PXD005104 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | The CVSC mechanically reinforces HSV-1 |
Description | Using atomic force microscopy imaging and nanoindentation measurements, the effect of the minor capsid proteins pUL17 and pUL25 on the structural stability of the icosahedral Herpes Simplex Virus type 1 capsids was investigated. pUL17 and pUL25 that form the capsid vertex-specific component particularly contributed to the capsid resilience along the 5-fold and 2-fold, but not the 3-fold icosahedral axes. We tested whether deletion of UL17 and UL25 changed the levels of the proteins that assemble in the nucleocapsid by quantitative mass spectrometry. |
HostingRepository | PRIDE |
AnnounceDate | 2017-04-20 |
AnnouncementXML | Submission_2017-04-20_00:16:40.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Eleonora Corradini |
SpeciesList | scientific name: Herpes simplex virus (type 1 / strain F); NCBI TaxID: 10304; |
ModificationList | iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2016-10-05 23:58:10 | ID requested | |
⏵ 1 | 2017-04-20 00:16:41 | announced | |
2 | 2024-10-22 04:28:23 | announced | 2024-10-22: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
curator keyword: Biological |
submitter keyword: HSV-1, LC-MS/MS |
Contact List
Albert J.R. Heck |
contact affiliation | Biomolecular mass spectrometry and proteomics, Utrecht University, Utrecht, The Netherlands |
contact email | a.j.r.heck@uu.nl |
lab head | |
Eleonora Corradini |
contact affiliation | Biomolecular and mass spectrometry group |
contact email | e.corradini1@uu.nl |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD005104
- Label: PRIDE project
- Name: The CVSC mechanically reinforces HSV-1