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Jay L. Dinerman

Researcher at Johns Hopkins University

Publications -  16
Citations -  4217

Jay L. Dinerman is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Nitric oxide synthase & Nitric oxide. The author has an hindex of 13, co-authored 15 publications receiving 4166 citations. Previous affiliations of Jay L. Dinerman include Johns Hopkins University School of Medicine.

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Nitric oxide: A physiologic messenger

TL;DR: A noxious, unstable gas, nitric oxide, a byproduct of automobile exhaust, electric power stations, and lightning, was discovered in the body, where it participates in various functions, including suppression of pathogens, vasodilation, and neurotransmission, focusing on its clinical relevance.
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Endothelial nitric oxide synthase localized to hippocampal pyramidal cells: implications for synaptic plasticity

TL;DR: Using antibodies that react selectively with peptide sequences unique to endothelial nitric oxide synthase (eNOS), it is demonstrated that eNOS in hippocampal pyramidal cells may generate the NO that has been postulated as a retrograde messenger of long-term potentiation.
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Immunosuppressant FK506 enhances phosphorylation of nitric oxide synthase and protects against glutamate neurotoxicity.

TL;DR: In a stably transfected human kidney 293 cell line overexpressing the gene encoding nitric oxide synthase, FK506 inhibits the calcium ionophore A23187, stimulated increases in nitrite, and potentiates phorbol ester-mediated inhibition of nitrite formation, establishing nitricoxide synthase as a calcineurin substrate.
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Endothelial NOS and the blockade of LTP by NOS inhibitors in mice lacking neuronal NOS

TL;DR: Immunocytochemical studies indicate that in the nNOS- mice as in wild-type mice, the endothelial form of NOS (eNOS) is expressed in CA1 neurons, suggesting that eNOS generates NO within the postsynaptic cell during LTP, suggesting the importance of NO in hippocampal synaptic plasticity.
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Heme oxygenase 2: endothelial and neuronal localization and role in endothelium-dependent relaxation

TL;DR: Tin protoporphyrin-9 is a selective inhibitor of HO with approximately 10-fold selectivity for HO over endothelial nitric oxide synthase (NOS) and soluble guanylyl cyclase, which implies complementary and possibly coordinated physiologic roles for these two mediators.