Evidence map›Paper›PMID 28148298›Full record

ReviewMolecular brain2017

TBK1: a new player in ALS linking autophagy and neuroinflammation.

James A Oakes, Maria C Davies, Mark O Collins

Open access · goldAbstract readReview
In one paragraph

Review in Molecular brain, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 188 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
188citing papers in PubMed, 3 pooled it
19.5field-weighted citation impact, top 1% 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

188 citing papers in PubMed, 3 syntheses or guidelines pooled it, 317 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Cell-based therapies for amyotrophic lateral sclerosis/motor neuron disease.The Cochrane database of systematic reviews · 2019
    Pooled it
  4. Article
  5. Review
  6. LINE-1 Retrotransposons and Amyotrophic Lateral Sclerosis.International journal of molecular sciences · 2026
    Review
  7. Review
  8. Review
  9. Review
  10. TBK1-NQO1 negative feedback loop regulates antiviral innate immunity.Cell communication and signaling : CCS · 2026
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

128 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

3 authors at 1 institution in 1 country.

James A OakesSchool of Medicine, University of Sheffield, Sheffield, UK.
Maria C DaviesDepartment of Biomedical Science, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.
Mark O CollinsDepartment of Biomedical Science, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK. mark.collins@sheffield.ac.uk.ORCID 0000-0002-7656-4975
University of Sheffield · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) is an adult-onset neurodegenerative disorder affecting motor neurons, resulting in progressive muscle weakness and death by respiratory failure. Protein and RNA aggregates are a hallmark of ALS pathology and are thought to contribute to ALS by impairing axonal transport. Mutations in several genes known to contribute to ALS result in deposition of their protein products as aggregates; these include TARDBP, C9ORF72, and SOD1. In motor neurons, this can disrupt transport of mitochondria to areas of metabolic need, resulting in damage to cells and can elicit a neuroinflammatory response leading to further neuronal damage. Recently, eight independent human genetics studies have uncovered a link between TANK-binding kinase 1 (TBK1) mutations and ALS. TBK1 belongs to the IKK-kinase family of kinases that are involved in innate immunity signaling pathways; specifically, TBK1 is an inducer of type-1 interferons. TBK1 also has a major role in autophagy and mitophagy, chiefly the phosphorylation of autophagy adaptors. Several other ALS genes are also involved in autophagy, including p62 and OPTN. TBK1 is required for efficient cargo recruitment in autophagy; mutations in TBK1 may result in impaired autophagy and contribute to the accumulation of protein aggregates and ALS pathology. In this review, we focus on the role of TBK1 in autophagy and the contributions of this process to the pathophysiology of ALS.

Indexed as

AutophagyAmyotrophic Lateral SclerosisAnimalsHumansInflammationModels, BiologicalNervous SystemProtein Serine-Threonine KinasesProtein Serine-Threonine KinasesALSAmyotrophic lateral sclerosisAutophagyFrontotemporal dementiaFTDMitophagyMotor neuron diseaseNeuroinflammationSignalingTBK1

Identifiers

PMID28148298
PMCPMC5288885
OpenAlexW2585432400

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.