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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
2009-4-13
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pubmed:abstractText |
Total synthesis through block glycosylation and selective chemical O-sulfation of tyrosine residues yielded the glycopeptide recognition domain A (X=SO(3) (-)) of the P-selectin glycoprotein ligand 1, in which the terminal sialic acid of the complex hexasaccharide side chain was replaced by (S)-cyclohexyl lactic acid. In binding assays the O-sulfated structure A showed high affinity towards P-selectin, the non-sulfated towards E-selectin.
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:issn |
1521-3773
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
48
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pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
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pubmed:pagination |
3174-8
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pubmed:meshHeading |
pubmed-meshheading:19322854-Animals,
pubmed-meshheading:19322854-E-Selectin,
pubmed-meshheading:19322854-Glycopeptides,
pubmed-meshheading:19322854-Glycosylation,
pubmed-meshheading:19322854-Humans,
pubmed-meshheading:19322854-Membrane Glycoproteins,
pubmed-meshheading:19322854-Mice,
pubmed-meshheading:19322854-P-Selectin,
pubmed-meshheading:19322854-Protein Structure, Tertiary,
pubmed-meshheading:19322854-Sulfates
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pubmed:year |
2009
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pubmed:articleTitle |
Sulfated and non-sulfated glycopeptide recognition domains of P-selectin glycoprotein ligand 1 and their binding to P- and E-selectin.
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pubmed:affiliation |
Institut für Organische Chemie, Johannes Gutenberg-Universität Mainz, Duesbergweg 10-14, 55128 Mainz, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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