Evidence map›Paper›PMID 35281276›Full record

ArticleFrontiers in molecular biosciences2022

Inhibitors of Human Neuraminidase Enzymes Block Transmigration

Md Amran Howlader, Tianlin Guo, Christopher W Cairo

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 43% 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

6 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Targeting Neuraminidase 4 Attenuates Kidney Fibrosis in Mice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  3. Article
  4. Neuraminidase inhibition improves endothelial function in diabetic mice.American journal of physiology. Heart and circulatory physiology · 2023
    Article
  5. The extracellular sialidase NEU3 primes neutrophils.Journal of leukocyte biology · 2022
    Article
  6. 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.

Md Amran HowladerDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
Tianlin GuoDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
Christopher W CairoDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
University of Alberta · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell migration to a site of inflammation is an important step of the immune response. This process is coordinated by cytokines, receptors, and the signal processing machinery of the cell. Many cellular receptors are glycosylated, and their activity can be modulated through changes in glycan structure. Furthermore, glycosylation can be critical to the folding and trafficking of receptors. In this work, we investigated the role of native human neuraminidase enzymes (NEU) in transmigration. We used a cultured T cell line (Jurkat) and a transwell assay with fibronectin (FN) coated wells and cytokines (IL-4 and TNF-α) as chemoattractants in the bottom chamber. We observed that NEU1, NEU3, and NEU4 were positive regulators of transmigration using an siRNA knockdown. Furthermore, we found that pharmacological inhibition of these enzymes inhibited transmigration. We conclude that human NEU isoenzymes NEU1, NEU3, and NEU4 can act as positive regulators of transmigration and should be investigated as targets for anti-inflammatory strategies.

Indexed as

cell adhesionchemotaxismigrationneuraminidasesialic acidsialidasetransmigration

Identifiers

PMID35281276
PMCPMC8913934
OpenAlexW4214743442

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.