Evidence map›Paper›PMID 35479093›Full record

SynthesisFrontiers in immunology2022

Mammalian Neuraminidases in Immune-Mediated Diseases: Mucins and Beyond.

Erik P Lillehoj, Irina G Luzina, Sergei P Atamas

Open access · goldAbstract readSystematic Review
In one paragraph

Synthesis in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. TFEB and MCOLN1 are important forFrontiers in cellular and infection microbiology · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Sialidase Inhibitors with Different Mechanisms.Journal of medicinal chemistry · 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

3 authors at 1 institution in 1 country.

Erik P LillehojDepartment of Pediatrics, University of Maryland School of Medicine, Baltimore, MD, United States.
Irina G LuzinaDepartment of Medicine, University of Maryland School of Medicine, Baltimore, MD, United States.
Sergei P AtamasDepartment of Medicine, University of Maryland School of Medicine, Baltimore, MD, United States.
University of Maryland, Baltimore · US

Funding

MUC1 Biotherapeutics for Pseudomonas aeruginosa InfectionsR21AI144497 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI LILLEHOJ, ERIK P · 2019 to 2020
$425k
NIAID NIH HHS R21 AI144497
6 · The paper itself

Abstract

Mammalian neuraminidases (NEUs), also known as sialidases, are enzymes that cleave off the terminal neuraminic, or sialic, acid resides from the carbohydrate moieties of glycolipids and glycoproteins. A rapidly growing body of literature indicates that in addition to their metabolic functions, NEUs also regulate the activity of their glycoprotein targets. The simple post-translational modification of NEU protein targets-removal of the highly electronegative sialic acid-affects protein folding, alters protein interactions with their ligands, and exposes or covers proteolytic sites. Through such effects, NEUs regulate the downstream processes in which their glycoprotein targets participate. A major target of desialylation by NEUs are mucins (MUCs), and such post-translational modification contributes to regulation of disease processes. In this review, we focus on the regulatory roles of NEU-modified MUCs as coordinators of disease pathogenesis in fibrotic, inflammatory, infectious, and autoimmune diseases. Special attention is placed on the most abundant and best studied NEU1, and its recently discovered important target, mucin-1 (MUC1). The role of the NEU1 - MUC1 axis in disease pathogenesis is discussed, along with regulatory contributions from other MUCs and other pathophysiologically important NEU targets.

Indexed as

Immune System DiseasesMucinsAnimalsGlycoproteinsMammalsN-Acetylneuraminic AcidNeuraminidaseGlycoproteinsMucinsN-Acetylneuraminic AcidNeuraminidaseautoimmunityfibrosisinfectioninflammationpost-translational modificationsialic acidsialidase

Identifiers

PMID35479093
PMCPMC9035539
OpenAlexW4223632065

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.