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Virus membrane-fusion proteins: more than one way to make a hairpin
Structure–function studies have defined two classes of viral membrane-fusion proteins that have radically different architectures but adopt a similar overall 'hairpin' conformation to induce fusion of the viral and cellular membranes and therefore initiate infection. In both classes, the h...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7097298/ https://www.ncbi.nlm.nih.gov/pubmed/16357862 http://dx.doi.org/10.1038/nrmicro1326 |
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author | Kielian, Margaret Rey, Félix A. |
author_facet | Kielian, Margaret Rey, Félix A. |
author_sort | Kielian, Margaret |
collection | PubMed |
description | Structure–function studies have defined two classes of viral membrane-fusion proteins that have radically different architectures but adopt a similar overall 'hairpin' conformation to induce fusion of the viral and cellular membranes and therefore initiate infection. In both classes, the hairpin conformation is achieved after a conformational change is triggered by interaction with the target cell. This review will focus in particular on the properties of the more recently described class II proteins. |
format | Online Article Text |
id | pubmed-7097298 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-70972982020-03-26 Virus membrane-fusion proteins: more than one way to make a hairpin Kielian, Margaret Rey, Félix A. Nat Rev Microbiol Article Structure–function studies have defined two classes of viral membrane-fusion proteins that have radically different architectures but adopt a similar overall 'hairpin' conformation to induce fusion of the viral and cellular membranes and therefore initiate infection. In both classes, the hairpin conformation is achieved after a conformational change is triggered by interaction with the target cell. This review will focus in particular on the properties of the more recently described class II proteins. Nature Publishing Group UK 2006 /pmc/articles/PMC7097298/ /pubmed/16357862 http://dx.doi.org/10.1038/nrmicro1326 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 Kielian, Margaret Rey, Félix A. Virus membrane-fusion proteins: more than one way to make a hairpin |
title | Virus membrane-fusion proteins: more than one way to make a hairpin |
title_full | Virus membrane-fusion proteins: more than one way to make a hairpin |
title_fullStr | Virus membrane-fusion proteins: more than one way to make a hairpin |
title_full_unstemmed | Virus membrane-fusion proteins: more than one way to make a hairpin |
title_short | Virus membrane-fusion proteins: more than one way to make a hairpin |
title_sort | virus membrane-fusion proteins: more than one way to make a hairpin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7097298/ https://www.ncbi.nlm.nih.gov/pubmed/16357862 http://dx.doi.org/10.1038/nrmicro1326 |
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