N-Glycan Insertion for Probing Protein-Protein Interactions and Epitope Mapping.

Shayma Abukar, Xiaohan Zhang, Bertina Dragūnaitė, Gwladys Chabrier, Rens de Groot

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.8field-weighted citation impact, top 21% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

Construction of anFrontiers in bioengineering and biotechnology · 2024
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

5 authors at 1 institution in 1 country.

Shayma AbukarInstitute of Cardiovascular Science, University College London, London, UK.

Xiaohan ZhangInstitute of Cardiovascular Science, University College London, London, UK.

Bertina DragūnaitėInstitute of Cardiovascular Science, University College London, London, UK.

Gwladys ChabrierInstitute of Cardiovascular Science, University College London, London, UK.

Rens de GrootInstitute of Cardiovascular Science, University College London, London, UK. r.degroot@ucl.ac.uk.

University College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Introducing an N-linked glycosylation motif into recombinant proteins at specific sites is a useful tool in probing protein-protein interactions and epitope mapping. Due to their large size, a new N-glycan can block protein-protein interactions if it is introduced by site-directed mutagenesis on the same face as a ligand or antibody binding site. Recombinant mutant proteins containing these engineered glycans can then be studied using binding or functional assays to establish if the new glycan causes steric hindrance, prevents an important protein-protein interaction, or blocks (auto)antibody binding. In this book chapter, we provide guides and protocols for inserting engineered glycans, including how to use AlphaFold models to choose amino acid residues on the surface of protein domains that are suitable for mutagenesis into N-linked glycosylation motifs as well as protocols for site-directed mutagenesis and recombinant protein expression of the N-glycan variants.

Indexed as

PolysaccharidesProtein Processing, Post-TranslationalEpitope MappingGlycosylationRecombinant ProteinsPolysaccharidesRecombinant ProteinsEngineered glycansGlycan insertionGlycan mutantsLigand binding sitesSite-directed mutagenesis

Identifiers

PMID38038930

DOI10.1038/s41592-022-01488-1

OpenAlexW4389244707

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.