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Yoshiki Yamaguchi

Researcher at Tohoku Pharmaceutical University

Publications -  270
Citations -  7268

Yoshiki Yamaguchi is an academic researcher from Tohoku Pharmaceutical University. The author has contributed to research in topics: Glycan & Glycosylation. The author has an hindex of 41, co-authored 247 publications receiving 6186 citations. Previous affiliations of Yoshiki Yamaguchi include University of Tokyo & Max Planck Society.

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Function and 3D Structure of the N-Glycans on Glycoproteins

TL;DR: This review provides an overview of crystallographic analyses of glycoproteins, in which electron density of the glycan moiety is clearly observed, and suggests the more mobile N-glycans on cell surface receptors seem to guide the partner ligand to its binding site and prevent irregular protein aggregation by covering oligomerization sites away from the ligand-binding site.
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Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI

TL;DR: P24 complexes act as cargo receptors for sorting GPI-anchored proteins into COPII vesicles and have shown the ability to modulate the GPI/COPII chiral reprograming process.
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Structural and molecular basis for hyperspecificity of RNA aptamer to human immunoglobulin G.

TL;DR: The ability of RNA aptamers to recognize--and bind to--human IgG with high specificity and affinity is demonstrated, and an optimized 23-nucleotide aptamer, Apt8-2, was shown to bind to the Fc domain of human IgG, but not to other IgG's, with high affinity.
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Synthesis of monoglucosylated high-mannose-type dodecasaccharide, a putative ligand for molecular chaperone, calnexin, and calreticulin

TL;DR: Interaction analysis of 2b with CRT was measured by 1H NMR spectroscopy, and the first NMR-based evidence for the specific binding of CRT to 2b was obtained.
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A Platform of C-type Lectin-like Receptor CLEC-2 for Binding O-Glycosylated Podoplanin and Nonglycosylated Rhodocytin

TL;DR: To elucidate the structural basis of the glycan-dependent and independent interactions, comparative crystallographic studies of podoplanin and rhodocytin in complex with CLEC-2 reveal unique and versatile binding modes that open a way to understand the functional consequences of CLEC -2-ligand interactions.