ArticleStructure (London, England : 1993)2013
Structural insights into the functions of TBK1 in innate antimicrobial immunity.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 120 citations in OpenAlex.
- NAP1 switches from an activator to a limiter of interferon induction by trapping TBK1 in condensates.Nature communications · 2026Article
- Evaluation of the Anti-Cancer Effects of KMU-11342 in In Vitro and Ex Vivo Models of Colorectal Cancer.Pharmaceuticals (Basel, Switzerland) · 2026Article
- PtdIns(3,5)PNature · 2026Article
- A novel small molecule KMU-11361 attenuates rheumatoid arthritis by mechanistic inhibition of the TAK1-NF-κB-NLRP3 axis.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026Article
- Review
- Dual roles of TRPV2 in the innate immune response to cytosolic DNA: Arresting dormant and boosting activated STING.Cell reports · 2026Article
- SVCV phosphoprotein hijacks phase separation to immobilize the IRF3-TBK1 signaling axis and suppress interferon antiviral immunity.Journal of virology · 2026Article
- Integrating state-space modeling, parameter estimation, deep learning, and docking techniques in drug repurposing: a case study on COVID-19 cytokine storm.Journal of the American Medical Informatics Association : JAMIA · 2026Article
- PtdIns(3,5)PbioRxiv : the preprint server for biology · 2025Article
- Exploring TANK-Binding Kinase 1 in Amyotrophic Lateral Sclerosis: From Structural Mechanisms to Machine Learning-Guided Therapeutics.Life (Basel, Switzerland) · 2025Review
- Nitrofuran-Based STING Inhibitors.ACS omega · 2025Article
- Targeting the cGAS-STING Pathway to Modulate Immune Inflammation in Diabetes and Cardiovascular Complications: Mechanisms and Therapeutic Insights.Current issues in molecular biology · 2025Review
- STING COPII ER Export Trafficking and Signaling Primed by Phosphorylation Switches.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- TBK1 is a signaling hub in coordinating stress-adaptive mechanisms in head and neck cancer progression.Autophagy · 2025Article
- Activated TBK1 promotes ACSL1-mediated microglia lipid droplet accumulation and neuroinflammation in Parkinson's disease.Journal of neuroinflammation · 2025Article
- Getah virus nonstructural protein 2 suppresses interferon-beta production by interrupting interferon regulatory factor 3 activation.Veterinary research · 2025Article
- Hepatitis B surface antigen hijacks TANK-binding kinase 1 to suppress type I interferon and induce early autophagy.Cell death & disease · 2025Article
- TANK-Binding Kinase 1 in the Pathogenesis and Treatment of Inflammation-Related Diseases.International journal of molecular sciences · 2025Review
- Article
- Development and characterization of high-efficiency cell-adapted live attenuated vaccine candidate against African swine fever.Emerging microbes & infections · 2024Article
12 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 4 institutions in 1 country.
Funding
Abstract
Tank-binding kinase 1 (TBK1) is a serine/threonine protein-kinase mediating innate antimicrobial immunity. TBK1 is involved in the signaling of TLRs, RLRs, and STING-mediated sensing of cytosolic DNA. Stimulation of these receptors results in the activation of TBK1, which phosphorylates interferon regulatory factor (IRF)-3. Phosphorylated IRF-3 translocates into the nucleus to initiate the transcription of the interferon (IFN)-β gene. Here, we show that TBK1 is activated by autophosphorylation at residue Ser172. Structures of TBK1 bound to two inhibitors showed that TBK1 has the IκB kinase fold with three distinct domains: the kinase domain, the ubiquitin-like domain, and the scaffold and dimerization domain. However, the overall structures of the TBK1 monomer and its dimer are different from IKKβ in the arrangements of the three domains and in dimer formation. Phosphorylation of IRF-3 by TBK1 in vitro results in its oligomerization, and phosphorylation of residue Ser386 plays a key role in IRF-3 activation.
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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.