Results 51 to 60 of about 4,132 (206)
The α1,6-fucosyltransferase (encoded by FUT8 gene) is the key enzyme transferring fucose to the innermost GlcNAc residue on an N-glycan through an α-1,6 linkage in the mammalian cells.
Ganglong Yang +5 more
doaj +1 more source
Glycoproteomic Analysis of Antibodies
Antibody glycosylation has been shown to change with various processes. This review presents mass spectrometric approaches for antibody glycosylation analysis at the level of released glycans, glycopeptides, and intact protein. With regard to IgG fragment crystallizable glycosylation, mass spectrometry has shown its potential for subclass-specific ...
Zauner, G. +6 more
openaire +4 more sources
Glycomics & Glycoproteomics in Glycoconjugate journal [PDF]
Glycoconjugates belong without doubt to the most complex and diverse molecules found in nature. They are crucial for both prokaryotic and eukaryotic life despite the fact that the glycosylation pathways and building blocks do diverge tremendously between the different phylogenetic kingdoms [1].
Kolarich, D., Wuhrer, M.
openaire +3 more sources
Databases and Associated Tools for Glycomics and Glycoproteomics
The access to biodatabases for glycomics and glycoproteomics has proven to be essential for current glycobiological research. This chapter presents available databases that are devoted to different aspects of glycobioinformatics.
Rojas-Macias, Miguel A. +43 more
core +1 more source
“Ghost” Fragment Ions in Structure and Site-Specific Glycoproteomics Analysis
Mass spectrometry (MS) can unlock crucial insights into the intricate world of glycosylation analysis. Despite its immense potential, the qualitative and quantitative analysis of isobaric glycopeptide structures remains one of the most daunting hurdles ...
Diana Campos (422207) +13 more
core +1 more source
The mouse is a key model in biomedical research, yet its tissue-specific glycoproteome remains incompletely characterized due to glycan complexity and microheterogeneity.
Yongqi Wu +9 more
doaj +1 more source
O‐GlcNAcylated TAP1 Impairs Antigen Presentation and Promotes Immune Evasion in Bladder Cancer
This article unveils a critical mechanism of immune evasion in bladder cancer, which the O‐GlcNAc modification of TAP1 disrupts antigen presentation. This modification triggers HLA‐A degradation, shielding tumor cells from CD8+ T cell attack. The findings highlight targeting this pathway as a promising therapeutic avenue to sensitize tumors to ...
Jinpeng Wu +10 more
wiley +1 more source
SSR4, a TRAP component induced in B cells, governs BAFFR N‐glycosylation via DDOST to sustain NF‐κB signaling, B‐cell differentiation, and TLS maturation. Its loss impairs anti‐tumor immunity, while overexpression improves antibody glycosylation and ADCC, revealing a critical regulator for cancer immunotherapy.
Wei Zhao +15 more
wiley +1 more source
This Perspective explores the emerging landscape of cell membrane‐coated nanoparticles (CM‐NPs) as intelligent, immune‐compatible platforms for cancer therapy. Highlighting design strategies, translational challenges, and competitive positioning, it outlines how integrating biomimetic targeting with advanced analytical and manufacturing tools could ...
A. K. M. M. Alam +4 more
wiley +1 more source
Glycoproteomics Technologies in Glycobiotechnology
Glycosylation is a key factor determining the pharmacological properties of biotherapeutics, including their stability, solubility, bioavailability, pharmacokinetics, and immunogenicity. As such, comprehensive information about glycosylation of biotherapeutics is critical to demonstrate similarity.
Kathirvel Alagesan +3 more
openaire +5 more sources

