| References |
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| REF 1 |
N-terminal PDZ-binding domain in Kv1 potassium channels. FEBS Lett. 2002 Nov 20;531(3):529-37.
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| REF 2 |
Ligand binding of the second PDZ domain regulates clustering of PSD-95 with the Kv1.4 potassium channel. J Biol Chem. 2002 Feb 1;277(5):3640-6.
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| REF 3 |
The PDZ1 domain of SAP90. Characterization of structure and binding. J Biol Chem. 2002 Mar 1;277(9):6967-73.
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| REF 4 |
Activation of NMDA receptors and L-type voltage-gated calcium channels mediates enhanced formation of Fyn-PSD95-NR2A complex after transient brain ischemia. Brain Res. 2002 Nov 15;955(1-2):123-32.
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| REF 5 |
DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95. Genes Cells. 1997 Jun;2(6):415-24.
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| REF 6 |
Selectivity and promiscuity of the first and second PDZ domains of PSD-95 and synapse-associated protein 102. J Biol Chem. 2002 Jun 14;277(24):21697-711.
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| REF 7 |
Binding of neuroligins to PSD-95. Science. 1997 Sep 5;277(5331):1511-5.
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| REF 8 |
Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science. 1995 Sep 22;269(5231):1737-40.
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| REF 9 |
Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. J Neurosci. 1996 Apr 1;16(7):2157-63.
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| REF 10 |
A specific N-terminal residue in Kv1.5 is required for upregulation of the channel by SAP97. Biochem Biophys Res Commun. 2006 Mar 31;342(1):1-8.
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| REF 11 |
Molecular mechanisms regulating the differential association of kainate receptor subunits with SAP90/PSD-95 and SAP97. J Biol Chem. 2001 May 11;276(19):16092-9.
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| REF 12 |
SAP90 binds and clusters kainate receptors causing incomplete desensitization. Neuron. 1998 Oct;21(4):727-39.
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| REF 13 |
beta 1-adrenergic receptor association with PSD-95. Inhibition of receptor internalization and facilitation of beta 1-adrenergic receptor interaction with N-methyl-D-aspartate receptors. J Biol Chem. 2000 Dec 8;275(49):38659-66.
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| REF 14 |
beta 1-adrenergic receptor association with the synaptic scaffolding protein membrane-associated guanylate kinase inverted-2 (MAGI-2). Differential regulation of receptor internalization by MAGI-2 and PSD-95. J Biol Chem. 2001 Nov 2;276(44):41310-7.
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| REF 15 |
The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3596-601.
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| REF 16 |
Regulation of neuregulin signaling by PSD-95 interacting with ErbB4 at CNS synapses. Neuron. 2000 May;26(2):443-55.
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| REF 17 |
Proteasome-independent polyubiquitin linkage regulates synapse scaffolding, efficacy, and plasticity. Proc Natl Acad Sci U S A. 2017 Oct 10;114(41):E8760-E8769.
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| REF 18 |
Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD-95/SAP90. A possible regulatory role in molecular clustering at synaptic sites. J Biol Chem. 1999 Feb 26;274(9):5782-90.
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| REF 19 |
CAPON: a protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95. Neuron. 1998 Jan;20(1):115-24.
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| REF 20 |
Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains. Cell. 1996 Mar 8;84(5):757-67.
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| REF 21 |
Selective interaction of megalin with postsynaptic density-95 (PSD-95)-like membrane-associated guanylate kinase (MAGUK) proteins. Biochem J. 2003 Jul 15;373(Pt 2):381-91.
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| REF 22 |
Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction. J Biol Chem. 2000 Aug 18;275(33):25616-24.
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| REF 23 |
GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules. J Cell Biol. 1997 Feb 10;136(3):669-78.
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| REF 24 |
SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density. J Biol Chem. 1997 May 2;272(18):11943-51.
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