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David J. Singel
Researcher at Montana State University
Publications - 104
Citations - 15764
David J. Singel is an academic researcher from Montana State University. The author has contributed to research in topics: Electron paramagnetic resonance & Nitric oxide. The author has an hindex of 39, co-authored 104 publications receiving 15273 citations. Previous affiliations of David J. Singel include Duke University & Brigham and Women's Hospital.
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Journal ArticleDOI
Biochemistry of nitric oxide and its redox-activated forms
TL;DR: The integration of this chemistry with current perspectives of NO biology illuminates many aspects of NO biochemistry, including the enzymatic mechanism of synthesis, the mode of transport and targeting in biological systems, the means by which its toxicity is mitigated, and the function-regulating interaction with target proteins.
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A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds
Stuart A. Lipton,Yun-Beom Choi,Yun-Beom Choi,Zhuo Hua Pan,Zhuo Hua Pan,Sizheng Z. Lei,Sizheng Z. Lei,Huei-Sheng Vincent Chen,Huei-Sheng Vincent Chen,Nikolaus J. Sucher,Nikolaus J. Sucher,Joseph Loscalzo,Joseph Loscalzo,David J. Singel,Jonathan S. Stamler,Jonathan S. Stamler +15 more
TL;DR: It is reported that NO.-mediated neurotoxicity is engendered, at least in part, by reaction with superoxide anion (O.-2), apparently leading to formation of peroxynitrite (ONOO−), and not by NO.
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S-nitrosylation of proteins with nitric oxide: synthesis and characterization of biologically active compounds
Jonathan S. Stamler,Daniel I. Simon,John A. Osborne,Mark E. Mullins,Omar Jaraki,Thomas Michel,David J. Singel,Joseph Loscalzo +7 more
TL;DR: It is demonstrated that S-nitroso proteins form readily under physiologic conditions and possess EDRF-like effects of vasodilation and platelet inhibition, suggesting that S -nitrosothiol groups in proteins may serve as intermediates in the cellular metabolism of NO and raise the possibility of an additional type of cellular regulatory mechanism.
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Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin.
Jonathan S. Stamler,Omar Jaraki,Jihan K. Osborne,Daniel I. Simon,John F. Keaney,Joseph A. Vita,David J. Singel,C R Valeri,Joseph Loscalzo +8 more
TL;DR: It is found that naturally produced nitric oxide circulates in plasma primarily complexed in S-nitrosothiol species, principal among which is S-Nitroso-serum albumin, which likely serves as a reservoir with which plasma levels of highly reactive, short-lived free nitrics can be regulated for the maintenance of vascular tone.
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Adverse vascular effects of homocysteine are modulated by endothelium-derived relaxing factor and related oxides of nitrogen.
Jonathan S. Stamler,John A. Osborne,Omar Jaraki,LeRoy E. Rabbani,Mark E. Mullins,David J. Singel,Joseph Loscalzo +6 more
TL;DR: These results suggest that the normal endothelium modulates the potential, adverse effects of homocysteine by releasing EDRF and forming the adduct S-NO-homocysteines, a potent antiplatelet agent and vasodilator.