ArticleCurrent biology : CB2018
TIR Domain Proteins Are an Ancient Family of NAD
Article in Current biology : CB, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 146 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
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Who cites it
146 citing papers in PubMed, 250 citations in OpenAlex.
- Article
- Boldine inhibits SARM1 NADase Activity and Preserves Axonal Integrity After Nerve Injury.bioRxiv : the preprint server for biology · 2026Article
- Eukaryotic domestication of a bacterial immune protein following horizontal transfer.bioRxiv : the preprint server for biology · 2026Article
- The rise and fall of SARM1 base-exchange inhibitors.Communications chemistry · 2026Article
- Chemical inactivation of a bacterial immune system de-domesticates a temperate phage and promotes its spread.bioRxiv : the preprint server for biology · 2026Article
- TIR-like NADases act in bacterial immunity and the RNA vault.bioRxiv : the preprint server for biology · 2026Article
- A unique echinoderm NLR triggers Vibrio phagocytosis by promoting microtubule severing to facilitate microfilament polymerization.The Journal of biological chemistry · 2026Article
- SARM1 activation promotes axonal degeneration via a two-step phase transition.Nature chemical biology · 2026Article
- Chemical inhibition of a bacterial immune system.Cell host & microbe · 2026Article
- Molecular mechanisms of plant NLR activation and signalling.The Plant journal : for cell and molecular biology · 2026Review
- Regulated cell death in fungi from a comparative immunology perspective.Cell death and differentiation · 2026Review
- Programmed axon degeneration: mechanism, inhibition and therapeutic potential.Nature reviews. Neuroscience · 2026Review
- Manipulation of the nucleotide pool in human, bacterial and plant immunity.Nature reviews. Immunology · 2026Review
- Molecular characterisation of the Bacillus subtilis SpbK antiphage defence system.Nature communications · 2025Article
- TIR-domain-containing protein C as modulator of innate immune checkpoints.Scientific reports · 2025Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2025Article
- miR825-5p-regulated TNLs govern Arabidopsis resistance to Tetranychus urticae and Pieris brassicae.The New phytologist · 2025Article
- SARM1: The Checkpoint of Axonal Degeneration in the Nervous System Disorders.Molecular neurobiology · 2025Review
- Carnosol, a Rosemary Ingredient Discovered in a Screen for Inhibitors of SARM1-NADAntioxidants (Basel, Switzerland) · 2025Article
- Evolutionarily ancient functions of enzymatic TIR proteins in innate immunity.Trends in immunology · 2025Review
86 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The Toll/interleukin-1 receptor (TIR) domain is the signature signaling domain of Toll-like receptors (TLRs) and their adaptors, serving as a scaffold for the assembly of protein complexes for innate immune signaling [1, 2]. TIR domain proteins are also expressed in plants, where they mediate disease resistance [3, 4], and in bacteria, where they have been associated with virulence [5-9]. In pursuing our work on axon degeneration [10], we made the surprising discovery that the TIR domain of SARM1 (sterile alpha and TIR motif containing 1), a TLR adaptor protein, has enzymatic activity [11]. Upon axon injury, the SARM1 TIR domain cleaves nicotinamide adenine dinucleotide (NAD
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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.