Linked Life Data

9878803

Source:http://linkedlifedata.com/resource/pubmed/id/9878803

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-2-17
pubmed:abstractText
The Golgi complex is the site where the terminal carbohydrate modification of proteins and lipids occurs. These carbohydrates play a variety of biological roles, ranging from the stabilization of glycoprotein structure to the provision of ligands for cell-cell interactions to the regulation of cell surface properties. Progress in our understanding of the biosynthesis and regulation of glycoconjugates has been accelerating at a rapid pace. Recent advances in the field of yeast glycobiology have been particularly impressive. This review focuses on glycosylation of proteins in the Golgi of the yeast Saccharomyces cerevisiae, with emphasis on the candidate mannosyltransferases that participate in the synthesis of N-linked oligosaccharides. Current views on how these enzymes may be regulated and how glycosylation relates on other cellular processes are also discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
1426
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
309-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Asparagine-linked glycosylation in the yeast Golgi.
pubmed:affiliation
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York, Stony Brook, NY 11794-5215, USA. ndean@mcbsgi.bio.sunnysb.edu
pubmed:publicationType
Journal Article, Review