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Jun Hirabayashi

Researcher at National Institute of Advanced Industrial Science and Technology

Publications -  273
Citations -  16685

Jun Hirabayashi is an academic researcher from National Institute of Advanced Industrial Science and Technology. The author has contributed to research in topics: Lectin & Galectin. The author has an hindex of 66, co-authored 270 publications receiving 15579 citations. Previous affiliations of Jun Hirabayashi include Teikyo University & Kagawa University.

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Oligosaccharide specificity of galectins: a search by frontal affinity chromatography.

TL;DR: In this paper, a frontal affinity chromatography (FAC) was used to quantitatively analyze the interactions at 20 °C between 13 galectins including 16 CRDs originating from mammals, chick, nematode, sponge, and mushroom, with 41 pyridylaminated (PA) oligosaccharides.
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Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins

TL;DR: The approach, termed isotope-coded glycosylation-site-specific tagging (IGOT), is based on the lectin column–mediated affinity capture of a set of glycopeptides generated by tryptic digestion of protein mixtures, followed by peptide-N-glycosidase–mediated incorporation of a stable isotope tag, 18O, specifically into the N-glyCosylation site.
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The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution

TL;DR: It appears that beta-galactoside-binding lectins and some non-lectin proteins form a superfamily whose members are widely distributed from vertebrates to invertebrates and a consideration of molecular evolution suggests that lectins belonging to this family probably existed in the Precambrian era.
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Evanescent-field fluorescence-assisted lectin microarray: a new strategy for glycan profiling.

TL;DR: A new microarray procedure based on an evanescent-field fluorescence-detection principle that allows sensitive, real-time observation of multiple lectin-carbohydrate interactions under equilibrium conditions is described, which should contribute to creation of a new paradigm for glycomics.