Evidence map›Paper›PMID 16775307›Full record

ArticleJournal of virology2006

Functional replacement of the RING, B-box 2, and coiled-coil domains of tripartite motif 5alpha (TRIM5alpha) by heterologous TRIM domains.

Xing Li, Yuan Li, Matthew Stremlau, Wen Yuan, Byeongwoon Song, Michel Perron, Joseph Sodroski

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

40 citing papers in PubMed, 58 citations in OpenAlex.

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  15. Lentiviral vector gene transfer to porcine airways.Molecular therapy. Nucleic acids · 2012
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  17. HIV type 1 Gag as a target for antiviral therapy.AIDS research and human retroviruses · 2012
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  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

7 authors at 2 institutions in 1 country.

Xing LiDepartment of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, 44 Binney Street-JFB 824, Boston, MA 02115, USA.
Yuan Li
Matthew Stremlau
Wen Yuan
Byeongwoon Song
Michel Perron
Joseph Sodroski
Harvard University · USDana-Farber Cancer Institute · US

Funding

TRANSPLANTATION IN MODELS OF GENETIC DISEASEP50HL054785 · NHLBI · DANA-FARBER CANCER INSTITUTE · PI NATHAN, DAVID G. · 1995 to 2004
$8.8M
DFCI-BIDMC-CH CENTER FOR AIDS RESEARCHP30AI028691 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1989 to 2003
$6.2M
Antiretroviral Activity of TRIM5alphaR01AI063987 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 2005 to 2014
$4.2M
NHLBI NIH HHS HL 54785NHLBI NIH HHS P50 HL054785NIAID NIH HHS AI 063987NIAID NIH HHS P30 AI028691NIAID NIH HHS R01 AI063987
6 · The paper itself

Abstract

Tripartite motif 5alpha (TRIM5alpha) restricts some retroviruses, including human immunodeficiency virus type 1 (HIV-1), from infecting the cells of particular species. TRIM5alpha is a member of the TRIM family of proteins, which contain RING, B-box, coiled-coil (CC), and, in some cases, B30.2(SPRY) domains. Here we investigated the abilities of domains from TRIM proteins (TRIM6, TRIM34, and TRIM21) that do not restrict HIV-1 infection to substitute for the domains of rhesus monkey TRIM5alpha (TRIM5alpha(rh)). The RING, B-box 2, and CC domains of the paralogous TRIM6 and TRIM34 proteins functionally replaced the corresponding TRIM5alpha(rh) domains, allowing HIV-1 restriction. By contrast, similar chimeras containing the components of TRIM21, a slightly more distant relative of TRIM5, did not restrict HIV-1 infection. The TRIM21 B-box 2 domain and its flanking linker regions contributed to the functional defectiveness of these chimeras. All of the chimeric proteins formed trimers. All of the chimeras that restricted HIV-1 infection bound the assembled HIV-1 capsid complexes. These results indicate that heterologous RING, B-box 2, and CC domains from related TRIM proteins can functionally substitute for TRIM5alpha(rh) domains.

Indexed as

Amino Acid MotifsAnimalsCarrier ProteinsDNA-Binding ProteinsHeLa CellsHIV-1HIV InfectionsHumansMacaca mulattaMolecular Sequence DataMultiprotein ComplexesMutant Chimeric ProteinsNuclear ProteinsNucleocapsidProtein BindingProteinsCarrier ProteinsDNA-Binding ProteinsMultiprotein ComplexesMutant Chimeric ProteinsNuclear ProteinsProteinsRibonucleoproteinsSS-A AntigenTRIM34 protein, humanTRIM5(alpha) protein, rhesus monkeyTRIM6 protein, humanTripartite Motif ProteinsUbiquitin-Protein Ligases

Identifiers

PMID16775307
PMCPMC1488960
OpenAlexW2136137668

What OpenQuestion holds

Textmetadata
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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.