Evidence map›Paper›PMID 23453972›Full record

ArticleCell reports2013

Structure and ubiquitination-dependent activation of TANK-binding kinase 1.

Daqi Tu, Zehua Zhu, Alicia Y Zhou, Cai-hong Yun, Kyung-Eun Lee, Angela V Toms, Yiqun Li, Gavin P Dunn, Edmond Chan, Tran Thai and 7 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed, 1 pooled it
7.5field-weighted citation impact, top 2% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

131 citing papers in PubMed, 1 synthesis or guideline pooled it, 208 citations in OpenAlex.

  1. Pooled it
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  6. Role of autophagy in antiviral innate immunity.Cellular & molecular biology letters · 2026
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  12. PtdIns(3,5)PbioRxiv : the preprint server for biology · 2025
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71 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

17 authors at 4 institutions in 2 countries.

Daqi TuDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA.
Zehua Zhu
Alicia Y Zhou
Cai-hong Yun
Kyung-Eun Lee
Angela V Toms
Yiqun Li
Gavin P Dunn
Edmond Chan
Tran Thai
Shenghong Yang
Scott B Ficarro
Jarrod A Marto
Hyesung Jeon
William C Hahn
David A Barbie
Michael J Eck
Dana-Farber Cancer Institute · USBroad Institute · USHarvard University · USKorea Institute of Science and Technology · KR

Funding

The RAS and P13K Pathways in Pancreatic AdenocarcinomaP01CA117969 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI DEPINHO, RONALD ANTHONY · 2006 to 2025
$41.7M
StructureP01CA154303 · NCI · DANA-FARBER CANCER INST · PI JANNE, PASI A · 2012 to 2021
$17.8M
Regulation and function of IKKe in breast cancer initiation and maintenanceR01CA130988 · NCI · DANA-FARBER CANCER INST · PI HAHN, WILLIAM C. · 2009 to 2018
$3.5M
Structural Biology of Formin ProteinsR01GM071834 · NIGMS · DANA-FARBER CANCER INSTITUTE · PI ECK, MICHAEL J · 2004 to 2013
$3.1M
Structural biology of kinase signaling in T-cellsR01CA080942 · NCI · DANA-FARBER CANCER INSTITUTE · PI ECK, MICHAEL J · 1999 to 2010
$2.3M
Synthetic-Lethal-Based Targeted Therapy for Oncogenic KRAS-Driven CancerK08CA138918 · NCI · DANA-FARBER CANCER INST · PI BARBIE, DAVID A · 2010 to 2014
$891k
New Models of Human CancerK01CA094223 · NCI · DANA-FARBER CANCER INSTITUTE · PI HAHN, WILLIAM C · 2001 to 2005
$765k
NCI NIH HHS K01 CA094223NCI NIH HHS K08 CA138918NCI NIH HHS K08 CA138918-01A1NCI NIH HHS P01 CA117969NCI NIH HHS P01 CA154303NCI NIH HHS R01 CA080942NCI NIH HHS R01 CA130988NIGMS NIH HHS R01 GM071834
6 · The paper itself

Abstract

Upon stimulation by pathogen-associated inflammatory signals, TANK-binding kinase 1 (TBK1) induces type I interferon expression and modulates nuclear factor κB (NF-κB) signaling. Here, we describe the 2.4 Å-resolution crystal structure of nearly full-length TBK1 in complex with specific inhibitors. The structure reveals a dimeric assembly created by an extensive network of interactions among the kinase, ubiquitin-like, and scaffold/dimerization domains. An intact TBK1 dimer undergoes K63-linked polyubiquitination on lysines 30 and 401, and these modifications are required for TBK1 activity. The ubiquitination sites and dimer contacts are conserved in the close homolog inhibitor of κB kinase ε (IKKε) but not in IKKβ, a canonical IKK that assembles in an unrelated manner. The multidomain architecture of TBK1 provides a structural platform for integrating ubiquitination with kinase activation and IRF3 phosphorylation. The structure of TBK1 will facilitate studies of the atypical IKKs in normal and disease physiology and further the development of more specific inhibitors that may be useful as anticancer or anti-inflammatory agents.

Indexed as

Molecular Docking SimulationMolecular Dynamics SimulationUbiquitinationAmino Acid SequenceBinding SitesCrystallography, X-RayHumansI-kappa B KinaseInterferon Regulatory Factor-3Molecular Sequence DataProtein BindingProtein MultimerizationProtein Serine-Threonine KinasesProtein Structure, TertiaryI-kappa B KinaseInterferon Regulatory Factor-3Protein Serine-Threonine KinasesTBK1 protein, human

Identifiers

PMID23453972
PMCPMC3863638
OpenAlexW2085598239

What OpenQuestion holds

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LicenceTDM
Read underepoch 390

Registered trials

None linked

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.