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DLG4 — NOS1
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
NOS1
—
DLG4
(direct interaction, two hybrid)
Brenman et al., Cell 1996*
-
IRef Biogrid Interaction:
NOS1
—
DLG4
(physical association, affinity chromatography technology)
Jaffrey et al., Neuron 1998*
-
IRef Biogrid Interaction:
NOS1
—
DLG4
(association, biochemical)
Brenman et al., Cell 1996*
-
IRef Biogrid Interaction:
NOS1
—
DLG4
(direct interaction, pull down)
Brenman et al., Cell 1996*
-
IRef Hprd Interaction:
DLG4
—
NOS1
(two hybrid)
Christopherson et al., J Biol Chem 1999*, Brenman et al., Cell 1996*, Jaffrey et al., Neuron 1998*
-
IRef Hprd Interaction:
DLG4
—
NOS1
(in vitro)
Christopherson et al., J Biol Chem 1999*, Brenman et al., Cell 1996*, Jaffrey et al., Neuron 1998*
-
IRef Hprd Interaction:
DLG4
—
NOS1
(in vivo)
Christopherson et al., J Biol Chem 1999*, Brenman et al., Cell 1996*, Jaffrey et al., Neuron 1998*
-
IRef Ophid Interaction:
NOS1
—
DLG4
(aggregation, confirmational text mining)
Brenman et al., Cell 1996*
-
IRef Ophid Interaction:
NOS1
—
DLG4
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Yan et al., Neurosci Lett 2004
(Brain Ischemia) :
Postsynaptic density protein 95 mediates Ca2+/calmodulin dependent protein kinase II-activated serine phosphorylation of neuronal
nitric oxide synthase during brain ischemia in rat hippocampus
Cao et al., J Cell Biol 2005
:
Although the postsynaptic density protein PSD95 can recruit the calcium dependent
neuronal NO synthase (nNOS) to the mouth of the calcium-permeable NMDA receptor, and depletion of
PSD95 inhibits excitotoxicity, the possibility that selective uncoupling of nNOS from PSD95 might be neuroprotective is unexplored