Evidence map›Paper›PMID 33981616›Full record

ArticleEuropean thyroid journal2021

Glycosylation of Anti-Thyroglobulin IgG1 and IgG4 Subclasses in Thyroid Diseases.

Yuan Li, Chenxu Zhao, Keli Zhao, Nan Yu, Yan Li, Yang Yu, Yang Zhang, Zhijing Song, Youyuan Huang, Guizhi Lu and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in European thyroid journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. The role of autophagy in Graves disease: knowns and unknowns.Frontiers in cell and developmental biology · 2024
    Review
  6. Review
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  9. Review
  10. CD11cFrontiers in immunology · 2022
    Article
  11. 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

13 authors at 4 institutions in 1 country.

Yuan LiDepartment of Endocrinology, Peking University First Hospital, Beijing, China.
Chenxu ZhaoDepartment of Endocrinology, Peking University First Hospital, Beijing, China.
Keli ZhaoInstitute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Nan YuDepartment of Endocrinology, Peking University First Hospital, Beijing, China.
Yan LiInstitute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Yang YuDepartment of Endocrinology, Peking University First Hospital, Beijing, China.
Yang ZhangDepartment of Endocrinology, Peking University First Hospital, Beijing, China.
Zhijing SongInstitute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Youyuan HuangDepartment of Endocrinology, Peking University First Hospital, Beijing, China.
Guizhi LuDepartment of Endocrinology, Peking University First Hospital, Beijing, China.
Ying GaoDepartment of Endocrinology, Peking University First Hospital, Beijing, China.
Junqing ZhangDepartment of Endocrinology, Peking University First Hospital, Beijing, China.
Xiaohui GuoDepartment of Endocrinology, Peking University First Hospital, Beijing, China.
Peking University First Hospital · CNUniversity of Chinese Academy of Sciences · CNHebei Medical University · CNPeking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveThyroglobulin antibodies (TgAb), principally comprising immunoglobulin G (IgG), are frequently found in healthy individuals. Previously, we showed that the glycosylation levels of TgAb IgG differed across various thyroid diseases, suggesting an important role of glycosylation on antibodies in the pathogenesis of thyroid diseases. Since IgG1 and IgG4 are the primary TgAb IgG subclasses, this study aimed to investigate the glycosylation of TgAb IgG1 and IgG4 subclasses in thyroid diseases.

methodsTgAb IgG was purified by affinity chromatography from the serum of patients with Hashimoto's thyroiditis (HT) (

resultsSignificantly elevated mannose, sialic acid, and galactose levels on TgAb IgG1 were found in HT and PTC patients compared to GD patients and healthy controls (all

conclusionOur study describes different distributions of TgAb IgG1 glycosylation in various thyroid diseases. The aberrantly increased glycosylation levels of TgAb IgG1 observed in HT, PTC, and PTC-T might be indicative of immune disorders and participate in the pathogenesis of these diseases.

Indexed as

GlycosylationIgG subclassesThyroglobulin antibodyThyroid diseases

Identifiers

PMID33981616
PMCPMC8077608
OpenAlexW3082403020

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.