ArticleImmunogenetics2020
A survey of TIR domain sequence and structure divergence.
Article in Immunogenetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 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
18 citing papers in PubMed, 42 citations in OpenAlex.
- Eukaryotic domestication of a bacterial immune protein following horizontal transfer.bioRxiv : the preprint server for biology · 2026Article
- ARIES domains: functional signaling units of type I interferon responses.The FEBS journal · 2025Review
- Massively Parallel Screening of Toll/Interleukin-1 Receptor (TIR)-Derived Peptides Reveals Multiple Toll-Like Receptors (TLRs)-Targeting Immunomodulatory Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Toll-like Receptor Expression inGenes · 2024Article
- Target ssDNA activates the NADase activity of prokaryotic SPARTA immune system.Nature chemical biology · 2024Article
- TLR5-Derived, TIR-Interacting Decoy Peptides to Inhibit TLR Signaling.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- Variation in plant Toll/Interleukin-1 receptor domain protein dependence on ENHANCED DISEASE SUSCEPTIBILITY 1.Plant physiology · 2023Article
- Exploring a diverse world of effector domains and amyloid signaling motifs in fungal NLR proteins.PLoS computational biology · 2022Article
- Bacterial origins of human cell-autonomous innate immune mechanisms.Nature reviews. Immunology · 2022Review
- Article
- Molecular innovations in plant TIR-based immunity signaling.The Plant cell · 2022Review
- Products of gut microbial Toll/interleukin-1 receptor domain NADase activities in gnotobiotic mice and Bangladeshi children with malnutrition.Cell reports · 2022Article
- TIRAP-mediated activation of p38 MAPK in inflammatory signaling.Scientific reports · 2022Article
- Conformational Dynamics of the Soluble and Membrane-Bound Forms of Interleukin-1 Receptor Type-1: Insights into Linker Flexibility and Domain Orientation.International journal of molecular sciences · 2022Article
- NLRexpress-A bundle of machine learning motif predictors-Reveals motif stability underlying plant Nod-like receptors diversity.Frontiers in plant science · 2022Article
- TIAMMAt: Leveraging Biodiversity to Revise Protein Domain Models, Evidence from Innate Immunity.Molecular biology and evolution · 2021Article
- Toll-Like Receptors: General Molecular and Structural Biology.Journal of immunology research · 2021Review
- Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Toll-interleukin-1R resistance (TIR) domains are ubiquitously present in all forms of cellular life. They are most commonly found in signaling proteins, as units responsible for signal-dependent formation of protein complexes that enable amplification and spatial propagation of the signal. A less common function of TIR domains is their ability to catalyze nicotinamide adenine dinucleotide degradation. This survey analyzes 26,414 TIR domains, automatically classified based on group-specific sequence patterns presumably determining biological function, using a statistical approach termed Bayesian partitioning with pattern selection (BPPS). We examine these groups and patterns in the light of available structures and biochemical analyses. Proteins within each of thirteen eukaryotic groups (10 metazoans and 3 plants) typically appear to perform similar functions, whereas proteins within each prokaryotic group typically exhibit diverse domain architectures, suggesting divergent functions. Groups are often uniquely characterized by structural fold variations associated with group-specific sequence patterns and by herein identified sequence motifs defining TIR domain functional divergence. For example, BPPS identifies, in helices C and D of TIRAP and MyD88 orthologs, conserved surface-exposed residues apparently responsible for specificity of TIR domain interactions. In addition, BPPS clarifies the functional significance of the previously described Box 2 and Box 3 motifs, each of which is a part of a larger, group-specific block of conserved, intramolecularly interacting residues.
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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.