Abstract
IP3 analogs were synthesized by the modification of phosphate at the 1-position, and their affinity for the IP3 receptor was analyzed by means of surface plasmon resonance measurements. Our results suggest that a hydrophobic and charged moiety linked to this position enhances the affinity for the IP3 receptor.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding, Competitive
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Calcium Channels / metabolism
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Cloning, Molecular
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Humans
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Inositol 1,4,5-Trisphosphate / analogs & derivatives*
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Inositol 1,4,5-Trisphosphate / chemical synthesis
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Inositol 1,4,5-Trisphosphate / metabolism
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Inositol 1,4,5-Trisphosphate Receptors
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Molecular Structure
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Receptors, Cytoplasmic and Nuclear / metabolism
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Surface Plasmon Resonance
Substances
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Calcium Channels
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ITPR1 protein, human
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Inositol 1,4,5-Trisphosphate Receptors
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Receptors, Cytoplasmic and Nuclear
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Inositol 1,4,5-Trisphosphate