|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
11
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|
pubmed:dateCreated |
2003-5-16
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|
pubmed:abstractText |
A series of three O-methylated UDP-GalNAc analogues have been synthesised using a divergent strategy from a 3,6-di-O-pivaloyl GlcNAc derivative. The biological activity of these probes toward polypeptide-alpha-GalNAc-transferase T1 has been investigated. This study shows that this glycosyltransferase exhibits a very high substrate specificity.
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jun
|
|
pubmed:issn |
0960-894X
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|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
2
|
|
pubmed:volume |
13
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1853-6
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|
pubmed:dateRevised |
2006-11-15
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|
pubmed:meshHeading |
|
|
pubmed:year |
2003
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|
pubmed:articleTitle |
Synthesis and biological evaluation of new UDP-GalNAc analogues for the study of polypeptide-alpha-GalNAc-transferases.
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|
pubmed:affiliation |
Institut de Chimie Organique et Analytique, Université d'Orléans, BP 6759, 45067 Orléans, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
