Evidence map›Paper›PMID 30088207›Full record

ReviewGlycoconjugate journal2018

Keeping it trim: roles of neuraminidases in CNS function.

Alexey V Pshezhetsky, Mila Ashmarina

Open access · hybridAbstract readReview
In one paragraph

Review in Glycoconjugate journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

37 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Sialylation in the nervous system: Functions and mechanisms.The Journal of biological chemistry · 2026
    Review
  6. Sialidase Activity Imaging of Different Organs with BTP3-Neu5Ac.Advances in experimental medicine and biology · 2026
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Journal of advanced veterinary and animal research · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Inhibitors of the Sialidase NEU3 as Potential Therapeutics for Fibrosis.International journal of molecular sciences · 2022
    Review
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

2 authors at 1 institution in 1 country.

Alexey V PshezhetskySainte-Justine Hospital Research Center, Department of Paediatrics, University of Montreal, CHU Ste-Justine, Centre de recherche, 3175 Côte-Sainte-Catherine, Montréal, Québec, H3T 1C5, Canada. alexei.pchejetski@umontreal.ca.ORCID http://orcid.org/0000-0002-6612-1062
Mila AshmarinaSainte-Justine Hospital Research Center, Department of Paediatrics, University of Montreal, CHU Ste-Justine, Centre de recherche, 3175 Côte-Sainte-Catherine, Montréal, Québec, H3T 1C5, Canada.
Centre Hospitalier Universitaire Sainte-Justine · CA

Funding

Canadian Glycomics Network G2CIHR 148863CIHR 156345Institute of Genetics 148863Institute of Genetics 156345
6 · The paper itself

Abstract

The sialylated glyconjugates (SGC) are found in abundance on the surface of brain cells, where they form a dense array of glycans mediating cell/cell and cell/protein recognition in numerous physiological and pathological processes. Metabolic genetic blocks in processing and catabolism of SGC result in development of severe storage disorders, dominated by CNS involvement including marked neuroinflammation and neurodegeneration, the pathophysiological mechanisms of which are still discussed. SGC patterns in the brain are cell and organelle-specific, dynamic and maintained by highly coordinated processes of their biosynthesis, trafficking, processing and catabolism. The changes in the composition of SGC during development and aging of the brain cannot be explained based solely on the regulation of the SGC-synthesizing enzymes, sialyltransferases, suggesting that neuraminidases (sialidases) hydrolysing the removal of terminal sialic acid residues also play an essential role. In the current review we summarize the roles of three mammalian neuraminidases: neuraminidase 1, neuraminidase 3 and neuraminidase 4 in processing brain SGC. Emerging data demonstrate that these enzymes with different, yet overlapping expression patterns, intracellular localization and substrate specificity play essential roles in the physiology of the CNS.

Indexed as

AnimalsBrainGlycoconjugatesHumansNeuraminidaseNeurodegenerative DiseasesGlycoconjugatesNeuraminidaseCNSGangliosideLysosomeNeuraminidasePolysialic acidSialic acid

Identifiers

PMID30088207
PMCPMC6182584
OpenAlexW2887521924

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.