ArticleMethods in enzymology2023
DeGlyPHER: Highly sensitive site-specific analysis of N-linked glycans on proteins.
Article in Methods in enzymology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Diverse germline-targeting HIV Env immunogens select for distinct mutations in the same knock-in mice B cell receptors.Nature communications · 2026Article
- Mapping the placental galectin-3 interactome identifies CD9 and ITGB1 as functional glycoprotein counterreceptors during syncytialization.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural and functional insights into the evolution of SARS-CoV-2 KP.3.1.1 spike protein.Cell reports · 2025Article
- Structural and Functional Insights into the Evolution of SARS-CoV-2 KP.3.1.1 Spike Protein.bioRxiv : the preprint server for biology · 2024Article
- Repeat modules and N-linked glycans define structure and antigenicity of a critical enterotoxigenic E. coli adhesin.PLoS pathogens · 2024Article
- Repeat modules and N-linked glycans define structure and antigenicity of a critical enterotoxigenicbioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Traditional mass spectrometry-based glycoproteomic approaches have been widely used for site-specific N-glycoform analysis, but a large amount of starting material is needed to obtain sampling that is representative of the vast diversity of N-glycans on glycoproteins. These methods also often include a complicated workflow and very challenging data analysis. These limitations have prevented glycoproteomics from being adapted to high-throughput platforms, and the sensitivity of the analysis is currently inadequate for elucidating N-glycan heterogeneity in clinical samples. Heavily glycosylated spike proteins of enveloped viruses, recombinantly expressed as potential vaccines, are prime targets for glycoproteomic analysis. Since the immunogenicity of spike proteins may be impacted by their glycosylation patterns, site-specific analysis of N-glycoforms provides critical information for vaccine design. Using recombinantly expressed soluble HIV Env trimer, we describe DeGlyPHER, a modification of our previously reported sequential deglycosylation strategy to yield a "single-pot" process. DeGlyPHER is an ultrasensitive, simple, rapid, robust, and efficient approach for site-specific analysis of protein N-glycoforms, that we developed for analysis of limited quantities of glycoproteins.
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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.