Evidence map›Paper›PMID 26253764›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

A common glycan structure on immunoglobulin G for enhancement of effector functions.

Chin-Wei Lin, Ming-Hung Tsai, Shiou-Ting Li, Tsung-I Tsai, Kuo-Ching Chu, Ying-Chih Liu, Meng-Yu Lai, Chia-Yu Wu, Yung-Chieh Tseng, Sachin S Shivatare and 17 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
20.0field-weighted citation impact, top 1% 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

108 citing papers in PubMed, 204 citations in OpenAlex.

  1. Article
  2. Article
  3. Glycan Remodeling Technologies for Enhancing Antibody Function.Advances in experimental medicine and biology · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. BisectingACS chemical biology · 2025
    Article
  9. Article
  10. Making Universal Vaccines and Antibodies Through Glycoengineering.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  11. Current Landscape of Therapeutic Cancer Vaccines.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Increased expression of SSEA-4 on TKI-resistant non-small cell lung cancer with EGFR-T790M mutation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Cell-Free Systems for the Production of Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  19. Review
  20. Review

48 more citing papers are in PubMed but not listed here.

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

27 authors at 2 institutions in 1 country.

Chin-Wei LinGenomics Research Center, Academia Sinica, Taipei 115, Taiwan; Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan; Department of Chemistry, National Taiwan University, Taipei 106, Taiwan;
Ming-Hung TsaiCHO Pharma Inc., Taipei 11503, Taiwan;
Shiou-Ting LiGenomics Research Center, Academia Sinica, Taipei 115, Taiwan;
Tsung-I TsaiGenomics Research Center, Academia Sinica, Taipei 115, Taiwan;
Kuo-Ching ChuCHO Pharma Inc., Taipei 11503, Taiwan;
Ying-Chih LiuCHO Pharma Inc., Taipei 11503, Taiwan;
Meng-Yu LaiGenomics Research Center, Academia Sinica, Taipei 115, Taiwan; CHO Pharma Inc., Taipei 11503, Taiwan;
Chia-Yu WuGenomics Research Center, Academia Sinica, Taipei 115, Taiwan;
Yung-Chieh TsengGenomics Research Center, Academia Sinica, Taipei 115, Taiwan; Graduate Institute of Life Sciences, National Defense Medical Center, Taipei 114, Taiwan;
Sachin S ShivatareCHO Pharma Inc., Taipei 11503, Taiwan;
Chia-Hung WangCHO Pharma Inc., Taipei 11503, Taiwan;
Ping ChaoCHO Pharma Inc., Taipei 11503, Taiwan;
Shi-Yun WangCHO Pharma Inc., Taipei 11503, Taiwan;
Hao-Wei ShihCHO Pharma Inc., Taipei 11503, Taiwan;
Yi-Fang ZengCHO Pharma Inc., Taipei 11503, Taiwan;
Tsai-Hong YouCHO Pharma Inc., Taipei 11503, Taiwan;
Jung-Yu LiaoCHO Pharma Inc., Taipei 11503, Taiwan;
Yu-Chen TuCHO Pharma Inc., Taipei 11503, Taiwan;
Yih-Shyan LinCHO Pharma Inc., Taipei 11503, Taiwan;
Hong-Yang ChuangCHO Pharma Inc., Taipei 11503, Taiwan;
Chia-Lin ChenGenomics Research Center, Academia Sinica, Taipei 115, Taiwan; Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan; Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan.
Charng-Sheng TsaiCHO Pharma Inc., Taipei 11503, Taiwan;
Chiu-Chen HuangCHO Pharma Inc., Taipei 11503, Taiwan;
Nan-Horng LinCHO Pharma Inc., Taipei 11503, Taiwan;
Che MaGenomics Research Center, Academia Sinica, Taipei 115, Taiwan;
Chung-Yi WuGenomics Research Center, Academia Sinica, Taipei 115, Taiwan; Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan; chwong@gate.sinica.edu.tw cyiwu@gate.sinica.edu.tw.
Chi-Huey WongGenomics Research Center, Academia Sinica, Taipei 115, Taiwan; Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan; Department of Chemistry, National Taiwan University, Taipei 106, Taiwan; chwong@gate.sinica.edu.tw cyiwu@gate.sinica.edu.tw.
Academia Sinica · TWGenomics Research Center, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibodies have been developed as therapeutic agents for the treatment of cancer, infection, and inflammation. In addition to binding activity toward the target, antibodies also exhibit effector-mediated activities through the interaction of the Fc glycan and the Fc receptors on immune cells. To identify the optimal glycan structures for individual antibodies with desired activity, we have developed an effective method to modify the Fc-glycan structures to a homogeneous glycoform. In this study, it was found that the biantennary N-glycan structure with two terminal alpha-2,6-linked sialic acids is a common and optimized structure for the enhancement of antibody-dependent cell-mediated cytotoxicity, complement-dependent cytotoxicity, and antiinflammatory activities.

Indexed as

Acetylglucosaminealpha-L-FucosidaseAnimalsAntibodies, ViralAntibody-Dependent Cell CytotoxicityBacterial ProteinsBacteroides fragilisCell Line, TumorFemaleHEK293 CellsHumansImmunoglobulin Fc FragmentsImmunoglobulin GLymphoma, B-CellMiceMice, Inbred BALB CAcetylglucosaminealpha-L-FucosidaseAntibodies, ViralBacterial Proteinsendo-N-acetylneuraminidaseFCGR3A protein, humanImmunoglobulin Fc FragmentsImmunoglobulin GNeuraminidasePolysaccharidesReceptors, IgGRituximabSialic AcidsTrastuzumabendoglycosidaseFc glycosylationglycoengineered antibodieshomogeneous antibodiessugar oxazoline

Identifiers

PMID26253764
PMCPMC4553773
OpenAlexW1908224577

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.