ArticleNature protocols2018
Global site-specific analysis of glycoprotein N-glycan processing.
Article in Nature protocols, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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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
50 citing papers in PubMed, 89 citations in OpenAlex.
- IgA binding characteristics of golden hamster and ferret Fcα receptors.Journal of immunology (Baltimore, Md. : 1950) · 2026Article
- An Evolutionary Distinct Nipah Virus N-Glycosylation Site Provides Stability for Receptor Engagement.Molecular & cellular proteomics : MCP · 2026Article
- Glycan-related genes and genetic disorders.Journal of human genetics · 2026Review
- VAMP7-dependent late endosomal secretion of ER and mitochondrial proteins impacts the tumor microenvironment and macrophage engagement.Nature communications · 2026Article
- Asymmetrically glycosylated IgG1 antibodies are universal and drive human disease.Nature communications · 2025Article
- Article
- Posttranslational sialylation and its impact on neutrophil recruitment.Journal of leukocyte biology · 2025Review
- Establishment of a Novel Platform for Developing Oral Vaccines Based on the Surface Display System of Yeast Spores.International journal of molecular sciences · 2025Article
- Mechanisms underlining Kelp (Saccharina japonica) adaptation to relative high seawater temperature.BMC genomics · 2025Article
- [Applications of chromatography in glycomics].Se pu = Chinese journal of chromatography · 2024Review
- Growing Glycans in Rosetta: Accurate de novo glycan modeling, density fitting, and rational sequon design.PLoS computational biology · 2024Article
- SEL1L-HRD1 ER-associated degradation regulates leptin receptor maturation and signaling in POMC neurons in diet-induced obesity.Research square · 2024Article
- An mRNA-based platform for the delivery of pathogen-specific IgA into mucosal secretions.Cell reports. Medicine · 2023Article
- Glycan heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.PLoS pathogens · 2023Article
- Study of βScientific reports · 2023Article
- N-Linked Glycosylation and Expression of Duck Plague Virus pUL10 Promoted by pUL49.5.Microbiology spectrum · 2023Article
- Deciphering the Properties and Functions of Glycoproteins Using Quantitative Proteomics.Journal of proteome research · 2023Review
- Review
- Article
- Glucose-mediated N-glycosylation of RPTPα affects its subcellular localization and Src activation.Oncogene · 2023Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
N-glycans contribute to the folding, stability and functions of the proteins they decorate. They are produced by transfer of the glycan precursor to the sequon Asn-X-Thr/Ser, followed by enzymatic trimming to a high-mannose-type core and sequential addition of monosaccharides to generate complex-type and hybrid glycans. This process, mediated by the concerted action of multiple enzymes, produces a mixture of related glycoforms at each glycosite, making analysis of glycosylation difficult. To address this analytical challenge, we developed a robust semiquantitative mass spectrometry (MS)-based method that determines the degree of glycan occupancy at each glycosite and the proportion of N-glycans processed from high-mannose type to complex type. It is applicable to virtually any glycoprotein, and a complete analysis can be conducted with 30 μg of protein. Here, we provide a detailed description of the method that includes procedures for (i) proteolytic digestion of glycoprotein(s) with specific and nonspecific proteases; (ii) denaturation of proteases by heating; (iii) sequential treatment of the glycopeptide mixture with two endoglycosidases, Endo H and PNGase F, to create unique mass signatures for the three glycosylation states; (iv) LC-MS/MS analysis; and (v) data analysis for identification and quantitation of peptides for the three glycosylation states. Full coverage of site-specific glycosylation of glycoproteins is achieved, with up to thousands of high-confidence spectra hits for each glycosite. The protocol can be performed by an experienced technician or student/postdoc with basic skills for proteomics experiments and takes ∼7 d to complete.
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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.