| From glycosylation disorders back to glycosylation: what have we learned? | |
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MedLine Citation:
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PMID: 19007883 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Diseases of glycosylation have long remained confined to the rare hematological disorders, the Tn-syndrome and paroxysmal nocturnal hemoglobinuria. This rarity was often interpreted as a sign that defects of glycosylation are either lethal, or remain asymptomatic because of the large redundancy found in glycosylation pathways. The description of multiple glycosylation disorders over the last years has definitively settled the issue and demonstrated the broad range of biological processes relying on proper glycosylation. However, beyond establishing the developmental and physiological roles of glycosylation how did glycosylation disorders provided new insights to the field of glycobiology? |
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Authors:
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Thierry Hennet |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review Date: 2008-10-22 |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1792 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 2009 Sep |
Date Detail:
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Created Date: 2009-09-21 Completed Date: 2009-11-25 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: Netherlands |
Other Details:
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Languages: eng Pagination: 921-4 Citation Subset: IM |
Affiliation:
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Institute of Physiology, University of Zürich, Switzerland. thennet@access.uzh.ch |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Carbohydrate Metabolism, Inborn Errors
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complications*,
genetics Carbohydrate-Deficient Glycoprotein Syndrome / complications, genetics Cytidine Monophosphate N-Acetylneuraminic Acid / metabolism Glycosylation* Hemoglobinuria, Paroxysmal / etiology, genetics Hexosyltransferases / genetics, metabolism Humans Lipid Metabolism, Inborn Errors / complications Lipopolysaccharides / metabolism Membrane Proteins / genetics, metabolism |
| Chemical | |
Reg. No./Substance:
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0/Lipopolysaccharides; 0/Membrane Proteins; 0/lipid-linked oligosaccharides; 3063-71-6/Cytidine Monophosphate N-Acetylneuraminic Acid; EC 2.4.1.-/Hexosyltransferases; EC 2.4.1.119/dolichyl-diphosphooligosaccharide - protein glycotransferase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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