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Atlas of coronavirus replicase structure
The international response to SARS-CoV has produced an outstanding number of protein structures in a very short time. This review summarizes the findings of functional and structural studies including those derived from cryoelectron microscopy, small angle X-ray scattering, NMR spectroscopy, and X-r...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier B.V.
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114488/ https://www.ncbi.nlm.nih.gov/pubmed/24355834 http://dx.doi.org/10.1016/j.virusres.2013.12.004 |
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author | Neuman, Benjamin W. Chamberlain, Peter Bowden, Fern Joseph, Jeremiah |
author_facet | Neuman, Benjamin W. Chamberlain, Peter Bowden, Fern Joseph, Jeremiah |
author_sort | Neuman, Benjamin W. |
collection | PubMed |
description | The international response to SARS-CoV has produced an outstanding number of protein structures in a very short time. This review summarizes the findings of functional and structural studies including those derived from cryoelectron microscopy, small angle X-ray scattering, NMR spectroscopy, and X-ray crystallography, and incorporates bioinformatics predictions where no structural data is available. Structures that shed light on the function and biological roles of the proteins in viral replication and pathogenesis are highlighted. The high percentage of novel protein folds identified among SARS-CoV proteins is discussed. |
format | Online Article Text |
id | pubmed-7114488 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71144882020-04-02 Atlas of coronavirus replicase structure Neuman, Benjamin W. Chamberlain, Peter Bowden, Fern Joseph, Jeremiah Virus Res Article The international response to SARS-CoV has produced an outstanding number of protein structures in a very short time. This review summarizes the findings of functional and structural studies including those derived from cryoelectron microscopy, small angle X-ray scattering, NMR spectroscopy, and X-ray crystallography, and incorporates bioinformatics predictions where no structural data is available. Structures that shed light on the function and biological roles of the proteins in viral replication and pathogenesis are highlighted. The high percentage of novel protein folds identified among SARS-CoV proteins is discussed. Elsevier B.V. 2014-12-19 2013-12-16 /pmc/articles/PMC7114488/ /pubmed/24355834 http://dx.doi.org/10.1016/j.virusres.2013.12.004 Text en Copyright © 2013 Elsevier B.V. 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 Neuman, Benjamin W. Chamberlain, Peter Bowden, Fern Joseph, Jeremiah Atlas of coronavirus replicase structure |
title | Atlas of coronavirus replicase structure |
title_full | Atlas of coronavirus replicase structure |
title_fullStr | Atlas of coronavirus replicase structure |
title_full_unstemmed | Atlas of coronavirus replicase structure |
title_short | Atlas of coronavirus replicase structure |
title_sort | atlas of coronavirus replicase structure |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114488/ https://www.ncbi.nlm.nih.gov/pubmed/24355834 http://dx.doi.org/10.1016/j.virusres.2013.12.004 |
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