Regulation of influenza a virus nucleoprotein oligomerization by phosphorylation.
In the influenza virus ribonucleoprotein complex, the oligomerization of the nucleoprotein is mediated by an interaction between the tail-loop of one molecule and the groove of the neighboring molecule. In this study, we show that phosphorylation of a serine residue (S165) within the groove of influ...
| প্রধান লেখক: | , , , |
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| বিন্যাস: | Journal article |
| ভাষা: | English |
| প্রকাশিত: |
2015
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| _version_ | 1826267886322188288 |
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| author | Turrell, L Hutchinson, E Vreede, F Fodor, E |
| author_facet | Turrell, L Hutchinson, E Vreede, F Fodor, E |
| author_sort | Turrell, L |
| collection | OXFORD |
| description | In the influenza virus ribonucleoprotein complex, the oligomerization of the nucleoprotein is mediated by an interaction between the tail-loop of one molecule and the groove of the neighboring molecule. In this study, we show that phosphorylation of a serine residue (S165) within the groove of influenza A virus nucleoprotein inhibits oligomerization and, consequently, ribonucleoprotein activity and viral growth. We propose that nucleoprotein oligomerization in infected cells is regulated by reversible phosphorylation. |
| first_indexed | 2024-03-06T21:01:07Z |
| format | Journal article |
| id | oxford-uuid:3ae94fcb-49c1-4383-89c3-0a78dfae35c4 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:01:07Z |
| publishDate | 2015 |
| record_format | dspace |
| spelling | oxford-uuid:3ae94fcb-49c1-4383-89c3-0a78dfae35c42022-03-26T14:04:24ZRegulation of influenza a virus nucleoprotein oligomerization by phosphorylation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3ae94fcb-49c1-4383-89c3-0a78dfae35c4EnglishSymplectic Elements at Oxford2015Turrell, LHutchinson, EVreede, FFodor, EIn the influenza virus ribonucleoprotein complex, the oligomerization of the nucleoprotein is mediated by an interaction between the tail-loop of one molecule and the groove of the neighboring molecule. In this study, we show that phosphorylation of a serine residue (S165) within the groove of influenza A virus nucleoprotein inhibits oligomerization and, consequently, ribonucleoprotein activity and viral growth. We propose that nucleoprotein oligomerization in infected cells is regulated by reversible phosphorylation. |
| spellingShingle | Turrell, L Hutchinson, E Vreede, F Fodor, E Regulation of influenza a virus nucleoprotein oligomerization by phosphorylation. |
| title | Regulation of influenza a virus nucleoprotein oligomerization by phosphorylation. |
| title_full | Regulation of influenza a virus nucleoprotein oligomerization by phosphorylation. |
| title_fullStr | Regulation of influenza a virus nucleoprotein oligomerization by phosphorylation. |
| title_full_unstemmed | Regulation of influenza a virus nucleoprotein oligomerization by phosphorylation. |
| title_short | Regulation of influenza a virus nucleoprotein oligomerization by phosphorylation. |
| title_sort | regulation of influenza a virus nucleoprotein oligomerization by phosphorylation |
| work_keys_str_mv | AT turrelll regulationofinfluenzaavirusnucleoproteinoligomerizationbyphosphorylation AT hutchinsone regulationofinfluenzaavirusnucleoproteinoligomerizationbyphosphorylation AT vreedef regulationofinfluenzaavirusnucleoproteinoligomerizationbyphosphorylation AT fodore regulationofinfluenzaavirusnucleoproteinoligomerizationbyphosphorylation |