Temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infection
Here, Hashimoto et al. apply mass spectrometry-based thermal proximity coaggregation to characterize the temporal dynamics of virus-host protein-protein interactions during human cytomegalovirus (HCMV) infection, uncovering proviral functions including the internalization of the HCMV receptor integr...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2020-02-01
|
| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-14586-5 |
| _version_ | 1818423148360499200 |
|---|---|
| author | Yutaka Hashimoto Xinlei Sheng Laura A. Murray-Nerger Ileana M. Cristea |
| author_facet | Yutaka Hashimoto Xinlei Sheng Laura A. Murray-Nerger Ileana M. Cristea |
| author_sort | Yutaka Hashimoto |
| collection | DOAJ |
| description | Here, Hashimoto et al. apply mass spectrometry-based thermal proximity coaggregation to characterize the temporal dynamics of virus-host protein-protein interactions during human cytomegalovirus (HCMV) infection, uncovering proviral functions including the internalization of the HCMV receptor integrin beta 1 with CD63. |
| first_indexed | 2024-12-14T13:37:32Z |
| format | Article |
| id | doaj.art-0ca7fdb5104842789dbc540fcee827b1 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-14T13:37:32Z |
| publishDate | 2020-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-0ca7fdb5104842789dbc540fcee827b12022-12-21T22:59:33ZengNature PortfolioNature Communications2041-17232020-02-0111112010.1038/s41467-020-14586-5Temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infectionYutaka Hashimoto0Xinlei Sheng1Laura A. Murray-Nerger2Ileana M. Cristea3Department of Molecular Biology, Princeton University, Lewis Thomas LaboratoryDepartment of Molecular Biology, Princeton University, Lewis Thomas LaboratoryDepartment of Molecular Biology, Princeton University, Lewis Thomas LaboratoryDepartment of Molecular Biology, Princeton University, Lewis Thomas LaboratoryHere, Hashimoto et al. apply mass spectrometry-based thermal proximity coaggregation to characterize the temporal dynamics of virus-host protein-protein interactions during human cytomegalovirus (HCMV) infection, uncovering proviral functions including the internalization of the HCMV receptor integrin beta 1 with CD63.https://doi.org/10.1038/s41467-020-14586-5 |
| spellingShingle | Yutaka Hashimoto Xinlei Sheng Laura A. Murray-Nerger Ileana M. Cristea Temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infection Nature Communications |
| title | Temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infection |
| title_full | Temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infection |
| title_fullStr | Temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infection |
| title_full_unstemmed | Temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infection |
| title_short | Temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infection |
| title_sort | temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infection |
| url | https://doi.org/10.1038/s41467-020-14586-5 |
| work_keys_str_mv | AT yutakahashimoto temporaldynamicsofproteincomplexformationanddissociationduringhumancytomegalovirusinfection AT xinleisheng temporaldynamicsofproteincomplexformationanddissociationduringhumancytomegalovirusinfection AT lauraamurraynerger temporaldynamicsofproteincomplexformationanddissociationduringhumancytomegalovirusinfection AT ileanamcristea temporaldynamicsofproteincomplexformationanddissociationduringhumancytomegalovirusinfection |