Evidence map›Paper›PMID 17392513›Full record

ArticleMolecular biology of the cell2007

TRIM5 alpha cytoplasmic bodies are highly dynamic structures.

Edward M Campbell, Mark P Dodding, Melvyn W Yap, Xiaolu Wu, Sarah Gallois-Montbrun, Michael H Malim, Jonathan P Stoye, Thomas J Hope

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

46 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Human TRIM5α senses and restricts LINE-1 elements.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Restriction of HIV-1 and other retroviruses by TRIM5.Nature reviews. Microbiology · 2019
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

8 authors at 4 institutions in 2 countries.

Edward M CampbellDepartment of Cell and Molecular Biology, Northwestern University, Chicago, IL 60611-3008, USA.
Mark P Dodding
Melvyn W Yap
Xiaolu Wu
Sarah Gallois-Montbrun
Michael H Malim
Jonathan P Stoye
Thomas J Hope
Medical Research Council · GBGuy's Hospital · GBNorthwestern University · USUniversity of Illinois Chicago · US

Funding

Medical Research Council G0401570Medical Research Council MC_U117512710
6 · The paper itself

Abstract

Tripartite motif (TRIM)5 alpha has recently been identified as a host restriction factor that has the ability to block infection by certain retroviruses in a species-dependent manner. One interesting feature of this protein is that it is localized in distinct cytoplasmic clusters designated as cytoplasmic bodies. The potential role of these cytoplasmic bodies in TRIM5 alpha function remains to be defined. By using fluorescent fusion proteins and live cell microscopy, we studied the localization and dynamics of TRIM5 alpha cytoplasmic bodies. This analysis reveals that cytoplasmic bodies are highly mobile, exhibiting both short saltatory movements and unidirectional long-distance movements along the microtubule network. The morphology of the cytoplasmic bodies is also dynamic. Finally, photobleaching and photoactivation analysis reveals that the TRIM5 alpha protein present in the cytoplasmic bodies is very dynamic, rapidly exchanging between cytoplasmic bodies and a more diffuse cytoplasmic population. Therefore, TRIM5 alpha cytoplasmic bodies are dynamic structures more consistent with a role in function or regulation rather than protein aggregates or inclusion bodies that represent dead-end static structures.

Indexed as

AnimalsAntiviral Restriction FactorsCarrier ProteinsCell LineCytoplasmCytoskeletonFluorescence Recovery After PhotobleachingHumansInclusion BodiesMicroscopy, FluorescenceMicrotubulesRecombinant Fusion ProteinsTripartite Motif ProteinsUbiquitin-Protein LigasesAntiviral Restriction FactorsCarrier ProteinsRecombinant Fusion ProteinsTRIM5 protein, humanTripartite Motif ProteinsUbiquitin-Protein Ligases

Identifiers

PMID17392513
PMCPMC1877106
OpenAlexW2028811194

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.