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David M. Weiner

Researcher at ACADIA Pharmaceuticals Inc.

Publications -  54
Citations -  3381

David M. Weiner is an academic researcher from ACADIA Pharmaceuticals Inc.. The author has contributed to research in topics: Receptor & 5-HT5A receptor. The author has an hindex of 26, co-authored 45 publications receiving 3230 citations. Previous affiliations of David M. Weiner include Laboratory of Molecular Biology & University of California, San Diego.

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Human dopamine D1 receptor encoded by an intronless gene on chromosome 5.

TL;DR: The cloning of the D1 receptor gene is reported, which resides on an intronless region on the long arm of chromosome 5, near two other members of the G-linked receptor family, and binds drugs with affinities identical to the native human D1 receptors.
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D1 and D2 dopamine receptor mRNA in rat brain

TL;DR: Insight is provided into the neuroanatomical basis of the differential effects of drugs that act on D1 or D2 receptors by mapping the cellular expression of the corresponding mRNAs in rat brain by in situ hybridization histochemistry.
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Expression of muscarinic acetylcholine and dopamine receptor mRNAs in rat basal ganglia.

TL;DR: Detailed anatomical evidence is provided for the identity of the receptor subtypes which mediate the diverse effects of muscarinic and dopaminergic drugs on basal ganglia function.
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Intrinsic Efficacy of Antipsychotics at Human D2, D3, and D4 Dopamine Receptors: Identification of the Clozapine Metabolite N-Desmethylclozapine as a D2/D3 Partial Agonist

TL;DR: Using a cell-based functional assay, it is demonstrated that overexpression of Gαo induces constitutive activity in the human D2-like receptors (D2, D3, and D4) and it is proposed that bypassing clozapine blockade through direct administration of NDMC to patients may provide superior antipsychotic efficacy.
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Evidence for a model of agonist-induced activation of 5-hydroxytryptamine 2A serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6.

TL;DR: The results predict that the disruption of a strong ionic interaction between transmembrane helices 3 and 6 of 5-HT2A receptors is essential for agonist-induced receptor activation and, as recently predicted by ourselves and others, that this may represent a general mechanism of activation for many, but not all, G-protein-coupled receptors.