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ProteomicsRelative Quantitative Analysis of Site-Specific N-Linked Glycosylation in Hyperglycosylated In-terferon-β via Mass Spectrometry
Glycosylation is a critical determinant of the efficacy, stability, and pharmacological behavior of therapeutic proteins. R27T, an engineered variant of interferon-β1a, contains two N-glycosylation sites (Asn25 and Asn80), increasing its structural complexity and analytical requirements. In this stu...
ORGANISM(S): Homo sapiens (Human) 
2026-09-21 | PXD077477 | Pride
Interferon beta  n-linked glycan  site-specific glycosylation  relative quantitative analysis  r27t 
UnknownStability and Activity of the Hyperglycosylated Human Interferon-β R27T Variant.
Not available
S-EPMC7242330 | biostudies-literature
UnknownA Glycoengineered Interferon-β Mutein (R27T) Generates Prolonged Signaling by an Altered Receptor-Binding Kinetics.
Not available
S-EPMC6353837 | biostudies-literature
UnknownSensitization of glycoengineered interferon-β1a-resistant cancer cells by cFLIP inhibition for enhanced anti-cancer therapy.
Not available
S-EPMC5355153 | biostudies-literature
UnknownGlycosylation Heterogeneity of Hyperglycosylated Recombinant Human Interferon-β (rhIFN-β).
Not available
S-EPMC7114697 | biostudies-literature
UnknownGlycoengineering of interferon-β 1a improves its biophysical and pharmacokinetic properties.
Not available
S-EPMC4032242 | biostudies-literature
UnknownThe Comparison Between the Mutated HuIFN-β 27-101 and the Wild Type Interferon β: the Comprehensive In Silico Study to Evaluate the Effect of Mutations on IFN-β.
Not available
S-EPMC6912172 | biostudies-literature
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