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Acetylcholinesterase: The “Hub” for Neurodegenerative Diseases and Chemical Weapons Convention
This article describes acetylcholinesterase (AChE), an enzyme involved in parasympathetic neurotransmission, its activity, and how its inhibition can be pharmacologically useful for treating dementia, caused by Alzheimer’s disease, or as a warfare method due to the action of nerve agents. The chemic...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7175162/ https://www.ncbi.nlm.nih.gov/pubmed/32155996 http://dx.doi.org/10.3390/biom10030414 |
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author | Cavalcante, Samir F. de A. Simas, Alessandro B. C. Barcellos, Marcos C. de Oliveira, Victor G. M. Sousa, Roberto B. Cabral, Paulo A. de M. Kuča, Kamil França, Tanos C. C. |
author_facet | Cavalcante, Samir F. de A. Simas, Alessandro B. C. Barcellos, Marcos C. de Oliveira, Victor G. M. Sousa, Roberto B. Cabral, Paulo A. de M. Kuča, Kamil França, Tanos C. C. |
author_sort | Cavalcante, Samir F. de A. |
collection | PubMed |
description | This article describes acetylcholinesterase (AChE), an enzyme involved in parasympathetic neurotransmission, its activity, and how its inhibition can be pharmacologically useful for treating dementia, caused by Alzheimer’s disease, or as a warfare method due to the action of nerve agents. The chemical concepts related to the irreversible inhibition of AChE, its reactivation, and aging are discussed, along with a relationship to the current international legislation on chemical weapons. |
format | Online Article Text |
id | pubmed-7175162 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-71751622020-04-28 Acetylcholinesterase: The “Hub” for Neurodegenerative Diseases and Chemical Weapons Convention Cavalcante, Samir F. de A. Simas, Alessandro B. C. Barcellos, Marcos C. de Oliveira, Victor G. M. Sousa, Roberto B. Cabral, Paulo A. de M. Kuča, Kamil França, Tanos C. C. Biomolecules Review This article describes acetylcholinesterase (AChE), an enzyme involved in parasympathetic neurotransmission, its activity, and how its inhibition can be pharmacologically useful for treating dementia, caused by Alzheimer’s disease, or as a warfare method due to the action of nerve agents. The chemical concepts related to the irreversible inhibition of AChE, its reactivation, and aging are discussed, along with a relationship to the current international legislation on chemical weapons. MDPI 2020-03-07 /pmc/articles/PMC7175162/ /pubmed/32155996 http://dx.doi.org/10.3390/biom10030414 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 Cavalcante, Samir F. de A. Simas, Alessandro B. C. Barcellos, Marcos C. de Oliveira, Victor G. M. Sousa, Roberto B. Cabral, Paulo A. de M. Kuča, Kamil França, Tanos C. C. Acetylcholinesterase: The “Hub” for Neurodegenerative Diseases and Chemical Weapons Convention |
title | Acetylcholinesterase: The “Hub” for Neurodegenerative Diseases and Chemical Weapons Convention |
title_full | Acetylcholinesterase: The “Hub” for Neurodegenerative Diseases and Chemical Weapons Convention |
title_fullStr | Acetylcholinesterase: The “Hub” for Neurodegenerative Diseases and Chemical Weapons Convention |
title_full_unstemmed | Acetylcholinesterase: The “Hub” for Neurodegenerative Diseases and Chemical Weapons Convention |
title_short | Acetylcholinesterase: The “Hub” for Neurodegenerative Diseases and Chemical Weapons Convention |
title_sort | acetylcholinesterase: the “hub” for neurodegenerative diseases and chemical weapons convention |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7175162/ https://www.ncbi.nlm.nih.gov/pubmed/32155996 http://dx.doi.org/10.3390/biom10030414 |
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