Evidence map›Paper›PMID 41191168›Full record

ArticleNeuromolecular medicine2025

Glutamic Acid at Position 168 Is a Constitutive Activator of Tank Binding Kinase 1 Catalytic Function.

Noopur Bhore, Anubhuti Sarkar, Zhi Yao, Susanne Herbst, Patrick A Lewis

Abstract read
In one paragraph

Article in Neuromolecular medicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Noopur Bhore *Department of Comparative Biosciences, Royal Veterinary College, London, UK.
Anubhuti Sarkar *Department of Comparative Biosciences, Royal Veterinary College, London, UK.
Zhi YaoLifeArc, Stevenage, UK.
Susanne HerbstDepartment of Comparative Biosciences, Royal Veterinary College, London, UK. sherbst@rvc.ac.uk.
Patrick A LewisDepartment of Comparative Biosciences, Royal Veterinary College, London, UK. plewis@rvc.ac.uk.

Funding

My name'5 doddie foundation MN5DF/CAAu23/100008Royal Society IF\R2\222002
6 · The paper itself

Abstract

TANK binding kinase 1 (TBK1) is serine/threonine protein kinase member of the inhibitor of nuclear factor-kB kinase family, with links to the etiology of familial as well as idiopathic Amyotrophic Lateral Sclerosis. It contributes to several regulatory cellular processes such as autophagy, inflammation and apoptosis. Reduction or loss of TBK1 kinase activity is associated with increased risk of ALS, and so understanding the molecular basis of this activity is an important research priority. In this current study, the role of the E168 residue, located adjacent to the active site of TBK1, has been assessed using a combination of artificial and naturally occurring variants found at this codon - evaluated using multiple readouts for TBK1 kinase activity. The results suggest that the negative charge resulting from the presence of a glutamic acid at this codon is a constitutive activator of TBK1 activity.

Indexed as

Glutamic AcidProtein Serine-Threonine KinasesAmino Acid SubstitutionAmyotrophic Lateral SclerosisBiocatalysisCatalytic DomainCodonEnzyme ActivationHEK293 CellsHumansCodonGlutamic AcidProtein Serine-Threonine KinasesTBK1 protein, humanALSKinaseKinase activityMutationsP62PhosphorylationRAB7TBK1

Identifiers

PMID41191168
PMCPMC12589330

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Registered trials

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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.