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Anthony J. Baucum

Researcher at Indiana University – Purdue University Indianapolis

Publications -  47
Citations -  1157

Anthony J. Baucum is an academic researcher from Indiana University – Purdue University Indianapolis. The author has contributed to research in topics: Phosphorylation & Ca2+/calmodulin-dependent protein kinase. The author has an hindex of 19, co-authored 42 publications receiving 1021 citations. Previous affiliations of Anthony J. Baucum include Indiana University & College of William & Mary.

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Alcohol exposure alters NMDAR function in the bed nucleus of the stria terminalis.

TL;DR: The hypothesis that NMDAR-mediated synaptic transmission is sensitized at key synapses in the extended amygdala and thus may be a suitable target for manipulation of the behavioral deficits associated with acute withdrawal from chronic alcohol exposure is supported.
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GluN2B subunit deletion reveals key role in acute and chronic ethanol sensitivity of glutamate synapses in bed nucleus of the stria terminalis

TL;DR: It is shown that chronic ethanol exposure enhances LTP in the BNST via paradoxical extrasynaptic NMDAR involvement and a unique role of Extrasynaptic GluN2B-containing receptors in facilitating LTP is suggested.
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Methamphetamine Increases Dopamine Transporter Higher Molecular Weight Complex Formation via a Dopamine- and Hyperthermia-Associated Mechanism

TL;DR: These data are the first to demonstrate higher molecular weight DAT complex formation in vivo and that such formation can be altered by both pharmacological and physiological manipulations.
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CaMKII regulates diacylglycerol lipase-α and striatal endocannabinoid signaling

TL;DR: A functional interaction between the 2-AG synthetic enzyme diacylglycerol lipase-α (DGLα) and calcium/calmodulin dependent protein kinase II (CaMKII) is identified, providing mechanistic insights into the molecular regulation of striatal endocannabinoid signaling with implications for physiological control of motor function.
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Quantitative Proteomics Analysis of CaMKII Phosphorylation and the CaMKII Interactome in the Mouse Forebrain

TL;DR: In this article, a mass spectrometry-based approach was used to identify Ca2+-dependent and independent in vitro autophosphorylation sites in recombinant CaMKIIα and CaMK IIβ.