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Architecture of the SARS coronavirus prefusion spike

The emergence in 2003 of a new coronavirus (CoV) responsible for the atypical pneumonia termed severe acute respiratory syndrome (SARS) was a stark reminder that hitherto unknown viruses have the potential to cross species barriers to become new human pathogens. Here we describe the SARS-CoV 's...

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Detalles Bibliográficos
Autores principales: Beniac, Daniel R, Andonov, Anton, Grudeski, Elsie, Booth, Tim F
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group US 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7097490/
https://www.ncbi.nlm.nih.gov/pubmed/16845391
http://dx.doi.org/10.1038/nsmb1123
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author Beniac, Daniel R
Andonov, Anton
Grudeski, Elsie
Booth, Tim F
author_facet Beniac, Daniel R
Andonov, Anton
Grudeski, Elsie
Booth, Tim F
author_sort Beniac, Daniel R
collection PubMed
description The emergence in 2003 of a new coronavirus (CoV) responsible for the atypical pneumonia termed severe acute respiratory syndrome (SARS) was a stark reminder that hitherto unknown viruses have the potential to cross species barriers to become new human pathogens. Here we describe the SARS-CoV 'spike' structure determined by single-particle cryo-EM, along with the docked atomic structures of the receptor-binding domain and prefusion core. SUPPLEMENTARY INFORMATION: The online version of this article (doi:10.1038/nsmb1123) contains supplementary material, which is available to authorized users.
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spelling pubmed-70974902020-03-26 Architecture of the SARS coronavirus prefusion spike Beniac, Daniel R Andonov, Anton Grudeski, Elsie Booth, Tim F Nat Struct Mol Biol Article The emergence in 2003 of a new coronavirus (CoV) responsible for the atypical pneumonia termed severe acute respiratory syndrome (SARS) was a stark reminder that hitherto unknown viruses have the potential to cross species barriers to become new human pathogens. Here we describe the SARS-CoV 'spike' structure determined by single-particle cryo-EM, along with the docked atomic structures of the receptor-binding domain and prefusion core. SUPPLEMENTARY INFORMATION: The online version of this article (doi:10.1038/nsmb1123) contains supplementary material, which is available to authorized users. Nature Publishing Group US 2006-07-16 2006 /pmc/articles/PMC7097490/ /pubmed/16845391 http://dx.doi.org/10.1038/nsmb1123 Text en © Nature Publishing Group 2006 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Article
Beniac, Daniel R
Andonov, Anton
Grudeski, Elsie
Booth, Tim F
Architecture of the SARS coronavirus prefusion spike
title Architecture of the SARS coronavirus prefusion spike
title_full Architecture of the SARS coronavirus prefusion spike
title_fullStr Architecture of the SARS coronavirus prefusion spike
title_full_unstemmed Architecture of the SARS coronavirus prefusion spike
title_short Architecture of the SARS coronavirus prefusion spike
title_sort architecture of the sars coronavirus prefusion spike
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7097490/
https://www.ncbi.nlm.nih.gov/pubmed/16845391
http://dx.doi.org/10.1038/nsmb1123
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