ArticleBiology direct2017
The complex domain architecture of SAMD9 family proteins, predicted STAND-like NTPases, suggests new links to inflammation and apoptosis.
Article in Biology direct, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.
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Who cites it
43 citing papers in PubMed, 1 synthesis or guideline pooled it, 67 citations in OpenAlex.
- A genome-wide association study of survival in patients with sepsis.Critical care (London, England) · 2022Pooled it
- Structural mechanisms of SAMD9 autoinhibition and pathogenic dysregulation.Science advances · 2026Article
- A NACHT domain-containing protein Ncp is required for appendage-associated unconventional protein secretion in the fungusiScience · 2026Article
- From a novel pathogenic SAMD9L variant to cohort-wide insights: Whole-genome sequencing highlights somatic genetic rescue and phenotypic heterogeneity.British journal of haematology · 2026Article
- Lost in translation: interferon-stimulated genes targeting flavivirus protein synthesis.Journal of virology · 2026Review
- Bacterial Schlafen proteins mediate phage defence.Nature microbiology · 2026Article
- Diverse bacterial pattern recognition receptors sense the conserved phage proteome.bioRxiv : the preprint server for biology · 2026Article
- Evolution of SAMD9 and SAMD9L genes in primates: a complex history of gene loss, gene duplication and pseudogenization.Immunogenetics · 2025Article
- SAMD9L inhibits flavivirus translation independently of its capacity to trigger innate immune response.PLoS pathogens · 2025Article
- Evolutionary characterization of antiviral SAMD9/9L across kingdoms supports ancient convergence and lineage-specific adaptations.Nature ecology & evolution · 2025Article
- Normal Immune Function in a Newborn With Early Identification of aClinical case reports · 2025Article
- Poxvirus Host-Range Determinants: SAMD9/9L and Beyond.Annual review of virology · 2025Review
- Structural and functional studies of rabbit SAMD9 reveal a distinct tRNase module that underlies the antiviral activity.PLoS pathogens · 2025Article
- Ancient convergence with prokaryote defense and recent adaptations to lentiviruses in primates characterize the ancestral immune factors SAMD9s.bioRxiv : the preprint server for biology · 2025Article
- DnaJ mediates phage sensing by the bacterial NLR-related protein bNACHT25.PLoS biology · 2025Article
- SAMD9 senses cytosolic double-stranded nucleic acids in epithelial and mesenchymal cells to induce antiviral immunity.Nature communications · 2025Article
- Structural and Functional Studies of Rabbit SAMD9 Reveal a Distinct tRNase Module That Underlies the Antiviral Activity.bioRxiv : the preprint server for biology · 2025Article
- Review
- Overexpression of human SAMD9 inhibits protein translation and alters MYC signaling resulting in cell cycle arrest.Experimental hematology · 2024Article
- SAMD9L acts as an antiviral factor against HIV-1 and primate lentiviruses by restricting viral and cellular translation.PLoS biology · 2024Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
We report a comprehensive computational dissection of the domain architecture of the SAMD9 family proteins that are involved in antivirus and antitumor response in humans. We show that the SAMD9 protein family is represented in most animals and also, unexpectedly, in bacteria, in particular actinomycetes. From the N to C terminus, the core SAMD9 family architecture includes DNA/RNA-binding AlbA domain, a variant Sir2-like domain, a STAND-like P-loop NTPase, an array of TPR repeats and an OB-fold domain with predicted RNA-binding properties. Vertebrate SAMD9 family proteins contain the eponymous SAM domain capable of polymerization, whereas some family members from other animals instead contain homotypic adaptor domains of the DEATH superfamily, known as dedicated components of apoptosis networks. Such complex domain architecture is reminiscent of the STAND superfamily NTPases that are involved in various signaling processes, including programmed cell death, in both eukaryotes and prokaryotes. These findings suggest that SAMD9 is a hub of a novel, evolutionarily conserved defense network that remains to be characterized. REVIEWERS: This article was reviewed by Igor B. Zhulin and Mensur Dlakic.
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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.