ArticleACS medicinal chemistry letters2020
Structure-Functional-Selectivity Relationship Studies of Novel Apomorphine Analogs to Develop D1R/D2R Biased Ligands.
Article in ACS medicinal chemistry letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Apomorphine differentially engages the cAMP and β-arrestin signaling pathways relative to dopamine at human dopamine receptors.Journal of neural transmission (Vienna, Austria : 1996) · 2025Article
- Estimation of Dopamine DACS chemical neuroscience · 2025Article
- Perry Disease: Current Outlook and Advances in Drug Discovery Approach to Symptomatic Treatment.International journal of molecular sciences · 2024Review
- Natural Product-Inspired Dopamine Receptor Ligands.Journal of medicinal chemistry · 2024Review
- Computational insights into ligand-induced G protein and β-arrestin signaling of the dopamine D1 receptor.Journal of computer-aided molecular design · 2023Article
- Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Loss of dopamine neurons is central to the manifestation of Parkinson's disease motor symptoms. The dopamine precursor L-DOPA, the most commonly used therapeutic agent for Parkinson's disease, can restore normal movement yet cause side-effects such as dyskinesias upon prolonged administration. Dopamine D1 and D2 receptors activate G-protein- and arrestin-dependent signaling pathways that regulate various dopamine-dependent functions including locomotion. Studies have shown that shifting the balance of dopamine receptor signaling toward the arrestin pathway can be beneficial for inducing normal movement, while reducing dyskinesias. However, simultaneous activation of both D1 and D2Rs is required for robust locomotor activity. Thus, it is desirable to develop ligands targeting both D1 and D2Rs and their functional selectivity. Here, we report structure-functional-selectivity relationship (SFSR) studies of novel apomorphine analogs to identify structural motifs responsible for biased activity at both D1 and D2Rs.
Identifiers
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Registered trials
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