Irreversible inhibitors of the 3C protease of Coxsackie virus through templated assembly of protein-binding fragments

Molecular fragments are useful tools in drug-discovery but they might be hard to identify due to their weak affinity to the targets. Here, the authors use a protein-templated assembly to design high affinity inhibitors of Coxsackie virus 3C protease, a pharmacological target against enteroviral infe...

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Autores principales:	Daniel Becker, Zuzanna Kaczmarska, Christoph Arkona, Robert Schulz, Carolin Tauber, Gerhard Wolber, Rolf Hilgenfeld, Miquel Coll, Jörg Rademann
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a53d99ca5b15420c94025185b9b89835
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spelling	oai:doaj.org-article:a53d99ca5b15420c94025185b9b898352021-12-02T14:40:15ZIrreversible inhibitors of the 3C protease of Coxsackie virus through templated assembly of protein-binding fragments10.1038/ncomms127612041-1723https://doaj.org/article/a53d99ca5b15420c94025185b9b898352016-09-01T00:00:00Zhttps://doi.org/10.1038/ncomms12761https://doaj.org/toc/2041-1723Molecular fragments are useful tools in drug-discovery but they might be hard to identify due to their weak affinity to the targets. Here, the authors use a protein-templated assembly to design high affinity inhibitors of Coxsackie virus 3C protease, a pharmacological target against enteroviral infections.Daniel BeckerZuzanna KaczmarskaChristoph ArkonaRobert SchulzCarolin TauberGerhard WolberRolf HilgenfeldMiquel CollJörg RademannNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Daniel Becker Zuzanna Kaczmarska Christoph Arkona Robert Schulz Carolin Tauber Gerhard Wolber Rolf Hilgenfeld Miquel Coll Jörg Rademann Irreversible inhibitors of the 3C protease of Coxsackie virus through templated assembly of protein-binding fragments
description	Molecular fragments are useful tools in drug-discovery but they might be hard to identify due to their weak affinity to the targets. Here, the authors use a protein-templated assembly to design high affinity inhibitors of Coxsackie virus 3C protease, a pharmacological target against enteroviral infections.
format	article
author	Daniel Becker Zuzanna Kaczmarska Christoph Arkona Robert Schulz Carolin Tauber Gerhard Wolber Rolf Hilgenfeld Miquel Coll Jörg Rademann
author_facet	Daniel Becker Zuzanna Kaczmarska Christoph Arkona Robert Schulz Carolin Tauber Gerhard Wolber Rolf Hilgenfeld Miquel Coll Jörg Rademann
author_sort	Daniel Becker
title	Irreversible inhibitors of the 3C protease of Coxsackie virus through templated assembly of protein-binding fragments
title_short	Irreversible inhibitors of the 3C protease of Coxsackie virus through templated assembly of protein-binding fragments
title_full	Irreversible inhibitors of the 3C protease of Coxsackie virus through templated assembly of protein-binding fragments
title_fullStr	Irreversible inhibitors of the 3C protease of Coxsackie virus through templated assembly of protein-binding fragments
title_full_unstemmed	Irreversible inhibitors of the 3C protease of Coxsackie virus through templated assembly of protein-binding fragments
title_sort	irreversible inhibitors of the 3c protease of coxsackie virus through templated assembly of protein-binding fragments
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/a53d99ca5b15420c94025185b9b89835
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Irreversible inhibitors of the 3C protease of Coxsackie virus through templated assembly of protein-binding fragments

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