ArticleJournal of virology2008
Biochemical and biophysical characterization of a chimeric TRIM21-TRIM5alpha protein.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
What it found
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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.
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.
Who cites it
56 citing papers in PubMed, 69 citations in OpenAlex.
- Primate TRIM34 is a broadly-acting, TRIM5-dependent lentiviral restriction factor.Retrovirology · 2023Article
- Primate TRIM34 is a broadly-acting, TRIM5-dependent lentiviral restriction factor.bioRxiv : the preprint server for biology · 2023Article
- Restriction of HIV-1 and other retroviruses by TRIM5.Nature reviews. Microbiology · 2019Review
- General Model for Retroviral Capsid Pattern Recognition by TRIM5 Proteins.Journal of virology · 2018Article
- TRIM5α SPRY/coiled-coil interactions optimize avid retroviral capsid recognition.PLoS pathogens · 2017Article
- Role of SUMO activating enzyme in cancer stem cell maintenance and self-renewal.Nature communications · 2016Article
- Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5α.eLife · 2016Article
- Article
- RING Dimerization Links Higher-Order Assembly of TRIM5α to Synthesis of K63-Linked Polyubiquitin.Cell reports · 2015Article
- Contribution of MxB oligomerization to HIV-1 capsid binding and restriction.Journal of virology · 2015Article
- Article
- Article
- Intrapolypeptide interactions between the GTPase effector domain (GED) and the GTPase domain form the bundle signaling element in dynamin dimers.Biochemistry · 2014Article
- Restriction of HIV-1 by rhesus TRIM5α is governed by alpha helices in the Linker2 region.Journal of virology · 2014Article
- Functional evidence for the involvement of microtubules and dynein motor complexes in TRIM5α-mediated restriction of retroviruses.Journal of virology · 2014Article
- Recognition of the HIV capsid by the TRIM5α restriction factor is mediated by a subset of pre-existing conformations of the TRIM5α SPRY domain.Biochemistry · 2014Article
- The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Binding of the rhesus TRIM5α PRYSPRY domain to capsid is necessary but not sufficient for HIV-1 restriction.Virology · 2014Article
- Rhesus monkey TRIM5α SPRY domain recognizes multiple epitopes that span several capsid monomers on the surface of the HIV-1 mature viral core.Journal of molecular biology · 2013Article
- Host Factors and HIV-1 Replication: Clinical Evidence and Potential Therapeutic Approaches.Frontiers in immunology · 2013Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The tripartite motif (TRIM) protein, TRIM5alpha, is an endogenous factor in primates that recognizes the capsids of certain retroviruses after virus entry into the host cell. TRIM5alpha promotes premature uncoating of the capsid, thus blocking virus infection. Low levels of expression and tendencies to aggregate have hindered the biochemical, biophysical, and structural characterization of TRIM proteins. Here, a chimeric TRIM5alpha protein (TRIM5(Rh)-21R) with a RING domain derived from TRIM21 was expressed in baculovirus-infected insect cells and purified. Although a fraction of the TRIM5(Rh)-21R protein formed large aggregates, soluble fractions of the protein formed oligomers (mainly dimers), exhibited a protease-resistant core, and contained a high percentage of helical secondary structure. Cross-linking followed by negative staining and electron microscopy suggested a globular structure. The purified TRIM5(Rh)-21R protein displayed E3-ligase activity in vitro and also self-ubiquitylated in the presence of ubiquitin-activating and -conjugating enzymes. The purified TRIM5(Rh)-21R protein specifically associated with human immunodeficiency virus type 1 capsid-like complexes; a deletion within the V1 variable region of the B30.2(SPRY) domain decreased capsid binding. Thus, the TRIM5(Rh)-21R restriction factor can directly recognize retroviral capsid-like complexes in the absence of other mammalian proteins.
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What OpenQuestion holds
Registered trials
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.