ArticleSmall (Weinheim an der Bergstrasse, Germany)2025
Mammalian Cell Surface Display for High-Throughput Protein Engineering of Glycosyltransferases.
Article in Small (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Advancements and applications of click chemistry in protein labeling and bioconjugation.RSC advances · 2026Review
- Editor's Choice Protein engineering strategies to develop lectins by design.Glycobiology · 2025Review
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.
Funding
Abstract
High-throughput methods are needed to study structure-function relationships of mammalian glycosyltransferases due to their essential role in assembling the glycocalyx. Mutations in these enzymes result in Congenital Disorders of Glycosylation, and improvements of enzyme properties can yield new biocatalysts. In this manuscript, a cell-based glycosyltransferase activity assay is developed using mammalian surface display. It is demonstrated that coupling this approach with click chemistry enables rapid quantification of glycosyltransferase activity. Screening of 1680 different pig ST3Gal1 mutants yielded α(2,3)sialyltransferases with improved enzymatic properties. Using endogenous cell-surface substrates, the method is extended to other human sialyltransferases, including ST6Gal1, ST3Gal4, and ST6GalNAc2. Additionally, the approach is used to screen putative sialyltransferases from diverse organisms not characterized in the CAZy (Carbohydrate-Active EnZymes) database. Overall, a facile, robust, high-throughput, low-cost method is presented to study glycosyltransferase structure-function relationships.
Indexed as
Identifiers
What Socratic 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 Socratic graph.