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Timothy J. McCabe

Researcher at Yale University

Publications -  18
Citations -  5027

Timothy J. McCabe is an academic researcher from Yale University. The author has contributed to research in topics: Enos & Phosphorylation. The author has an hindex of 15, co-authored 18 publications receiving 4880 citations. Previous affiliations of Timothy J. McCabe include University of Texas Southwestern Medical Center & University of Texas Health Science Center at San Antonio.

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Journal ArticleDOI

Regulation of endothelium-derived nitric oxide production by the protein kinase Akt.

TL;DR: It is shown that the serine/threonine protein kinase Akt (protein kinase B) can directly phosphorylate eNOS on serine 1179 and activate the enzyme, leading to NO production, whereas mutant eN OS (S1179A) is resistant to phosphorylation and activation by Akt.
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Enhanced electron flux and reduced calmodulin dissociation may explain "calcium-independent" eNOS activation by phosphorylation.

TL;DR: Results suggest that a negative charge imposed at serine 1179, either by phosphorylation or by replacement with aspartate, increases eNOS catalytic activity by increasing electron flux at the reductase domain and by reducing calmodulin dissociation from activated eN OS when calcium levels are low.
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Neuronal nitric oxide synthase and dystrophin-deficient muscular dystrophy

TL;DR: Neuronal nitric oxide synthase (nNOS) in fast-twitch skeletal muscle fibers is primarily particulate in contrast to its greater solubility in brain, which may indicate a physiological role for NO in aging-related processes.
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Domain Mapping Studies Reveal That the M Domain of hsp90 Serves as a Molecular Scaffold to Regulate Akt-Dependent Phosphorylation of Endothelial Nitric Oxide Synthase and NO Release

TL;DR: It is demonstrated that stimulation of endothelial cells with vascular endothelial growth factor recruits eNOS and Akt to an adjacent region on the same domain of hsp90, thereby facilitating eN OS phosphorylation and enzyme activation.
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Reconstitution of an endothelial nitric-oxide synthase (eNOS), hsp90, and caveolin-1 complex in vitro. Evidence that hsp90 facilitates calmodulin stimulated displacement of eNOS from caveolin-1.

TL;DR: Results show that the actions of CaM on eNOS dissociation from caveolin are facilitated in the presence of hsp90, and eNos enzymatic activity is also less sensitive to inhibition by the caveolin scaffolding peptide when eN OS is prebound to hSp90.