Results 1 to 10 of about 151,535 (246)
Genetics and Molecular Biology, 2001 The N-linked glycosylation of secretory and membrane proteins is the most complex posttranslational modification known to occur in eukaryotic cells. It has been shown to play critical roles in modulating protein function.
Maia Ivan G., Leite Adilson
doaj +5 more sources
Platelets and Defective N-Glycosylation [PDF]
International Journal of Molecular Sciences, 2020 N-glycans are covalently linked to an asparagine residue in a simple acceptor sequence of proteins, called a sequon. This modification is important for protein folding, enhancing thermodynamic stability, and decreasing abnormal protein aggregation within the endoplasmic reticulum (ER), for the lifetime and for the subcellular localization of proteins ...
Mammadova-Bach, Elmina +3 more
openaire +2 more sources
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
doaj +1 more source
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
doaj +1 more source
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
doaj +1 more source
Studying Lactoferrin N-Glycosylation [PDF]
International Journal of Molecular Sciences, 2017 Lactoferrin is a multifunctional glycoprotein found in the milk of most mammals. In addition to its well-known role of binding iron, lactoferrin carries many important biological functions, including the promotion of cell proliferation and differentiation, and as an anti-bacterial, anti-viral, and anti-parasitic protein.
Sercan Karav +4 more
openaire +5 more sources
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
doaj +1 more source
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
doaj +1 more source
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
doaj +1 more source
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
doaj +1 more source