Evidence map›Paper›PMID 34842612›Full record

ReviewAntibodies (Basel, Switzerland)2021

Glycoengineering of Therapeutic Antibodies with Small Molecule Inhibitors.

Shasha Li, Alex J McCraw, Richard A Gardner, Daniel I R Spencer, Sophia N Karagiannis, Gerd K Wagner

Open access · goldAbstract readReview
In one paragraph

Review in Antibodies (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Review
  3. Antibody glycosylation in neuroimmune diseases.Journal of translational medicine · 2025
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
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  11. Article
  12. Review
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  14. Article
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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.

Shasha LiMedical Biology Centre, School of Pharmacy, Queen's University Belfast, 97 Lisburn Road, Belfast BT9 7BL, UK.
Alex J McCrawSt. John's Institute of Dermatology, School of Basic & Medical Biosciences, King's College London, 9th Floor Tower Wing, Guy's Hospital, London SE1 9RT, UK.
Richard A GardnerLudger, Ltd., Culham Science Centre, Abingdon, Oxfordshire OX14 3EB, UK.
Daniel I R SpencerLudger, Ltd., Culham Science Centre, Abingdon, Oxfordshire OX14 3EB, UK.
Sophia N KaragiannisSt. John's Institute of Dermatology, School of Basic & Medical Biosciences, King's College London, 9th Floor Tower Wing, Guy's Hospital, London SE1 9RT, UK.ORCID 0000-0002-4100-7810
Gerd K WagnerMedical Biology Centre, School of Pharmacy, Queen's University Belfast, 97 Lisburn Road, Belfast BT9 7BL, UK.
Culham Science Centre · GBGuy's Hospital · GBQueen's University Belfast · GB

Funding

Breast Cancer Now 147; KCL-BCN-Q3Cancer Research UK C30122/A11527Cancer Research UK C30122/A15774Cancer Research UK C604/A25135Guy's and St Thomas' Foundation Trust Charity Melanoma Special Fund SPF573Medical Research Council MR/L023091/1National Institute for Health Research Biomedical Research Centre IS-BRC-1215-20006NIHR CRUK Experimental Cancer Medicine Centre C10355/A15587
6 · The paper itself

Abstract

Monoclonal antibodies (mAbs) are one of the cornerstones of modern medicine, across an increasing range of therapeutic areas. All therapeutic mAbs are glycoproteins, i.e., their polypeptide chain is decorated with glycans, oligosaccharides of extraordinary structural diversity. The presence, absence, and composition of these glycans can have a profound effect on the pharmacodynamic and pharmacokinetic profile of individual mAbs. Approaches for the glycoengineering of therapeutic mAbs-the manipulation and optimisation of mAb glycan structures-are therefore of great interest from a technological, therapeutic, and regulatory perspective. In this review, we provide a brief introduction to the effects of glycosylation on the biological and pharmacological functions of the five classes of immunoglobulins (IgG, IgE, IgA, IgM and IgD) that form the backbone of all current clinical and experimental mAbs, including an overview of common mAb expression systems. We review selected examples for the use of small molecule inhibitors of glycan biosynthesis for mAb glycoengineering, we discuss the potential advantages and challenges of this approach, and we outline potential future applications. The main aim of the review is to showcase the expanding chemical toolbox that is becoming available for mAb glycoengineering to the biology and biotechnology community.

Indexed as

antibodychemical toolsglycanglycoengineeringglycoformglycosylationimmunoglobulininhibitor

Identifiers

PMID34842612
PMCPMC8628514
OpenAlexW3210890624

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.