D
David S. Bredt
Researcher at Johnson & Johnson
Publications - 224
Citations - 63974
David S. Bredt is an academic researcher from Johnson & Johnson. The author has contributed to research in topics: Nitric oxide synthase & Nitric oxide. The author has an hindex of 107, co-authored 223 publications receiving 62332 citations. Previous affiliations of David S. Bredt include Johns Hopkins University & Georgetown University Medical Center.
Papers
More filters
Journal ArticleDOI
Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs.
TL;DR: The requirements for PDZ domains and a C-terminal domain of PSD-95 indicate that protein-protein interactions cooperate with lipid interactions in synaptic targeting, suggesting that a specialized synaptic lipid environment mediates postsynaptic clustering.
Journal ArticleDOI
The localization of nitric oxide synthase in the rat eye and related cranial ganglia
TL;DR: Nitric oxide synthase thus localizes to peripheral ocular nerve fibers, chiefly parasympathetic in nature and derived from the pterygopalatine ganglion, and to several cell types in the retina, implying potential neurotransmitter functions for nitric oxide in this tissue.
Journal ArticleDOI
Projections and chemical coding of neurons with immunoreactivity for nitric oxide synthase in the guinea-pig small intestine
Marcello Costa,John B. Furness,S. Pompolo,Simon J. H. Brookes,Joel C. Bornstein,David S. Bredt,Solomon H. Snyder +6 more
TL;DR: It is concluded that nitric oxide synthase is located in a sub-population of enteric neurons, amongst which are inhibitory motor neurons that supply the circular muscle layer.
Journal ArticleDOI
Synaptic signaling by nitric oxide
Jay E. Brenman,David S. Bredt +1 more
TL;DR: Characterization of this pathway has provided new insights into the role of NO in brain physiology and disease.
Journal ArticleDOI
N-Terminal Palmitoylation of PSD-95 Regulates Association with Cell Membranes and Interaction with K+ Channel Kv1.4
J. Rick Topinka,David S. Bredt +1 more
TL;DR: This work identifies palmitoylation as a critical regulatory mechanism for receptor interactions with PSD-95, and shows it to partition as an integral membrane protein in brain homogenates.