Evidence map›Paper›PMID 22624877›Full record

ArticleTraffic (Copenhagen, Denmark)2012

Recruitment and dynamics of proteasome association with rhTRIM5α cytoplasmic complexes during HIV-1 infection.

Cindy M Danielson, Gianguido C Cianci, Thomas J Hope

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 21% 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

21 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Restriction of HIV-1 and other retroviruses by TRIM5.Nature reviews. Microbiology · 2019
    Review
  9. Role of the Ubiquitin Proteasome System (UPS) in the HIV-1 Life Cycle.International journal of molecular sciences · 2019
    Review
  10. Control of HIV infection by IFN-α: implications for latency and a cure.Cellular and molecular life sciences : CMLS · 2018
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  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 2 countries.

Cindy M DanielsonNorthwestern University, Chicago, IL 60611, USA.
Gianguido C Cianci
Thomas J Hope
Northwestern University · USNorthwestern Medicine · US

Funding

X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
INTRACELLULAR TRAFFICKING OF HIV-1 PARTICLESR01AI047770 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI HOPE, THOMAS · 2000 to 2010
$2.9M
Training Program in Viral ReplicationT32AI060523 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LAIMINS, LAIMONIS A. · 2004 to 2013
$1.4M
Cell Biology of HIV EntryR21AI052051 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI HOPE, THOMAS J · 2002 to 2002
$333k
NIAID NIH HHS 5 RO1 AI047770NIAID NIH HHS R01 AI047770NIAID NIH HHS R21 AI052051NIAID NIH HHS T32 AI060523NIGMS NIH HHS P50 GM082545
6 · The paper itself

Abstract

A variety of proteins have been identified that restrict infection by different viruses. One such restriction factor is the rhesus macaque variant of TRIM5α (rhTRIM5α), which potently blocks infection by HIV-1. The block to infection mediated by rhTRIM5α occurs early after entry into the host cell, generally prior to reverse transcription. However, proteasome inhibitors reveal an intermediate step of restriction in which virus can complete reverse transcription, but still fails to infect the cell. While proteasome inhibitors have been a useful tool in understanding how restriction takes place, the role of the proteasome itself during restriction has not yet been examined. Here, we characterize the interaction of rhTRIM5α and incoming virions with the proteasome. We show that proteasomes localize to rhTRIM5α cytoplasmic bodies, and this localization is more evident when the activity of the proteasome is inhibited pharmacologically. We also show that restricted virus associates with complexes of proteasomes and rhTRIM5α, suggesting that rhTRIM5α utilizes the proteasome during restriction. Finally, live cell imaging experiments reveal that virus associates with proteasomes, and proteasome inhibition affects the duration of association. Taken together, these studies implicate the proteasome as playing a functional role during rhTRIM5α restriction of incoming virions.

Indexed as

AnimalsCells, CulturedCysteine EndopeptidasesCysteine Proteinase InhibitorsCytoplasmHeLa CellsHIV-1HumansLeupeptinsMacaca mulattaOligopeptidesProteasome Endopeptidase ComplexProteinsUbiquitin-Protein LigasesVirionbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCysteine EndopeptidasesCysteine Proteinase InhibitorsepoxomicinLeupeptinsLMP-2 proteinOligopeptidesProteasome Endopeptidase ComplexProteinsTRIM5(alpha) protein, rhesus monkeyUbiquitin-Protein Ligases

Identifiers

PMID22624877
PMCPMC3760259
OpenAlexW1601183731

What OpenQuestion holds

Textmetadata
LicenceTDM
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.