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Hitoshi Kurose

Researcher at Duke University

Publications -  10
Citations -  1307

Hitoshi Kurose is an academic researcher from Duke University. The author has contributed to research in topics: Receptor & Interleukin 10 receptor, alpha subunit. The author has an hindex of 10, co-authored 10 publications receiving 1289 citations. Previous affiliations of Hitoshi Kurose include Howard Hughes Medical Institute & University of Tokyo.

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Journal ArticleDOI

Simultaneous coupling of alpha 2-adrenergic receptors to two G-proteins with opposing effects. Subtype-selective coupling of alpha 2C10, alpha 2C4, and alpha 2C2 adrenergic receptors to Gi and Gs.

TL;DR: It is observed that in the presence of low concentrations of the alpha 2AR agonist UK-14304, alpha 2C10 mediated inhibition of adenylyl cyclase activity, whereas at high concentrations of agonist,alpha 2C 10 mediated stimulation of adencylylcyclase activity.
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Constitutively active mutants of the alpha 2-adrenergic receptor.

TL;DR: The findings strengthen the idea that constitutively active adrenergic receptors mimic the "active" state of a G protein-coupled receptor adopting conformations similar to those induced by agonist when it binds to wild type receptors.
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Perikaryal and synaptic localization ofα2A-adrenergic receptor-like immunoreactivity

TL;DR: The results indicate that the A-subtype ofα2AR is distributed widely within brain and reflects the presence of newly synthesizedα2AAR in perikarya as well as those receptors along the plasma membrane ofperikarya, dendritic trunks and spines; and α2A AR in LC may operate as heteroreceptors on non-catecholaminergic terminals aswell as autoreceptor on noradrenergic terminals.
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Sites in the third intracellular loop of the alpha 2A-adrenergic receptor confer short term agonist-promoted desensitization. Evidence for a receptor kinase-mediated mechanism.

TL;DR: Long term agonist-induced desensitization of alpha 2AAR was found to be due in part to a decrease in the amount of cellular Gi, which was not dependent on receptor third loop phosphorylation sites.
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Tyrosine phosphorylation of G protein alpha subunits by pp60c-src

TL;DR: Heterotrimeric G proteins may represent a previously unappreciated class of potential substrates for pp60c-src and G proteins with functional consequences, and are explored in this study.