ArticleProtein & cell2012
Crystal structure of the ubiquitin-like domain of human TBK1.
Article in Protein & cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- TANK potentiates antiviral innate immunity by recruiting deubiquitinase USP46 to activate IKKε.PLoS pathogens · 2026Article
- Review
- A preliminary study on the regulatory role of phosphoribosyl pyrophosphate synthetase 2 in vesicular stomatitis virus infection.Virus genes · 2026Article
- Role of TBK1 Inhibition in Targeted Therapy of Cancer.Mini reviews in medicinal chemistry · 2024Review
- Mitochondria-associated membrane collapse impairs TBK1-mediated proteostatic stress response in ALS.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- TBK1-medicated DRP1 phosphorylation orchestrates mitochondrial dynamics and autophagy activation in osteoarthritis.Acta pharmacologica Sinica · 2023Article
- Influenza A virus use of BinCARD1 to facilitate the binding of viral NP to importin α7 is counteracted by TBK1-p62 axis-mediated autophagy.Cellular & molecular immunology · 2022Article
- Article
- The role of TBK1 in cancer pathogenesis and anticancer immunity.Journal of experimental & clinical cancer research : CR · 2022Review
- Inhibitory targeting cGAS-STING-TBK1 axis: Emerging strategies for autoimmune diseases therapy.Frontiers in immunology · 2022Review
- Global chromatin organizer SATB1 acts as a context-dependent regulator of the Wnt/Wg target genes.Scientific reports · 2021Article
- Small molecules targeting the innate immune cGAS‒STING‒TBK1 signaling pathway.Acta pharmaceutica Sinica. B · 2020Review
- Mendelian genes in primary open angle glaucoma.Experimental eye research · 2019Review
- Association of the TBK1 mutation p.Ile334Thr with frontotemporal dementia and literature review.Molecular genetics & genomic medicine · 2019Review
- Zika virus NS5 protein antagonizes type I interferon production via blocking TBK1 activation.Virology · 2019Article
- ALS-associated missense and nonsense TBK1 mutations can both cause loss of kinase function.Neurobiology of aging · 2018Article
- TBK1: a new player in ALS linking autophagy and neuroinflammation.Molecular brain · 2017Review
- Human TBK1: A Gatekeeper of Neuroinflammation.Trends in molecular medicine · 2016Review
- Structural insights into the functions of TBK1 in innate antimicrobial immunity.Structure (London, England : 1993) · 2013Article
- Structure and ubiquitination-dependent activation of TANK-binding kinase 1.Cell reports · 2013Article
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 3 institutions in 2 countries.
Funding
Abstract
TANK-binding kinase 1 (TBK1) is an important enzyme in the regulation of cellular antiviral effects. TBK1 regulates the activity of the interferon regulatory factors IRF3 and IRF7, thereby playing a key role in type I interferon (IFN) signaling pathways. The structure of TBK1 consists of an N-terminal kinase domain, a middle ubiquitin-like domain (ULD), and a C-terminal elongated helical domain. It has been reported that the ULD of TBK1 regulates kinase activity, playing an important role in signaling and mediating interactions with other molecules in the IFN pathway. In this study, we present the crystal structure of the ULD of human TBK1 and identify several conserved residues by multiple sequence alignment. We found that a hydrophobic patch in TBK1, containing residues Leu316, Ile353, and Val382, corresponding to the "Ile44 hydrophobic patch" observed in ubiquitin, was conserved in TBK1, IκB kinase epsilon (IKKɛ/IKKi), IκB kinase alpha (IKKα), and IκB kinase beta (IKKβ). In comparison with the structure of the IKKβ ULD domain of Xenopus laevis, we speculate that the Ile44 hydrophobic patch of TBK1 is present in an intramolecular binding surface between ULD and the C-terminal elongated helices. The varying surface charge distributions in the ULD domains of IKK and IKK-related kinases may be relevant to their specificity for specific partners.
Indexed as
Identifiers
What OpenQuestion holds
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.