| The roles of enzyme localisation and complex formation in glycan assembly within the Golgi apparatus. | |
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MedLine Citation:
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PMID: 15261667 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Cell surface glycans govern numerous cell-cell interactions are therefore key determinants of multicellular biology. They originate from biosynthetic pathways comprising an assembly line of glycosyltransferases within the Golgi compartment. Although the mechanisms of Golgi enzyme localisation are still under debate, the distribution of these enzymes among the Golgi cisternae can dictate the overall structures produced by the cell. Fine-tuning of glycan biosynthetic pathways is further accomplished by specific associations among glycosyltransferases. Together, localisation and association govern the assembly of complex glycans and thereby regulate interactions at the cell surface. |
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Authors:
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Christopher L de Graffenried; Carolyn R Bertozzi |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S.; Review |
Journal Detail:
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Title: Current opinion in cell biology Volume: 16 ISSN: 0955-0674 ISO Abbreviation: Curr. Opin. Cell Biol. Publication Date: 2004 Aug |
Date Detail:
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Created Date: 2004-07-20 Completed Date: 2005-01-31 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 8913428 Medline TA: Curr Opin Cell Biol Country: United States |
Other Details:
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Languages: eng Pagination: 356-63 Citation Subset: IM |
Affiliation:
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Department of Chemistry, University of California, Berkeley, California 94720-1460, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Gangliosides / biosynthesis Glycosylation Glycosyltransferases / metabolism* Golgi Apparatus / enzymology* Heparitin Sulfate / biosynthesis Humans Mannosidases / chemistry, metabolism Models, Biological Polysaccharides / metabolism* Protein Transport |
| Grant Support | |
ID/Acronym/Agency:
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GM59907/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Gangliosides; 0/Polysaccharides; 9050-30-0/Heparitin Sulfate; EC 2.4.-/Glycosyltransferases; EC 3.2.1.-/Mannosidases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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