKRINSKY, MICHAEL ILYA · 2001 to 2001
$215k
HIV-1 VPR AND BASIC CELLULAR FUNCTIONSR29AI040891 · NIAID · CHILDREN'S MEMORIAL HOSPITAL (CHICAGO) · PI ZHAO, RICHARD YUQI · 1997 to 2001
$209k
MATRIX PROTEIN (MAP17) AND HIV-1 LIFE CYCLER29AI033776 · NIAID · PICOWER INSTITUTE FOR MEDICAL RESEARCH · PI BUKRINSKY, MICHAEL ILYA · 1993 to 1997
–
NIAID NIH HHS AI33776NIAID NIH HHS AI40891NIAID NIH HHS R01 AI033776NIAID NIH HHS R01 AI040891NIAID NIH HHS R21 AI033776NIAID NIH HHS R21 AI040891NIAID NIH HHS R29 AI033776NIAID NIH HHS R29 AI040891NIGMS NIH HHS GM63080NIGMS NIH HHS R01 GM063080
6 · The paper itself

Abstract

HIV-1 Vpr plays a pivotal role in viral pathogenesis and is preferentially targeted by the host immune system. In this report, we demonstrate that a small heat shock protein, HSP27, exhibits Vpr-specific antiviral activity, as its expression is specifically responsive to vpr gene expression and increased levels of HSP27 inhibit Vpr-induced cell cycle G2 arrest and cell killing. We further show that overexpression of HSP27 reduces viral replication in T-lymphocytes in a Vpr-dependent manner. Mechanistically, Vpr triggers HSP27 expression through heat shock factor (HSF) 1, but inhibits prolonged expression of HSP27 under heat-shock conditions. Together, these data suggest a potential dynamic and antagonistic interaction between HIV-1 Vpr and a host cell HSP27, suggesting that HSP27 may contribute to cellular intrinsic immunity against HIV infection.

Indexed as

ApoptosisCell LineDNA-Binding ProteinsG2 PhaseGene ExpressionGene Products, vprHeat-Shock ProteinsHeat-Shock ResponseHeat Shock Transcription FactorsHIV-1HIV InfectionsHumansT-LymphocytesTranscription FactorsVirus Replicationvpr Gene Products, Human Immunodeficiency VirusDNA-Binding ProteinsGene Products, vprHeat-Shock ProteinsHeat Shock Transcription FactorsTranscription Factorsvpr Gene Products, Human Immunodeficiency Virus

Identifiers

PMID17622316
PMCPMC1906686
OpenAlexW2469615346

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.