Evidence map›Paper›PMID 31724708›Full record

ReviewBrain : a journal of neurology2020

Disrupted glycosylation of lipids and proteins is a cause of neurodegeneration.

Tobias Moll, Pamela J Shaw, Johnathan Cooper-Knock

Abstract readReview
In one paragraph

Review in Brain : a journal of neurology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. Article
  2. Combination Pharmacology for ALS: A Mechanistic Rationale.International journal of molecular sciences · 2026
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. AUGMENTED DOUBLY ROBUST POST-IMPUTATION INFERENCE FOR PROTEOMIC DATA.bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. A GMR enzymatic assay for quantifying nuclease and peptidase activity.Frontiers in bioengineering and biotechnology · 2024
    Article
  14. Review
  15. Article
  16. Article
  17. Golgi-IP, a tool for multimodal analysis of Golgi molecular content.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Review
  19. Immunomodulatory role of glycoRNAs in the brain.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2023
    Review
  20. Intergenic Interactions ofLife (Basel, Switzerland) · 2023
    Article
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.

Tobias MollSheffield Institute for Translational Neuroscience (SITraN), Sheffield, UK.
Pamela J ShawSheffield Institute for Translational Neuroscience (SITraN), Sheffield, UK.
Johnathan Cooper-KnockSheffield Institute for Translational Neuroscience (SITraN), Sheffield, UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosyltransferases represent a large family of enzymes that catalyse the biosynthesis of oligosaccharides, polysaccharides, and glycoconjugates. A number of studies have implicated glycosyltransferases in the pathogenesis of neurodegenerative diseases but differentiating cause from effect has been difficult. We have recently discovered that mutations proximal to the substrate binding site of glycosyltransferase 8 domain containing 1 (GLT8D1) are associated with familial amyotrophic lateral sclerosis (ALS). We demonstrated that ALS-associated mutations reduce activity of the enzyme suggesting a loss-of-function mechanism that is an attractive therapeutic target. Our work is the first evidence that isolated dysfunction of a glycosyltransferase is sufficient to cause a neurodegenerative disease, but connection between neurodegeneration and genetic variation within glycosyltransferases is not new. Previous studies have identified associations between mutations in UGT8 and sporadic ALS, and between ST6GAL1 mutations and conversion of mild cognitive impairment into clinical Alzheimer's disease. In this review we consider potential mechanisms connecting glycosyltransferase dysfunction to neurodegeneration. The most prominent candidates are ganglioside synthesis and impaired addition of O-linked β-N-acetylglucosamine (O-GlcNAc) groups to proteins important for axonal and synaptic function. Special consideration is given to examples where genetic mutations within glycosyltransferases are associated with neurodegeneration in recognition of the fact that these changes are likely to be upstream causes present from birth.

Indexed as

AnimalsGlycosylationGlycosyltransferasesHumansLipid MetabolismLipidsMutationNerve DegenerationProteinsGlycosyltransferasesLipidsProteinsgangliosidesglycosyltransferaseneurodegenerationO-linked β-N-acetylglucosamine

Identifiers

PMID31724708
PMCPMC7241952

What OpenQuestion holds

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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.