ArticleBioengineered2015
Enhanced expression of heterologous proteins in yeast cells via the modification of N-glycosylation sites.
Article in Bioengineered, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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.
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.
Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- Recombinant collagen in regenerative medicine: Expression strategies, structural design, and translational applications.Materials today. Bio · 2025Review
- The MFα signal sequence in yeast-based protein secretion: challenges and innovations'.Applied microbiology and biotechnology · 2025Review
- Modifying Naturally Occurring, Nonmammalian-Sourced Biopolymers for Biomedical Applications.ACS biomaterials science & engineering · 2024Review
- A new Bowman-Birk type protease inhibitor regulated by MeJA pathway in maize exhibits anti-feedant activity against the Ostrinia furnacalis.Plant molecular biology · 2024Article
- The introduction of an N-glycosylation site into prochymosin greatly enhances its production and secretion by Pichia pastoris.Microbial cell factories · 2022Article
- Improved methanol tolerance of Rhizomucor miehei lipase based on N‑glycosylation within the α-helix region and its application in biodiesel production.Biotechnology for biofuels · 2021Article
- Platforms for Production of Protein-Based Vaccines: From Classical to Next-Generation Strategies.Biomolecules · 2021Review
- Protein Engineering Approaches to Enhance Fungal Laccase Production inInternational journal of molecular sciences · 2021Article
- Edible Vaccines: Promises and Challenges.Molecular biotechnology · 2020Review
- Yeast Expression Systems: Overview and Recent Advances.Molecular biotechnology · 2019Review
- Alternative Methods of Vaccine Delivery: An Overview of Edible and Intradermal Vaccines.Journal of immunology research · 2019Review
- The Goldilocks Approach: A Review of Employing Design of Experiments in Prokaryotic Recombinant Protein Production.Bioengineering (Basel, Switzerland) · 2018Review
- Fusion of a highly N-glycosylated polypeptide increases the expression of ER-localized proteins in plants.Scientific reports · 2018Article
- Protein profile in Aspergillus nidulans recombinant strains overproducing heterologous enzymes.Microbial biotechnology · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Yeasts are widely used for the production of heterologous proteins. Improving the expression of such proteins is a top priority for pharmaceutical and industrial applications. N-Glycosylation, a common form of protein modification in yeasts, facilitates proper protein folding and secretion. Accordingly, our previous study revealed that the attachment of additional N-glycans to recombinant elastase by introducing an N-glycosylation sequon at suitable locations could stimulate its expression. Interestingly, the sequon Asn-Xaa-Thr is N-glycosylated more efficiently than Asn-Xaa-Ser, so improving the N-glycosylation efficiency via the conversion of Ser to Thr in the sequon would enhance the efficiency of N-glycosylation and increase glycoprotein expression. Recently, the expression level of recombinant elastase was enhanced by this means in our lab. Actually, the modification of N-glycosylation sites can generally be achieved through site-directed mutagenesis; thus, the method described in this report represents a feasible means of improving heterologous protein expression in yeasts.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.