Evidence map›Paper›PMID 36557993›Full record

ReviewMolecules (Basel, Switzerland)2022

Impact of N-Linked Glycosylation on Therapeutic Proteins.

Baoquan Chen, Wenqiang Liu, Yaohao Li, Bo Ma, Shiying Shang, Zhongping Tan

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Glycoscience in Advancing PD-1/PD-L1-Axis-Targeted Tumor Immunotherapy.International journal of molecular sciences · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Glycosylation in aging and neurodegenerative diseases.Acta biochimica et biophysica Sinica · 2024
    Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Study on antibody Fc-glycosylation for optimal effector functions.Chemical communications (Cambridge, England) · 2023
    Article
  20. 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.

Baoquan ChenState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China.
Wenqiang LiuState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China.
Yaohao LiState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China.ORCID 0000-0002-4333-9042
Bo MaState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China.
Shiying ShangCenter of Pharmaceutical Technology, School of Pharmaceutical Sciences, Tsinghua University, Beijing 100084, China.
Zhongping TanState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China.

Funding

Glycoengineering of Therapeutic Peptides for Improved Treatment of Human DiseasesR01EB025892 · NIBIB · UNIVERSITY OF COLORADO · PI SAMMAKIA, TAREK · 2018 to 2021
$1.3M
NIBIB NIH HHS R01 EB025892The CAMS Innovation Fund for Medical Sciences CIFMS, 2021-I2M-1-026The National Key R & D Program of China 2018YFE0111400The National Major Scientific and Technological Special Project of China 2018ZX09711001-005 and 2018ZX09711001-013The Training Program of the Major Research Plan of National Natural Science Foundation of China 91853120
6 · The paper itself

Abstract

Therapeutic proteins have unique advantages over small-molecule drugs in the treatment of various diseases, such as higher target specificity, stronger pharmacological efficacy and relatively low side effects. These advantages make them increasingly valued in drug development and clinical practice. However, although highly valued, the intrinsic limitations in their physical, chemical and pharmacological properties often restrict their wider applications. As one of the most important post-translational modifications, glycosylation has been shown to exert positive effects on many properties of proteins, including molecular stability, and pharmacodynamic and pharmacokinetic characteristics. Glycoengineering, which involves changing the glycosylation patterns of proteins, is therefore expected to be an effective means of overcoming the problems of therapeutic proteins. In this review, we summarize recent efforts and advances in the glycoengineering of erythropoietin and IgG monoclonal antibodies, with the goals of illustrating the importance of this strategy in improving the performance of therapeutic proteins and providing a brief overview of how glycoengineering is applied to protein-based drugs.

Indexed as

Antibodies, MonoclonalProtein EngineeringGlycosylationImmunoglobulin GPolysaccharidesProtein Processing, Post-TranslationalAntibodies, MonoclonalImmunoglobulin GPolysaccharideserythropoietinglycosylationmonoclonal antibodiesproteins

Identifiers

PMID36557993
PMCPMC9781892

What OpenQuestion holds

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Registered trials

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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.