ArticleImmunogenetics2009
Different subcellular localisations of TRIM22 suggest species-specific function.
Article in Immunogenetics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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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.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- TRIM22 inhibits the proliferation of gastric cancer cells through the Smad2 protein.Cell death discovery · 2021Article
- TRIM22. A Multitasking Antiviral Factor.Cells · 2021Review
- Tripartite Motif 22 (TRIM22) protein restricts herpes simplex virus 1 by epigenetic silencing of viral immediate-early genes.PLoS pathogens · 2021Article
- Characterization of the primate TRIM gene family reveals the recent evolution in primates.Molecular genetics and genomics : MGG · 2020Article
- Tripartite Motif 22 and Class II Transactivator Restriction Factors: Unveiling Their Concerted Action against Retroviruses.Frontiers in immunology · 2017Review
- Variants in TRIM22 That Affect NOD2 Signaling Are Associated With Very-Early-Onset Inflammatory Bowel Disease.Gastroenterology · 2016Article
- Interferon alpha (IFNα)-induced TRIM22 interrupts HCV replication by ubiquitinating NS5A.Cellular & molecular immunology · 2016Article
- TRIM22: A Diverse and Dynamic Antiviral Protein.Molecular biology international · 2012Article
- TRIM22 inhibits HIV-1 transcription independently of its E3 ubiquitin ligase activity, Tat, and NF-kappaB-responsive long terminal repeat elements.Journal of virology · 2011Article
- Estrogen induced breast cancer is the result in the disruption of the asymmetric cell division of the stem cell.Hormone molecular biology and clinical investigation · 2010Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The B30.2/SPRY domain is present in many proteins, including various members of the tripartite motif (TRIM) protein family such as TRIM5alpha, which mediates innate intracellular resistance to retroviruses in several primate species. This resistance is dependent on the integrity of the B30.2 domain that evolves rapidly in primates and exhibits species-specific anti-viral activity. TRIM22 is another positively selected TRIM gene. Particularly, the B30.2 domain shows rapid evolution in the primate lineage and recently published data indicate an anti-viral function of TRIM22. We show here that human and rhesus TRIM22 localise to different subcellular compartments and that this difference can be assigned to the positively selected B30.2 domain. Moreover, we could demonstrate that amino acid changes in two variable loops (VL1 and VL3) are responsible for the different subcellular localisations.
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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.