Evidence map›Paper›PMID 21928149›Full record

ReviewGlycoconjugate journal2011

Where catabolism meets signalling: neuraminidase 1 as a modulator of cell receptors.

Alexey V Pshezhetsky, Aleksander Hinek

Abstract readReview
PubMed Publisher
In one paragraph

Review in Glycoconjugate journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 84 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Sialidase Inhibitors with Different Mechanisms.Journal of medicinal chemistry · 2022
    Review
  12. Review
  13. The Janus-like role of neuraminidase isoenzymes in inflammation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

2 authors at 2 institutions in 2 countries.

Alexey V PshezhetskyDepartment of Medical Genetics, CHU Sainte-Justine Research Center, 3175 Côte Ste-Catherine, Montreal, (Qc), H3T 1C5, Canada. alexei.pchejetski@umontreal.ca
Aleksander Hinek
Hospital for Sick Children · CAHTC (Taiwan) · TW

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Terminal sialic acid residues are found in abundance in glycan chains of glycoproteins and glycolipids on the surface of all live cells forming an outer layer of the cell originally known as glycocalyx. Their presence affects the molecular properties and structure of glycoconjugates, modifying their function and interactions with other molecules. Consequently, the sialylation state of glycoproteins and glycolipids has been recognized as a critical factor modulating molecular recognitions inside the cell, between the cells, between the cells and the extracellular matrix, and between the cells and certain exogenous pathogens. Sialyltransferases that attach sialic acid residues to the glycan chains in the process of their initial synthesis were thought to be mainly responsible for the creation and maintenance of a temporal and spatial diversity of sialylated moieties. However, the growing evidence also suggests that in mammalian cells, at least equally important roles belong to sialidases/neuraminidases, which are located on the cell surface and in intracellular compartments, and may either initiate the catabolism of sialoglycoconjugates or just cleave their sialic acid residues, and thereby contribute to temporal changes in their structure and functions. The current review summarizes emerging data demonstrating that neuraminidase 1 (NEU1), well known for its lysosomal catabolic function, can be also targeted to the cell surface and assume the previously unrecognized role as a structural and functional modulator of cellular receptors.

Indexed as

ImmunityAnimalsB-LymphocytesCell MembraneGlycocalyxGlycoconjugatesGlycolipidsGlycoproteinsHumansLysosomesMammalsMiceMyocytes, Smooth MuscleN-Acetylneuraminic AcidNeuraminidasePhagocytosisGlycoconjugatesGlycolipidsGlycoproteinsN-Acetylneuraminic AcidNEU1 protein, humanNeu1 protein, mouseNeuraminidaseSialyltransferases

Identifiers

PMID21928149
OpenAlexW2065166241

What OpenQuestion holds

Textmetadata
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.