Synthetic glycopeptides reveal specific binding pattern and conformational change at O-mannosylated position of α-dystroglycan by POMGnT1 catalyzed GlcNAc modification-Reference-Cited by-同舟云学术

Synthetic glycopeptides reveal specific binding pattern and conformational change at O-mannosylated position of α-dystroglycan by POMGnT1 catalyzed GlcNAc modification

Published:2019-07 Issue:13 Volume:27 Page:2822-2831
ISSN:0968-0896
Container-title:Bioorganic & Medicinal Chemistry
language:en
Short-container-title:Bioorganic & Medicinal Chemistry

Author:

Hinou Hiroshi,Kikuchi Seiya,Ochi Rika,Igarashi Kota,Takada Wataru,Nishimura Shin-Ichiro

Funder

Hokkaido University

MEXT

JSPS

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

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5. The muscular dystrophy gene TMEM5 encodes a ribitol beta1,4-xylosyltransferase required for the functional glycosylation of dystroglycan;Manya;J Biol Chem,2016

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