Evidence map›Paper›PMID 29071407›Full record

ReviewAdvances in biochemical engineering/biotechnology2021

Recombinant Proteins and Monoclonal Antibodies.

Roy Jefferis

Abstract readReview
PubMed Publisher
In one paragraph

Review in Advances in biochemical engineering/biotechnology, 2021. 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
2.9field-weighted citation impact, top 8% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Core fucosylation and its roles in gastrointestinal glycoimmunology.World journal of gastrointestinal oncology · 2023
    Review
  8. The Role of Clinical Glyco(proteo)mics in Precision Medicine.Molecular & cellular proteomics : MCP · 2023
    Article
  9. Cell-freeFrontiers in molecular biosciences · 2023
    Article
  10. Glycobiology of rheumatic diseases.Nature reviews. Rheumatology · 2023
    Review
  11. Article
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 at 1 institution in 1 country.

Roy JefferisInstitute of Immunology and Immunotherapy, College of Medical and Dental Sciences, University of Birmingham, Birmingham, B15 2TT, UK. R.Jefferis@bham.ac.uk.
University of Birmingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human genome has become a subject of public interest, whilst the proteome remains the province of specialists. Less appreciated is the human glycoprotein (GP) repertoire (proteoglycome!); however, some 50% of open reading frame genes encode for proteins (P) that may accept the addition of N-linked and/or O-linked sugar chains (oligosaccharides). It is established that the attachment of defined oligosaccharide structures impacts mechanisms of action (MoAs), pharmacokinetics, pharmacodynamics, etc., and is a critical quality attribute (CQA) for recombinant GP therapeutics. The oligosaccharide structure attached at a given site may exhibit structural heterogeneity, and individual structures (glycoforms) may modulate MoAs. The biopharmaceutical industry is challenged, therefore, to produce recombinant GP therapeutics that have structural fidelity to the natural (endogenous) molecule, in non-human cells. Multiple production platforms have been developed that, in addition to the natural glycoform, may produce unnatural glycoforms, including sugar residues that can be immunogenic in human subjects. Following a general introduction to the field, this review discusses glycosylation of recombinant monoclonal antibodies (mAbs), the contribution of glycoforms to MoAs and the development of customised mAb therapeutic glycoforms to optimise MoAs for individual disease indications.

Indexed as

Antibodies, MonoclonalGlycoproteinsGlycosylationOligosaccharidesRecombinant ProteinsAntibodies, MonoclonalGlycoproteinsOligosaccharidesRecombinant ProteinsCritical quality attributesGlycoformsGlycoproteinsIgG subclassesMechanisms of actionOligosaccharidesRecombinant antibody therapeutics

Identifiers

PMID29071407
OpenAlexW2766705223

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.