Evidence map›Paper›PMID 31509989›Full record

ArticleInternational journal of molecular sciences2019

Altered Cell Surface N-Glycosylation of Resting and Activated T Cells in Systemic Lupus Erythematosus.

Enikő Szabó, Ákos Hornung, Éva Monostori, Márta Bocskai, Ágnes Czibula, László Kovács

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. The diverseFrontiers in immunology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. The Role of B Cell and T Cell Glycosylation in Systemic Lupus Erythematosus.International journal of molecular sciences · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Aberrant sialylation in ovarian cancers.Journal of the Chinese Medical Association : JCMA · 2020
    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

6 authors at 3 institutions in 1 country.

Enikő SzabóInstitute of Genetics, Biological Research Centre of the Hungarian Academy of Sciences 6726 Szeged, Hungary. szabo.eniko@brc.hu.
Ákos HornungDepartment of Rheumatology and Immunology, Faculty of Medicine, University of Szeged, 6725 Szeged, Hungary.
Éva MonostoriInstitute of Genetics, Biological Research Centre of the Hungarian Academy of Sciences 6726 Szeged, Hungary. monosbeni@gmail.com.
Márta BocskaiDepartment of Rheumatology and Immunology, Faculty of Medicine, University of Szeged, 6725 Szeged, Hungary. bocskai.marta@med.u-szeged.hu.
Ágnes CzibulaInstitute of Genetics, Biological Research Centre of the Hungarian Academy of Sciences 6726 Szeged, Hungary. czibula.agnes@brc.hu.
László KovácsDepartment of Rheumatology and Immunology, Faculty of Medicine, University of Szeged, 6725 Szeged, Hungary. kovacs.laszlo@med.u-szeged.hu.
University of Szeged · HUHUN-REN Szegedi Biológiai Kutatóközpont · HUHungarian Academy of Sciences · HU

Funding

GINOP 2.2.1-15-2016-00007
6 · The paper itself

Abstract

Altered cell surface glycosylation in congenital and acquired diseases has been shown to affect cell differentiation and cellular responses to external signals. Hence, it may have an important role in immune regulation; however, T cell surface glycosylation has not been studied in systemic lupus erythematosus (SLE), a prototype of autoimmune diseases. Analysis of the glycosylation of T cells from patients suffering from SLE was performed by lectin-binding assay, flow cytometry, and quantitative real-time PCR. The results showed that resting SLE T cells presented an activated-like phenotype in terms of their glycosylation pattern. Additionally, activated SLE T cells bound significantly less galectin-1 (Gal-1), an important immunoregulatory lectin, while other lectins bound similarly to the controls. Differential lectin binding, specifically Gal-1, to SLE T cells was explained by the increased gene expression ratio of sialyltransferases and neuraminidase 1 (

Indexed as

Lymphocyte ActivationAdultAntigens, CDbeta-D-Galactoside alpha 2-6-SialyltransferaseFemaleGalectin 1Gene ExpressionGlycosylationHumansLectinsLupus Erythematosus, SystemicMaleMiddle AgedNeuraminidaseSialyltransferasesSurface PropertiesAntigens, CDbeta-D-Galactoside alpha 2-6-SialyltransferaseGalectin 1LectinsNeuraminidaseSialyltransferasesST6GAL1 protein, humangalectin 1glycosylationglycosylation enzymeslectin bindingsialylationsystemic lupus erythematosusT cells

Identifiers

PMID31509989
PMCPMC6770513
OpenAlexW2972966730

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.