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Potential targets for anti-SARS drugs in the structural proteins from SARS related coronavirus

This is a further study on the severe acute respiratory syndrome (SARS) using the probabilistic models. The purpose was to define the potential targets for anti-SARS drugs in the structural proteins from human SARS related coronavirus (SARS-CoV) while knowing little about the functional sites and po...

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Detalles Bibliográficos
Autores principales: Wu, Guang, Yan, Shaomin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Inc. 2004
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7124239/
https://www.ncbi.nlm.nih.gov/pubmed/15203235
http://dx.doi.org/10.1016/j.peptides.2004.03.002
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author Wu, Guang
Yan, Shaomin
author_facet Wu, Guang
Yan, Shaomin
author_sort Wu, Guang
collection PubMed
description This is a further study on the severe acute respiratory syndrome (SARS) using the probabilistic models. The purpose was to define the potential targets for anti-SARS drugs in the structural proteins from human SARS related coronavirus (SARS-CoV) while knowing little about the functional sites and possible mutations in these proteins. From a probabilistic viewpoint, we can theoretically select the amino acid pairs as potential candidates for anti-SARS drugs. These candidates have a greater chance of colliding with anti-SARS drugs, are more likely to link with the protein functions and are less vulnerable to mutations.
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spelling pubmed-71242392020-04-08 Potential targets for anti-SARS drugs in the structural proteins from SARS related coronavirus Wu, Guang Yan, Shaomin Peptides Article This is a further study on the severe acute respiratory syndrome (SARS) using the probabilistic models. The purpose was to define the potential targets for anti-SARS drugs in the structural proteins from human SARS related coronavirus (SARS-CoV) while knowing little about the functional sites and possible mutations in these proteins. From a probabilistic viewpoint, we can theoretically select the amino acid pairs as potential candidates for anti-SARS drugs. These candidates have a greater chance of colliding with anti-SARS drugs, are more likely to link with the protein functions and are less vulnerable to mutations. Elsevier Inc. 2004-06 2004-04-10 /pmc/articles/PMC7124239/ /pubmed/15203235 http://dx.doi.org/10.1016/j.peptides.2004.03.002 Text en Copyright © 2004 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Wu, Guang
Yan, Shaomin
Potential targets for anti-SARS drugs in the structural proteins from SARS related coronavirus
title Potential targets for anti-SARS drugs in the structural proteins from SARS related coronavirus
title_full Potential targets for anti-SARS drugs in the structural proteins from SARS related coronavirus
title_fullStr Potential targets for anti-SARS drugs in the structural proteins from SARS related coronavirus
title_full_unstemmed Potential targets for anti-SARS drugs in the structural proteins from SARS related coronavirus
title_short Potential targets for anti-SARS drugs in the structural proteins from SARS related coronavirus
title_sort potential targets for anti-sars drugs in the structural proteins from sars related coronavirus
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7124239/
https://www.ncbi.nlm.nih.gov/pubmed/15203235
http://dx.doi.org/10.1016/j.peptides.2004.03.002
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