Cryo-Electron Tomography of the Herpesvirus Procapsid Reveals Interactions of the Portal with the Scaffold and a Shift on Maturation
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Title
Cryo-Electron Tomography of the Herpesvirus Procapsid Reveals Interactions of the Portal with the Scaffold and a Shift on Maturation
Authors
Keywords
-
Journal
mBio
Volume 12, Issue 2, Pages -
Publisher
American Society for Microbiology
Online
2021-03-15
DOI
10.1128/mbio.03575-20
References
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Note: Only part of the references are listed.- Structures of the portal vertex reveal essential protein-protein interactions for Herpesvirus assembly and maturation
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- (2020) J. Bernard Heymann PROTEIN SCIENCE
- Cryo-EM structures of herpes simplex virus type 1 portal vertex and packaged genome
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- Portal Protein: The Orchestrator of Capsid Assembly for the dsDNA Tailed Bacteriophages and Herpesviruses
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- Guidelines for using Bsoft for high resolution reconstruction and validation of biomolecular structures from electron micrographs
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- Extensive subunit contacts underpin herpesvirus capsid stability and interior-to-exterior allostery
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- Herpesviruses remodel host membranes for virus egress
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- (2010) R. H. Rochat et al. JOURNAL OF VIROLOGY
- Tryptophan Residues in the Portal Protein of Herpes Simplex Virus 1 Critical to the Interaction with Scaffold Proteins and Incorporation of the Portal into Capsids
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- Proline and Tyrosine Residues in Scaffold Proteins of Herpes Simplex Virus 1 Critical to the Interaction with Portal Protein and Its Incorporation into Capsids
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