Evidence map›Paper›PMID 33732900›Full record

ArticleBiochemistry and biophysics reports2021

A biotechnological tool for glycoprotein desialylation based on immobilized neuraminidase from

Lucía Bidondo, Mercedes Landeira, Florencia Festari, Teresa Freire, Cecilia Giacomini

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry and biophysics reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 42% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

5 authors at 2 institutions in 1 country.

Lucía BidondoLaboratorio de Bioquímica, Departamento de Biociencias, Facultad de Química, UdelaR, Gral. Flores, 2124, Montevideo, Uruguay.
Mercedes LandeiraLaboratorio de Inmunomodulación y desarrollo de Vacunas, Departamento de Inmunobiología, Facultad de Medicina, UdelaR, Gral Flores, 2125, Montevideo, Uruguay.
Florencia FestariLaboratorio de Inmunomodulación y desarrollo de Vacunas, Departamento de Inmunobiología, Facultad de Medicina, UdelaR, Gral Flores, 2125, Montevideo, Uruguay.
Teresa FreireLaboratorio de Inmunomodulación y desarrollo de Vacunas, Departamento de Inmunobiología, Facultad de Medicina, UdelaR, Gral Flores, 2125, Montevideo, Uruguay.
Cecilia GiacominiLaboratorio de Bioquímica, Departamento de Biociencias, Facultad de Química, UdelaR, Gral. Flores, 2124, Montevideo, Uruguay.
Universidad de la República de Uruguay · UYCentro Uruguayo de Imagenología Molecular · UY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundSialic acids are widely distributed in nature and have biological relevance owing to their varied structural and functional roles. Immobilized neuraminidase can selectively remove terminal N-acetyl neuraminic acid from glycoproteins without altering the protein backbone while it can be easily removed from the reaction mixture avoiding sample contamination. This enables the evaluation of changes in glycoprotein performance upon desialylation.

methodsNeuraminidase was immobilized onto agarose activated with cyanate ester groups and further used for desialylation of model glycoproteins, a lysate from tumour cells and tumour cells. Desialylation process was analysed by lectin binding assay, determination of sialyl-Tn or flow cytometry.

results

conclusionsImmobilized neuraminidase is an interesting as well as a robust biotechnological tool for enzymatic desialylation purposes. GENERAL SIGNIFICANCE: Immobilized neuraminidase would contribute to understand the role of sialic acid in biological processes.

Indexed as

4 MU-NANA, 2′-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic acidBCA, Bicinchonninic acidCDAP-BF4, 1-Cyano-4-dimethylaminopyridinium tetrafluoroborateECA, Erythrina cristagalli lectinELISA-type assay, Enzyme-linked Immuno Sorbent assayEnzymatic desialylationFBS, Fetal bovine serumGal, GalactoseGalNAc, N-acetylgalactosamineGlcNAc, N-acetylglucosamineGlycomic analysisImmobilizationNeu5Ac, N-Acetyl neuraminic acidNeura-agarose, Neuraminidase immobilized onto agaroseNeuraminidaseOPD, ortho-PhenylendiamineOSM, Ovine submaxilar mucinPBS, Phosphate saline bufferPE, PhycoerythrinPNA, Arachis hipogaea lectinSialic acidSialyl-Tn antigen, Neu 5 Ac-2,6 GalNAcSNA, Sambucus nigra lectin

Identifiers

PMID33732900
PMCPMC7937660
OpenAlexW3134754285

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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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.