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Foot-and-mouth disease virus 3C protease: Recent structural and functional insights into an antiviral target

The 3C protease from foot-and-mouth disease virus (FMDV 3C(pro)) is critical for viral pathogenesis, having vital roles in both the processing of the polyprotein precursor and RNA replication. Although recent structural and functional studies have revealed new insights into the mechanism and functio...

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Autores principales: Curry, Stephen, Roqué-Rosell, Núria, Zunszain, Patricia A., Leatherbarrow, Robin J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7185863/
https://www.ncbi.nlm.nih.gov/pubmed/16979372
http://dx.doi.org/10.1016/j.biocel.2006.07.006
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author Curry, Stephen
Roqué-Rosell, Núria
Zunszain, Patricia A.
Leatherbarrow, Robin J.
author_facet Curry, Stephen
Roqué-Rosell, Núria
Zunszain, Patricia A.
Leatherbarrow, Robin J.
author_sort Curry, Stephen
collection PubMed
description The 3C protease from foot-and-mouth disease virus (FMDV 3C(pro)) is critical for viral pathogenesis, having vital roles in both the processing of the polyprotein precursor and RNA replication. Although recent structural and functional studies have revealed new insights into the mechanism and function of the enzyme, key questions remain that must be addressed before the potential of FMDV 3C(pro) as an antiviral drug target can be realised.
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spelling pubmed-71858632020-04-28 Foot-and-mouth disease virus 3C protease: Recent structural and functional insights into an antiviral target Curry, Stephen Roqué-Rosell, Núria Zunszain, Patricia A. Leatherbarrow, Robin J. Int J Biochem Cell Biol Molecules in Focus The 3C protease from foot-and-mouth disease virus (FMDV 3C(pro)) is critical for viral pathogenesis, having vital roles in both the processing of the polyprotein precursor and RNA replication. Although recent structural and functional studies have revealed new insights into the mechanism and function of the enzyme, key questions remain that must be addressed before the potential of FMDV 3C(pro) as an antiviral drug target can be realised. Elsevier Ltd. 2007 2006-08-14 /pmc/articles/PMC7185863/ /pubmed/16979372 http://dx.doi.org/10.1016/j.biocel.2006.07.006 Text en Copyright © 2006 Elsevier Ltd. 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 Molecules in Focus
Curry, Stephen
Roqué-Rosell, Núria
Zunszain, Patricia A.
Leatherbarrow, Robin J.
Foot-and-mouth disease virus 3C protease: Recent structural and functional insights into an antiviral target
title Foot-and-mouth disease virus 3C protease: Recent structural and functional insights into an antiviral target
title_full Foot-and-mouth disease virus 3C protease: Recent structural and functional insights into an antiviral target
title_fullStr Foot-and-mouth disease virus 3C protease: Recent structural and functional insights into an antiviral target
title_full_unstemmed Foot-and-mouth disease virus 3C protease: Recent structural and functional insights into an antiviral target
title_short Foot-and-mouth disease virus 3C protease: Recent structural and functional insights into an antiviral target
title_sort foot-and-mouth disease virus 3c protease: recent structural and functional insights into an antiviral target
topic Molecules in Focus
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7185863/
https://www.ncbi.nlm.nih.gov/pubmed/16979372
http://dx.doi.org/10.1016/j.biocel.2006.07.006
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