N-Linked glycosylation of hemagglutinin (HA) has been demonstrated to regulate the virulence and receptor-binding specificity of avian influenza virus (AIV).
Liu-gang TAN +8 more
doaj +1 more source
Proteome-wide analysis of single-nucleotide variations in the N-glycosylation sequon of human genes. [PDF]
N-linked glycosylation is one of the most frequent post-translational modifications of proteins with a profound impact on their biological function.
Raja Mazumder +4 more
doaj +1 more source
TbGT8 is a bifunctional glycosyltransferase that elaborates N-linked glycans on a protein phosphatase AcP115 and a GPI-anchor modifying glycan in Trypanosoma brucei [PDF]
The procyclic form of Trypanosoma brucei expresses procyclin surface glycoproteins with unusual glycosylphosphatidylinositol-anchor side chain structures that contain branched N-acetyllactosamine and lacto-N-biose units.
Hashida, Kazunori +7 more
core +1 more source
Regulation of the Axillary Osmidrosis-Associated ABCC11 Protein Stability by N-Linked Glycosylation: Effect of Glucose Condition. [PDF]
ATP-binding cassette C11 (ABCC11) is a plasma membrane protein involved in the transport of a variety of lipophilic anions. ABCC11 wild-type is responsible for the high-secretion phenotypes in human apocrine glands, such as that of wet-type ear wax, and ...
Yu Toyoda +4 more
doaj +1 more source
Identifying Components of a Halobacterium salinarum N-Glycosylation Pathway
Whereas N-glycosylation is a seemingly universal process in Archaea, pathways of N-glycosylation have only been experimentally verified in a mere handful of species.
Zlata Vershinin +3 more
doaj +1 more source
Analysis of N-Glycosylation Sites in HIV glycoprotein 160 [PDF]
HIV infection is a condition caused by the human immunodeficiency virus. The condition gradually destroys the immune system, which makes it harder for the body to fight infections. HIV presents a complex knot for scientists to unravel.
Rajendra Mandage
core +1 more source
Computational Prediction of N- and O-Linked Glycosylation Sites for Human and Mouse Proteins
Protein glycosylation is one of the most complex posttranslational modifications (PTM) that play a fundamental role in protein function. Identification and annotation of these sites using experimental approaches are challenging and time consuming. Hence,
Campbell, M, Taherzadeh, G, Zhou, Y
core +1 more source
Approaching the secrets of N-glycosylation in Aspergillus fumigatus [PDF]
The mannosyltransferase Och1 is the key enzyme for synthesis of elaborated protein N-glycans in yeast. In filamentous fungi genes implicated in outer chain formation are present, but their function is unclear.
Engel Jakob +25 more
core +2 more sources
Precursor ion scanning for detection and structural characterization of heterogeneous glycopeptide mixtures [PDF]
The structure of N-linked glycans is determined by a complex, anabolic, intracellular pathway but the exact role of individual glycans is not always clear.
Gill, A C +7 more
core +1 more source
Impact of Yeast Glycosylation Pathway on Cell Integrity and Morphology, Glycosylation, Stefana Petrescu (Ed.), ISBN: 978-953-51-0771-2, InTech, Available from: http://www.intechopen.com/books/glycosylation/impact-of-yeast-glycosylation-pathway-on-cell-integrity-and-morphology [PDF]
Protein glycosylation is a multi step reaction, well conserved in the eukaryotic cells. In N-glycosylation reactions dolichyl phosphate (DolP) serves as a lipid acceptor of sugar residues forming DolPPGlcNAc2Man9Glc3.
Palamarczyk, Grazyna +5 more
core +1 more source

