Allosteric GABA(A) Receptor Modulators—A Review on the Most Recent Heterocyclic Chemotypes and Their Synthetic Accessibility †

GABA(A) receptor modulators are structurally almost as diverse as their target protein. A plethora of heterocyclic scaffolds has been described as modulating this extremely important receptor family. Some made it into clinical trials and, even on the market, some were dismissed. This review focuses...

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Autores principales: Vega Alanis, Blanca Angelica, Iorio, Maria Teresa, Silva, Luca L., Bampali, Konstantina, Ernst, Margot, Schnürch, Michael, Mihovilovic, Marko D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7070463/
https://www.ncbi.nlm.nih.gov/pubmed/32102309
http://dx.doi.org/10.3390/molecules25040999
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author Vega Alanis, Blanca Angelica
Iorio, Maria Teresa
Silva, Luca L.
Bampali, Konstantina
Ernst, Margot
Schnürch, Michael
Mihovilovic, Marko D.
author_facet Vega Alanis, Blanca Angelica
Iorio, Maria Teresa
Silva, Luca L.
Bampali, Konstantina
Ernst, Margot
Schnürch, Michael
Mihovilovic, Marko D.
author_sort Vega Alanis, Blanca Angelica
collection PubMed
description GABA(A) receptor modulators are structurally almost as diverse as their target protein. A plethora of heterocyclic scaffolds has been described as modulating this extremely important receptor family. Some made it into clinical trials and, even on the market, some were dismissed. This review focuses on the synthetic accessibility and potential for library synthesis of GABA(A) receptor modulators containing at least one heterocyclic scaffold, which were disclosed within the last 10 years.
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spelling pubmed-70704632020-03-19 Allosteric GABA(A) Receptor Modulators—A Review on the Most Recent Heterocyclic Chemotypes and Their Synthetic Accessibility † Vega Alanis, Blanca Angelica Iorio, Maria Teresa Silva, Luca L. Bampali, Konstantina Ernst, Margot Schnürch, Michael Mihovilovic, Marko D. Molecules Review GABA(A) receptor modulators are structurally almost as diverse as their target protein. A plethora of heterocyclic scaffolds has been described as modulating this extremely important receptor family. Some made it into clinical trials and, even on the market, some were dismissed. This review focuses on the synthetic accessibility and potential for library synthesis of GABA(A) receptor modulators containing at least one heterocyclic scaffold, which were disclosed within the last 10 years. MDPI 2020-02-24 /pmc/articles/PMC7070463/ /pubmed/32102309 http://dx.doi.org/10.3390/molecules25040999 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Vega Alanis, Blanca Angelica
Iorio, Maria Teresa
Silva, Luca L.
Bampali, Konstantina
Ernst, Margot
Schnürch, Michael
Mihovilovic, Marko D.
Allosteric GABA(A) Receptor Modulators—A Review on the Most Recent Heterocyclic Chemotypes and Their Synthetic Accessibility †
title Allosteric GABA(A) Receptor Modulators—A Review on the Most Recent Heterocyclic Chemotypes and Their Synthetic Accessibility †
title_full Allosteric GABA(A) Receptor Modulators—A Review on the Most Recent Heterocyclic Chemotypes and Their Synthetic Accessibility †
title_fullStr Allosteric GABA(A) Receptor Modulators—A Review on the Most Recent Heterocyclic Chemotypes and Their Synthetic Accessibility †
title_full_unstemmed Allosteric GABA(A) Receptor Modulators—A Review on the Most Recent Heterocyclic Chemotypes and Their Synthetic Accessibility †
title_short Allosteric GABA(A) Receptor Modulators—A Review on the Most Recent Heterocyclic Chemotypes and Their Synthetic Accessibility †
title_sort allosteric gaba(a) receptor modulators—a review on the most recent heterocyclic chemotypes and their synthetic accessibility †
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7070463/
https://www.ncbi.nlm.nih.gov/pubmed/32102309
http://dx.doi.org/10.3390/molecules25040999
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