1. Characterization of a novel modification on IgG2 light chain Evidence for the presence of O-linked mannosylation 2. O-Fucosylation of an antibody light chain: Characterization of a modification occurring on an IgG1 molecule 3. Carbohydrate compostion and presence of a fucose protein linkage in...
[4]Liping Zhang, Kelly G. Ten Hagen. Dissecting the Biological Role of Mucin-type O-Glycosylation Using RNA Interference in Drosophila Cell Culture. [5]John F Valliere-Douglass, Lowell J Brady, Chris Farnsworth, et al. O-Fucosylation of an antibody light chain: Characterization of a modificat...
O-fucosylation of an antibody light chain: characterization of a modification occurring on an IgG1 molecule.doi:10.1093/GLYCOB/CWN116John F Valliere-DouglassLowell J BradyChris FarnsworthDanielle PaceAlain BallandAlison WallaceWesley WangMichael J Treuheit...
[4]Liping Zhang, Kelly G. Ten Hagen. Dissecting the Biological Role of Mucin-type O-Glycosylation Using RNA Interference in Drosophila Cell Culture. [5]John F Valliere-Douglass, Lowell J Brady, Chris Farnsworth, et al. O-Fucosylation of an antibody ...
F Valliere-Douglass, Lowell J Brady, Chris Farnsworth, et al. O-Fucosylation of an antibody ...
O-Fucosylation plays crucial roles in various essential biological events. Alongside the well-established O-fucosylation of epidermal growth factor-like repeats by protein O-fucosyltransferase 1 (POFUT1) and thrombospondin type 1 repeats by POFUT2, we re
Immunoprecipitation (IP): protein pulled down with an anti-Notch1 antibody. Immune blot (IB): detection of O-fucosylation by an O-fucose assay. (F, G) IP and western blot analysis of Notch1 and Jagged-1 in hESCs transfected with scramble, poFUT1 siRNA, or vector, poFUT1 cDNA or po...
Surprisingly, we identified >150 glycosites on mature peptide hormones with many located in the receptor-interacting regions. O-glycans are known to modulate receptor functions, as first described for O-fucosylation of the Notch receptor53, and more recently for GalNAc-type O-glycosylation of the ...
We observed a novel fucosylation of MMRN1 at T216, which is within the N-terminal EMI domain of the protein. The O-fucosylation on T216 of MMRN1 was confirmed by EThcD analysis as was the predicted O-fucosylation of the C-terminal EGF-like domain at T1055 (Fig. 5A and supplemental ...
Type II (LAD II) disorder results from a defect in fucose metabolism which enables the correct fucosylation of glycoproteins, including H antigen biosynthesis51,52. Due to the low prevalence of each rare disease, medical expertise is rare, knowledge is scarce, care offerings inadequate, and ...