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Lindsey E. McQuade

Researcher at Massachusetts Institute of Technology

Publications -  21
Citations -  1371

Lindsey E. McQuade is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Dopaminergic & Nucleus accumbens. The author has an hindex of 15, co-authored 21 publications receiving 1277 citations. Previous affiliations of Lindsey E. McQuade include Stanford University & McGill University.

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Bacillus anthracis-derived nitric oxide is essential for pathogen virulence and survival in macrophages.

TL;DR: It is demonstrated that pathogenic bacteria use their own NO as a key defense against the immune oxidative burst, thereby establishing bNOS as an essential virulence factor and representing an attractive antimicrobial target for treatment of anthrax and other infectious diseases.
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Bacterial Nitric-oxide Synthases Operate without a Dedicated Redox Partner

TL;DR: In this article, the authors demonstrate that bNOS enzymes from Bacillus subtilis and Bacillus anthracis can produce NO in living cells and accomplish this task by hijacking available cellular redox partners that are not normally committed to NO production.
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Fluorescent probes to investigate nitric oxide and other reactive nitrogen species in biology (truncated form: fluorescent probes of reactive nitrogen species).

TL;DR: Progress in the field of nitric oxide, peroxynitrite, and nitroxyl sensing promises to advance the knowledge of important signaling events involving these species and lead to a better understanding of oxidative biochemistry crucial to health and disease.
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Visualization of nitric oxide production in the mouse main olfactory bulb by a cell-trappable copper(II) fluorescent probe

TL;DR: The visualization of NO production using fluorescence in tissue slices of the mouse main olfactory bulb is reported, using a novel, cell-trappable probe for intracellular nitric oxide detection based on a symmetric scaffold with two NO-reactive sites.
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Detecting and understanding the roles of nitric oxide in biology.

TL;DR: The studies reveal that NO disassembles the Fe-S clusters to form dinitrosyl iron complexes, and this work employs synthetic model complexes of iron-sulfur clusters to probe their reactivity toward nitric oxide as biomimics of the active sites of Iron-Sulfur proteins.