Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression-Reference-Cited by-同舟云学术

Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression

Published:2011-02 Issue:1 Volume:489 Page:10-15
ISSN:0304-3940
Container-title:Neuroscience Letters
language:en
Short-container-title:Neuroscience Letters

Author:

Hu Huaiyu,Li Jing,Zhang Zhen,Yu Miao

Publisher

Elsevier BV

Subject

General Neuroscience

Reference36 articles.

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3. LARGE can functionally bypass alpha-dystroglycan glycosylation defects in distinct congenital muscular dystrophies;Barresi;Nat. Med.,2004

4. Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin;Chiba;J. Biol. Chem.,1997

5. The effects of dystrophin gene mutations on the ERG in mice and humans;Cibis;Invest. Ophthalmol. Vis. Sci.,1993

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