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Kurt Lingenhoehl

Researcher at Novartis

Publications -  26
Citations -  2984

Kurt Lingenhoehl is an academic researcher from Novartis. The author has contributed to research in topics: Agonist & GABAB receptor. The author has an hindex of 17, co-authored 26 publications receiving 2857 citations. Previous affiliations of Kurt Lingenhoehl include Ciba Specialty Chemicals.

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Role of NMDA Receptor Subtypes in Governing the Direction of Hippocampal Synaptic Plasticity

TL;DR: Using hippocampal slice preparations, it is shown that selectively blocking NMDARs that contain the NR2B subunit abolishes the induction of LTD but not LTP, demonstrating that distinct N MDAR subunits are critical factors that determine the polarity of synaptic plasticity.
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Positive allosteric modulation of native and recombinant gamma-aminobutyric acid(B) receptors by 2,6-Di-tert-butyl-4-(3-hydroxy-2,2-dimethyl-propyl)-phenol (CGP7930) and its aldehyde analog CGP13501.

TL;DR: It is shown that CGP7930 enhances the inhibitory effect of L-baclofen on the oscillatory activity of cultured cortical neurons and may represent a novel means of therapeutic interference with the GABA-ergic system.
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5-Phosphonomethylquinoxalinediones as competitive NMDA receptor antagonists with a preference for the human 1A/2A, rather than 1A/2B receptor composition.

TL;DR: NMDA antagonists derived from 5-phosphonomethyl-1,4-dihydroquinoxaline-2,3-dione (3a) are potent anticonvulsant agents, and display strong protective effects in the electroshock-induced convulsion assay in mice.
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Behavioral Characterization of the Novel GABAB Receptor-Positive Modulator GS39783 (N,N′-Dicyclopentyl-2-methylsulfanyl-5-nitro-pyrimidine-4,6-diamine): Anxiolytic-Like Activity without Side Effects Associated with Baclofen or Benzodiazepines

TL;DR: The data obtained here suggest that positive modulation of GABAB receptors may serve as a novel therapeutic strategy for the development of anxiolytics, with a superior side effect profile to both baclofen and benzodiazepines.
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γ-Hydroxybutyrate is a weak agonist at recombinant GABAB receptors

TL;DR: Results indicate that GHB is a weak partial agonist at the GABA binding site of GABA(B)R1/R2, and this hypothesis is consistent with previous reports on GHB and gamma-aminobutyric acid.