Disruption of spike protein N-glycosylation induces its endoplasmic reticulum retention and attenuates SARS-CoV-2 infectivity [PDF]
Journal of VirologyThe spike (S) protein of SARS-CoV-2 is extensively glycosylated, with N-glycosylation sites remaining highly conserved during viral evolution. While inhibiting N-glycosylation has been shown to significantly suppress SARS-CoV-2 infection, the underlying ...
Weili Kong +8 more
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N-Glycosylation at Asn291 Stabilizes TIM-4 and Promotes the Metastasis of NSCLC
Frontiers in Oncology, 2022 T-cell immunoglobulin domain and mucin domain 4 (TIM-4) is a transmembrane protein that promotes epithelial-mesenchymal transition (EMT), migration and invasion of non-small cell lung cancer (NSCLC) cells.
Siyuan Chen +9 more
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Glycosylation of viral proteins: Implication in virus–host interaction and virulence
Virulence, 2022 Glycans are among the most important cell molecular components. However, given their structural diversity, their functions have not been fully explored. Glycosylation is a vital post-translational modification for various proteins.
Tingting Feng +6 more
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ERO1 alpha deficiency impairs angiogenesis by increasing N-glycosylation of a proangiogenic VEGFA
Redox Biology, 2022 N-glycosylation and disulfide bond formation are two essential steps in protein folding that occur in the endoplasmic reticulum (ER) and reciprocally influence each other.
Ersilia Varone +10 more
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DeepNGlyPred: A Deep Neural Network-Based Approach for Human N-Linked Glycosylation Site Prediction
Molecules, 2021 Protein N-linked glycosylation is a post-translational modification that plays an important role in a myriad of biological processes. Computational prediction approaches serve as complementary methods for the characterization of glycosylation sites. Most
Subash C. Pakhrin +3 more
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IEEE Access, 2020 Glycosylation is the most complex post-modification effect of proteins. It participates in many biological processes in the human body and is closely related to many disease states.
Ching-Hsuan Chien +5 more
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Influence of N-Glycosylation on Virus–Host Interactions in Halorubrum lacusprofundi
Viruses, 2023 N-glycosylation is a post-translational modification of proteins that occurs across all three domains of life. In Archaea, N-glycosylation is crucial for cell stability and motility, but importantly also has significant implications for virus–host ...
L. Johanna Gebhard +4 more
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Frontiers in Cell and Developmental Biology, 2022 Glycosylation is a ubiquitous and universal cellular process in all domains of life. In eukaryotes, many glycosylation pathways occur simultaneously onto proteins and lipids for generating a complex diversity of glycan structures.
Zoé Durin +7 more
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GlypNirO: An automated workflow for quantitative N- and O-linked glycoproteomic data analysis
Beilstein Journal of Organic Chemistry, 2020 Mass spectrometry glycoproteomics is rapidly maturing, allowing unprecedented insights into the diversity and functions of protein glycosylation. However, quantitative glycoproteomics remains challenging.
Toan K. Phung +2 more
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Glycoform Modification of Secreted Recombinant Glycoproteins through Kifunensine Addition during Transient Vacuum Agroinfiltration. [PDF]
, 2018 Kifunensine, a potent and selective inhibitor of class I α-mannosidases, prevents α-mannosidases I from trimming mannose residues on glycoproteins, thus resulting in oligomannose-type glycans.
Kailemia, Muchena J +5 more
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