Results 11 to 20 of about 191,408 (290)
Background Congenital disorders of glycosylation (CDG) are a growing group of rare genetic disorders. The most common CDG is phosphomannomutase 2 (PMM2)-CDG which often has a severe clinical presentation and life-limiting consequences.
C. Pascoal +13 more
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Concerted Regulation of Glycosylation Factors Sustains Tissue Identity and Function
Glycosylation is a fundamental cellular process affecting human development and health. Complex machinery establishes the glycan structures whose heterogeneity provides greater structural diversity than other post-translational modifications.
Daniel Sobral +4 more
doaj +1 more source
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
Innovative Metrics for Reporting and Comparing the Glycan Structural Profile in Biotherapeutics
Glycosylation is a critical quality attribute in biotherapeutics, impacting properties such as protein stability, solubility, clearance rate, efficacy, immunogenicity, and safety.
Renato Mastrangeli +2 more
doaj +1 more source
Involvement of ST6Gal I‐mediated α2,6 sialylation in myoblast proliferation and differentiation
Myogenesis is a physiological process which involves the proliferation of myoblasts and their differentiation into multinucleated myotubes, which constitute the future muscle fibers.
Caroline Vergé +5 more
doaj +1 more source
Glycosylation of viral proteins: Implication in virus–host interaction and virulence
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
Osteocalcin is a bone matrix protein that acts like a hormone when it reaches the blood, and has different effects in mice and humans.
Harry C Blair, Paul H Schlesinger
openaire +3 more sources
O-Glycosylation in many fungal species is initiated in the endoplasmic reticulum by protein mannosyltransferases (Pmt-proteins), which transfer mannose to serine or threonine residues, and it is completed by mannosyltransferases (Mnt-proteins) in the Golgi.
J F, Ernst, S K, Prill
openaire +2 more sources
Glycosylation alterations, a key driver throughout tumorigenesis and tumor progression, could regulate the microenvironment and immune response as well as lead to harmful metabolism and cell signaling.
Guihua Tang +3 more
doaj +1 more source
Glycosylation is a ubiquitous process that is universally conserved in nature. The various products of glycosylation, such as polysaccharides, glycoproteins, and glycolipids, perform a myriad of intra- and extracellular functions.
Liubov Yakovlieva +2 more
doaj +1 more source

