Literature DB >> 15467391

Structure, function and pathology of O-mannosyl glycans.

Tamao Endo1.   

Abstract

Animal cells contain many glycoproteins, i.e. , proteins with covalently liked sugar chains. The major glycans of glycoproteins can be classified into two groups, N-glycans and O-glycans, according to their glycan-peptide linkage regions. Development of sensitive methods for the analyses of glycan structures have revealed a new type of glycosidic linkage to the peptide portion, the O-mannosyl linkage, in mammals, which used to be considered specific to yeast. O-Mannosylation is present in a limited number of glycoproteins of brain, nerve, and skeletal muscle. Recently O-mannosylation has been shown to be important in muscle and brain development. Glycobiology of O-mannosyl glycans is expected to produce remarkable advances in the understanding and treatment of congenital muscular dystrophies. In this article, I describe the structure, biosynthesis, and pathology of O-mannosyl glycans.

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Year:  2004        PMID: 15467391     DOI: 10.1023/B:GLYC.0000043740.26062.2c

Source DB:  PubMed          Journal:  Glycoconj J        ISSN: 0282-0080            Impact factor:   2.916


  30 in total

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Journal:  Biochim Biophys Acta       Date:  1999-12-06

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9.  Loss-of-function of an N-acetylglucosaminyltransferase, POMGnT1, in muscle-eye-brain disease.

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  15 in total

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Journal:  Nat Clin Pract Neurol       Date:  2006-04

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Review 7.  Glycosylation and other PTMs alterations in neurodegenerative diseases: Current status and future role in neurotrauma.

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8.  Expression of the murine Pomt1 gene in both the developing brain and adult muscle tissues and its relationship with clinical aspects of Walker-Warburg syndrome.

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9.  Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins.

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