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Michael R. Kozlowski

Researcher at Bristol-Myers Squibb

Publications -  27
Citations -  880

Michael R. Kozlowski is an academic researcher from Bristol-Myers Squibb. The author has contributed to research in topics: Olfactory tubercle & Dopaminergic. The author has an hindex of 15, co-authored 27 publications receiving 867 citations. Previous affiliations of Michael R. Kozlowski include University of California, Irvine & Oregon Health & Science University.

Papers
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Journal ArticleDOI

Plasticity of neostriatal dopamine receptors after nigrostriatal injury: Relationship to recovery of sensorimotor functions and behavioral supersensitivity

TL;DR: The results suggest that a proliferation of DA receptors may contribute to the pharmacological supersensitivity and the recovery of function, and that these early receptor changes may be revealed with greater sensitivity using in vivo binding techniques.
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DNA synthesis and neuronal apoptosis caused by familial Alzheimer disease mutants of the amyloid precursor protein are mediated by the p21 activated kinase PAK3.

TL;DR: Data suggest that a normal signaling pathway mediated by the interaction of APP, PAK3, and Go is constitutively activated in neurons by FAD mutations in APP and that this activation causes cell cycle entry and consequent apoptosis.
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Plasticity of [14C]2-deoxy-d-glucose incorporation into neostriatum and related structures in response to dopamine neuron damage and apomorphine replacement

TL;DR: This autoradiographic technique can be used to demonstrate neostriatal output circuits that show altered metabolic activity in response to diminished or excessive forebrain dopamine receptor stimulation.
Patent

Dihydropyridine NPY antagonists: piperidine derivatives

TL;DR: A series of non-peptidergic antagonists of NPY have been synthesized and are comprised of piperidine and tetrahydropyridine derivatives of 4-phenyl-1,4-dihydroparidines of Formula I.
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The neurotoxic carboxy-terminal fragment of the Alzheimer amyloid precursor binds specifically to a neuronal cell surface molecule: pH dependence of the neurotoxicity and the binding

TL;DR: It is shown that beta APP-C104 synthesized in vitro binds specifically and with high affinity to the surface of NGF-treated PC12 cells and is dependent at least in part on the presence of a tyrosine residue that is a potential site of phosphorylation at the carboxy terminus of the fragment.