Tyrosylprotein sulfotransferase inhibitors generated by combinatorial target-Guided ligand assembly

Tyrosylprotein sulfotransferases (TPSTs) catalyze the sulfation of tyrosine residues within secreted and membrane-bound proteins. The modification modulates protein–protein interactions in the extracellular environment. Here we use combinatorial target-guided ligand assembly to discover the first kn...

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Veröffentlicht in:	Bioorganic & medicinal chemistry letters 2002-02, Vol.12 (3), p.329-332
Hauptverfasser:	Kehoe, John W., Maly, Dustin J., Verdugo, Dawn E., Armstrong, Joshua I., Cook, Brian N., Ouyang, Ying-Bin, Moore, Kevin L., Ellman, Jonathan A., Bertozzi, Carolyn R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aldehydes - chemistry Biological and medical sciences Combinatorial Chemistry Techniques Cytosol - drug effects Cytosol - enzymology Drug Evaluation, Preclinical Enzyme Inhibitors - chemical synthesis Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology Indicators and Reagents Ligands Medical sciences Miscellaneous Pharmacology. Drug treatments Sulfotransferases - antagonists & inhibitors
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Zusammenfassung:	Tyrosylprotein sulfotransferases (TPSTs) catalyze the sulfation of tyrosine residues within secreted and membrane-bound proteins. The modification modulates protein–protein interactions in the extracellular environment. Here we use combinatorial target-guided ligand assembly to discover the first known inhibitors of human TPST-2. Graphic
ISSN:	0960-894X 1464-3405
DOI:	10.1016/S0960-894X(01)00744-2