Evidence map›Paper›PMID 30397726›Full record

ArticleAdvances in biochemical engineering/biotechnology2021

Engineering of Yeast Glycoprotein Expression.

Charlot De Wachter, Linde Van Landuyt, Nico Callewaert

Abstract read
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In one paragraph

Article 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 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
6.4field-weighted citation impact, top 3% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.

  1. Pooled it
  2. Metabolic engineering ofApplied and environmental microbiology · 2026
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  8. Article
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  11. EngineeringEngineering microbiology · 2024
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  12. Microorganisms · 2024
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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

3 authors at 1 institution in 1 country.

Charlot De Wachter *VIB-UGent Center for Medical Biotechnology, Ghent, Belgium.
Linde Van Landuyt *VIB-UGent Center for Medical Biotechnology, Ghent, Belgium.
Nico CallewaertVIB-UGent Center for Medical Biotechnology, Ghent, Belgium. Nico.Callewaert@vib-ugent.be.
VIB-UGent Center for Medical Biotechnology · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yeasts are valuable hosts for recombinant protein production, as these unicellular eukaryotes are easy to handle, grow rapidly to a high cell density on cost-effective defined media, often offer a high space-time yield, and are able to perform posttranslational modifications. However, a key difference between yeasts and mammalian cells involves the type of glycosylation structures, which hampers the use of yeasts for the production of many biopharmaceuticals. Glycosylation is not only important for the folding process of most recombinant proteins; it has a large impact on pharmacokinetics and pharmacodynamics of the therapeutic proteins as well. Yeasts' hypermannosylated glycosyl structures in some cases can evoke immune responses and lead to rapid clearance of the therapeutic protein from the blood. This chapter highlights the efforts made so far regarding the glyco-engineering of N- and O-type glycosylation, removing or reducing yeast-specific glycans. In some cases, this is combined with the introduction of humanized glycosylation pathways. After many years of patient development to overcome remaining challenges, these efforts have now culminated in effective solutions that should allow yeasts to reclaim the primary position in biopharmaceutical manufacturing that they enjoyed in the early days of biotechnology. Graphical Abstract.

Indexed as

GlycoproteinsSaccharomyces cerevisiaeAnimalsGlycosylationHumansPichiaPolysaccharidesProtein EngineeringRecombinant ProteinsGlycoproteinsPolysaccharidesRecombinant ProteinsFungiN-glycosylation engineeringO-glycosylation engineeringPichia pastorisRecombinant protein expressionSaccharomyces cerevisiaeYeast

Identifiers

PMID30397726
OpenAlexW2899791629

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.