Abstract
Racemic 2'-methyl- and 3'-methyl-6-nitroquipazine ligands were selected as targets, synthesized and evaluated at the serotonin transporter employing an in vitro competitive inhibition assay with [3H]paroxetine and rat cortical membrane. The 2'-methyl-6-nitroquipazine was found to be 50 times more potent than the 3'-methyl-substituted counterpart and of comparable potency to the known high affinity agent 5-iodo-6-nitroquipazine.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Binding, Competitive
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Carrier Proteins / antagonists & inhibitors*
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Carrier Proteins / metabolism
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Cerebral Cortex / metabolism
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Membrane Glycoproteins / antagonists & inhibitors*
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Membrane Glycoproteins / metabolism
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Membrane Transport Proteins*
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Nerve Tissue Proteins*
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Paroxetine / metabolism
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Quipazine / analogs & derivatives
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Quipazine / chemical synthesis*
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Quipazine / metabolism
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Rats
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Selective Serotonin Reuptake Inhibitors / metabolism
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Serotonin Plasma Membrane Transport Proteins
Substances
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2'-methyl-6-nitroquipazine
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3'-methyl-6-nitroquipazine
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Carrier Proteins
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Membrane Glycoproteins
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Membrane Transport Proteins
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Nerve Tissue Proteins
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Serotonin Plasma Membrane Transport Proteins
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Serotonin Uptake Inhibitors
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Slc6a4 protein, rat
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Paroxetine
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Quipazine