Matches in DBpedia 2016-04 for { ?s ?p "The N-methyl-D-aspartate receptor (also known as the NMDA receptor or NMDAR), is a glutamate receptor and ion channel protein found in nerve cells. It is activated when glutamate and glycine (or D-serine) bind to it, and when activated it allows positively charged ions to flow through the cell membrane. The NMDA receptor is very important for controlling synaptic plasticity and memory function.The NMDAR is a specific type of ionotropic glutamate receptor. The NMDA receptor is named this because the agonist molecule N-methyl-D-aspartate (NMDA) binds selectively to it, and not to other glutamate receptors. Activation of NMDA receptors results in the opening of an ion channel that is nonselective to cations with a reversal potential near 0 mV. While the opening and closing of the ion channel is primarily gated by ligand binding, the current flow through the ion channel is voltage-dependent, a result of blockade of the open ion channel block by extracellular Mg2+ & Zn2+ ions. This allows the flow of Na+ and small amounts of Ca2+ ions into the cell and K+ out of the cell to be voltage-dependent.Calcium flux through NMDARs is thought to be critical in synaptic plasticity, a cellular mechanism for learning and memory. The gating (opening and closing) of the NMDA receptor is somewhat complex. It is primarily a ligand-gated channel, but does display some weaker voltage-dependence modulation of the ligand-dependent gating. The ligand-gating requires co-activation by two ligands: glutamate and either D-serine or glycine. Most of the voltage-dependence of the current flow through the channel ionophore derives from the voltage dependence of Magnesium or Zinc ions to a site inside the channel. This voltage-dependence arises because the Magnesium or Zinc are charged (both are divalent cations), the binding site is located at a location in the protein that is within the plasma membrane and thus within the electric field generated by the membrane voltage, and because binding of these ions within the channel prevents the flow of other ions through the channel. The activity of the NMDA receptor is affected by many psychoactive drugs such as phencyclidine (PCP), alcohol (ethanol) and dextromethorphan (DXM). The anaesthetic effects of the drugs ketamine and nitrous oxide are partially because of their effects on NMDA receptor activity."@en }
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- NMDA_receptor abstract "The N-methyl-D-aspartate receptor (also known as the NMDA receptor or NMDAR), is a glutamate receptor and ion channel protein found in nerve cells. It is activated when glutamate and glycine (or D-serine) bind to it, and when activated it allows positively charged ions to flow through the cell membrane. The NMDA receptor is very important for controlling synaptic plasticity and memory function.The NMDAR is a specific type of ionotropic glutamate receptor. The NMDA receptor is named this because the agonist molecule N-methyl-D-aspartate (NMDA) binds selectively to it, and not to other glutamate receptors. Activation of NMDA receptors results in the opening of an ion channel that is nonselective to cations with a reversal potential near 0 mV. While the opening and closing of the ion channel is primarily gated by ligand binding, the current flow through the ion channel is voltage-dependent, a result of blockade of the open ion channel block by extracellular Mg2+ & Zn2+ ions. This allows the flow of Na+ and small amounts of Ca2+ ions into the cell and K+ out of the cell to be voltage-dependent.Calcium flux through NMDARs is thought to be critical in synaptic plasticity, a cellular mechanism for learning and memory. The gating (opening and closing) of the NMDA receptor is somewhat complex. It is primarily a ligand-gated channel, but does display some weaker voltage-dependence modulation of the ligand-dependent gating. The ligand-gating requires co-activation by two ligands: glutamate and either D-serine or glycine. Most of the voltage-dependence of the current flow through the channel ionophore derives from the voltage dependence of Magnesium or Zinc ions to a site inside the channel. This voltage-dependence arises because the Magnesium or Zinc are charged (both are divalent cations), the binding site is located at a location in the protein that is within the plasma membrane and thus within the electric field generated by the membrane voltage, and because binding of these ions within the channel prevents the flow of other ions through the channel. The activity of the NMDA receptor is affected by many psychoactive drugs such as phencyclidine (PCP), alcohol (ethanol) and dextromethorphan (DXM). The anaesthetic effects of the drugs ketamine and nitrous oxide are partially because of their effects on NMDA receptor activity.".
- Q414896 abstract "The N-methyl-D-aspartate receptor (also known as the NMDA receptor or NMDAR), is a glutamate receptor and ion channel protein found in nerve cells. It is activated when glutamate and glycine (or D-serine) bind to it, and when activated it allows positively charged ions to flow through the cell membrane. The NMDA receptor is very important for controlling synaptic plasticity and memory function.The NMDAR is a specific type of ionotropic glutamate receptor. The NMDA receptor is named this because the agonist molecule N-methyl-D-aspartate (NMDA) binds selectively to it, and not to other glutamate receptors. Activation of NMDA receptors results in the opening of an ion channel that is nonselective to cations with a reversal potential near 0 mV. While the opening and closing of the ion channel is primarily gated by ligand binding, the current flow through the ion channel is voltage-dependent, a result of blockade of the open ion channel block by extracellular Mg2+ & Zn2+ ions. This allows the flow of Na+ and small amounts of Ca2+ ions into the cell and K+ out of the cell to be voltage-dependent.Calcium flux through NMDARs is thought to be critical in synaptic plasticity, a cellular mechanism for learning and memory. The gating (opening and closing) of the NMDA receptor is somewhat complex. It is primarily a ligand-gated channel, but does display some weaker voltage-dependence modulation of the ligand-dependent gating. The ligand-gating requires co-activation by two ligands: glutamate and either D-serine or glycine. Most of the voltage-dependence of the current flow through the channel ionophore derives from the voltage dependence of Magnesium or Zinc ions to a site inside the channel. This voltage-dependence arises because the Magnesium or Zinc are charged (both are divalent cations), the binding site is located at a location in the protein that is within the plasma membrane and thus within the electric field generated by the membrane voltage, and because binding of these ions within the channel prevents the flow of other ions through the channel. The activity of the NMDA receptor is affected by many psychoactive drugs such as phencyclidine (PCP), alcohol (ethanol) and dextromethorphan (DXM). The anaesthetic effects of the drugs ketamine and nitrous oxide are partially because of their effects on NMDA receptor activity.".