Abstract
The title compound, which differs from the powerful O-GlcNAcase (OGA) inhibitor GlcNAc-thiazoline only at the chalcogen atom (Se for S), is a much weaker inhibitor in a direct OGA assay. In human cells, however, the selenazoline shows comparable ability to induce hyper-O-GlcNAc-ylation, and the two show similar reduction of insulin-stimulated translocation of glucose transporter 4 in differentiated 3T3 adipocytes.
Copyright © 2010 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, N.I.H., Intramural
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Research Support, Non-U.S. Gov't
MeSH terms
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3T3-L1 Cells
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Acetylglucosamine / analysis
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Acetylglucosamine / metabolism
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Adipocytes / metabolism
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Amino Acid Sequence
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Animals
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Cell Differentiation / drug effects
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Cell Line
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Clostridium perfringens / enzymology
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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Glucosamine / analogs & derivatives*
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Glucosamine / chemical synthesis
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Glucosamine / chemistry
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Glucosamine / pharmacology
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Glucose Transporter Type 4 / metabolism
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Glycosylation
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HeLa Cells
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Humans
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Insulin / pharmacology
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Mice
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Models, Molecular
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Molecular Sequence Data
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Molecular Structure
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Sequence Alignment
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Structure-Activity Relationship
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Thiazoles / chemical synthesis
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Thiazoles / chemistry
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Thiazoles / pharmacology*
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beta-N-Acetylhexosaminidases / antagonists & inhibitors*
Substances
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Enzyme Inhibitors
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GlcNAc-thiazoline
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Glucose Transporter Type 4
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Insulin
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Thiazoles
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hexosaminidase C
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beta-N-Acetylhexosaminidases
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Glucosamine
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Acetylglucosamine