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Katsuyoshi Masuda

Researcher at Kyoto University

Publications -  81
Citations -  1910

Katsuyoshi Masuda is an academic researcher from Kyoto University. The author has contributed to research in topics: Mass spectrometry & Photoaffinity labeling. The author has an hindex of 22, co-authored 80 publications receiving 1777 citations. Previous affiliations of Katsuyoshi Masuda include Niigata University of Pharmacy and Applied Life Sciences & Meijo University.

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Differential N-glycan patterns of secreted and intracellular IgG produced in Trichoplusia ni cells.

TL;DR: The studies indicate that Trichoplusia ni TN-5B1-4 cells are capable of terminal galactosylation, however, the processing pathways in these cell lines appear to diverge from mammalian cells in the formation of paucimannosidic structures, in the presence of α1,3-fucose linkages, and in the absence of sialylation.
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Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region.

TL;DR: The structure of squid rhodopsin was determined at 3.7Å resolution, which transduces signals through the Gq protein to the phosphoinositol cascade, and showed seven transmembrane helices and an amphipathic helix H8 has similar geometry to structures from bovine rhodopin, coupling to Gt, and humanβ2-adrenergic receptor, coupled to Gs.
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Characterization of the Modes of Binding between Human Sweet Taste Receptor and Low-Molecular-Weight Sweet Compounds

TL;DR: This work successfully determined the amino acid residues responsible for binding to sweeteners in the cleft of hT1R2 ATD and suggests that individual ligands have sets of specific residues for binding in correspondence with the chemical structures and other residuesresponsible for interacting with multiple ligands.
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N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells: effects of mammalian galactosyltransferase.

TL;DR: The ability to promote galactosylation and reduce paucimannosidic N-glycans suggests that the oligosaccharide processing pathway in insect cells may be manipulated to mimic more closely that of mammalian cells.
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Pairing of oligosaccharides in the Fc region of immunoglobulin G

TL;DR: A comparison of electrospray ionization mass spectrometry data obtained using a variety of Fc fragments derived from human and mouse IgG that do and do not retain the inter‐chain disulfide bridge revealed that the Fc portion can be asymmetric as well as symmetric with respect to glycosylation.