Evidence map›Paper›PMID 33907996›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2021

Glycosylation of Therapeutic Proteins: A Critical Quality Attribute.

Arnaud Delobel

Abstract readReview
PubMed Publisher
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
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  5. Review
  6. Article
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  8. Review
  9. Article
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  11. Article
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  14. Glycomimetics and Glycoconjugates in Drug Discovery.Pharmaceuticals (Basel, Switzerland) · 2024
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. CRISPR Technologies in Chinese Hamster Ovary Cell Line Engineering.International journal of molecular sciences · 2023
    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

1 author.

Arnaud DelobelQuality Assistance sa, Technoparc de Thudinie 2, Donstiennes, Belgium. arnaud.delobel@quality-assistance.be.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is a common posttranslational modification of therapeutic proteins. The glycosylation pattern is dependent on many parameters such as the host cell line or the culture conditions. N- and O-linked glycans usually play a great role on the stability, safety, and efficacy of the drug. For this reason, glycosylation is considered as a critical quality attribute of therapeutic glycoproteins, and a thorough characterization should be performed, as well as a systematic control for each batch produced. This chapter gives a short presentation of the structure of glycans commonly found on recombinant therapeutic proteins, and their role on the properties of the drug, in terms of stability, pharmacokinetics, safety, and efficacy. Lastly, the use of mass spectrometry for the analysis of glycoproteins is briefly described.

Indexed as

Protein Processing, Post-TranslationalAnimalsAntibodies, MonoclonalBiological ProductsCarbohydrate ConformationDrug StabilityGlycoproteinsGlycosylationHumansMass SpectrometryProtein ConformationRecombinant ProteinsAntibodies, MonoclonalBiological ProductsGlycoproteinsRecombinant ProteinsCritical quality attributeGlycoproteinGlycosylationImmunogenicityMass spectrometryMonoclonal antibodyPharmacokinetics

Identifiers

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.