Evidence map›Paper›PMID 35076453›Full record

ReviewAntibodies (Basel, Switzerland)2022

New Opportunities in Glycan Engineering for Therapeutic Proteins.

Xiaotian Zhong, Aaron M D'Antona, John J Scarcelli, Jason C Rouse

Abstract readReview
In one paragraph

Review in Antibodies (Basel, Switzerland), 2022. 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
–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

11 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Introduction of Carbonyl Groups into Antibodies.Molecules (Basel, Switzerland) · 2023
    Review
  10. Article
  11. Impact of N-Linked Glycosylation on Therapeutic Proteins.Molecules (Basel, Switzerland) · 2022
    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

4 authors.

Xiaotian ZhongBioMedicine Design, Medicinal Sciences, Pfizer Worldwide R&D, 610 Main Street, Cambridge, MA 02139, USA.
Aaron M D'AntonaBioMedicine Design, Medicinal Sciences, Pfizer Worldwide R&D, 610 Main Street, Cambridge, MA 02139, USA.
John J ScarcelliBioProcess R&D, Biotherapeutics Pharmaceutical Sciences, Medicinal Sciences, Pfizer Worldwide R&D, 1 Burtt Road, Andover, MA 01810, USA.
Jason C RouseAnalytical R&D, Biotherapeutics Pharmaceutical Sciences, Medicinal Sciences, Pfizer Worldwide R&D, 1 Burtt Road, Andover, MA 01810, USA.ORCID 0000-0002-2721-7264

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycans as sugar polymers are important metabolic, structural, and physiological regulators for cellular and biological functions. They are often classified as critical quality attributes to antibodies and recombinant fusion proteins, given their impacts on the efficacy and safety of biologics drugs. Recent reports on the conjugates of N-acetyl-galactosamine and mannose-6-phosphate for lysosomal degradation, Fab glycans for antibody diversification, as well as sialylation therapeutic modulations and O-linked applications, have been fueling the continued interest in glycoengineering. The current advancements of the human glycome and the development of a comprehensive network in glycosylation pathways have presented new opportunities in designing next-generation therapeutic proteins.

Indexed as

antibody diversificationFab glycansglycomeglycosylation pathwayslysosomal degradationmannose-6-phosphateN-acetyl-galactosamineO-linked glycanssialylationtherapeutic proteins

Identifiers

PMID35076453
PMCPMC8788452

What OpenQuestion holds

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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.