Release of the herpes simplex virus 1 protease by self cleavage is required for proper conformation of the portal vertex

scientific article published on 28 April 2012

Release of the herpes simplex virus 1 protease by self cleavage is required for proper conformation of the portal vertex is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.VIROL.2012.03.009
P932PMC publication ID3367450
P698PubMed publication ID22543049
P5875ResearchGate publication ID224866830

P2093author name stringKui Yang
Joel D Baines
Elizabeth G Wills
P2860cites workInvolvement of the portal at an early step in herpes simplex virus capsid assemblyQ24534403
Identification of a region in the herpes simplex virus scaffolding protein required for interaction with the portalQ24558694
Assembly of the herpes simplex virus capsid: identification of soluble scaffold-portal complexes and their role in formation of portal-containing capsidsQ24646283
Visualization of the herpes simplex virus portal in situ by cryo-electron tomographyQ24685687
The protease of herpes simplex virus type 1 is essential for functional capsid formation and viral growthQ28776766
Isolation of herpes simplex virus procapsids from cells infected with a protease-deficient mutant virus.Q30304621
The UL6 gene product forms the portal for entry of DNA into the herpes simplex virus capsid.Q30308062
Amino acids 143 to 150 of the herpes simplex virus type 1 scaffold protein are required for the formation of portal-containing capsidsQ30440972
Separate functional domains of the herpes simplex virus type 1 protease: evidence for cleavage inside capsidsQ30452589
Identification of a minimal hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein.Q30452599
Release of the catalytic domain N(o) from the herpes simplex virus type 1 protease is required for viral growthQ30452610
Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsidQ30454077
Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexesQ30467365
Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formationQ30469651
Construction of an excisable bacterial artificial chromosome containing a full-length infectious clone of herpes simplex virus type 1: viruses reconstituted from the clone exhibit wild-type properties in vitro and in vivoQ34464526
Putative terminase subunits of herpes simplex virus 1 form a complex in the cytoplasm and interact with portal protein in the nucleusQ35857283
Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2.Q36591208
Domain within herpes simplex virus 1 scaffold proteins required for interaction with portal protein in infected cells and incorporation of the portal vertex into capsidsQ36594192
The herpes simplex virus 1 gene encoding a protease also contains within its coding domain the gene encoding the more abundant substrateQ36797992
Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteinsQ36820134
Differentiation of multiple domains in the herpes simplex virus 1 protease encoded by the UL26 geneQ36879562
The putative leucine zipper of the UL6-encoded portal protein of herpes simplex virus 1 is necessary for interaction with pUL15 and pUL28 and their association with capsidsQ37157132
Proline and tyrosine residues in scaffold proteins of herpes simplex virus 1 critical to the interaction with portal protein and its incorporation into capsidsQ37275037
Nuclear localization sequences in cytomegalovirus capsid assembly proteins (UL80 proteins) are required for virus production: inactivating NLS1, NLS2, or both affects replication to strikingly different extentsQ38610191
Cytomegalovirus assembly protein precursor and proteinase precursor contain two nuclear localization signals that mediate their own nuclear translocation and that of the major capsid protein.Q39580849
Regions of the herpes simplex virus scaffolding protein that are important for intermolecular self-interactionQ39686010
Alterations in catalytic activity and virus maturation produced by mutation of the conserved histidine residues of herpes simplex virus type 1 proteaseQ39882240
Herpes simplex virus type 1 protease expressed in Escherichia coli exhibits autoprocessing and specific cleavage of the ICP35 assembly proteinQ40062250
Identification and Characterization of a Herpes Simplex Virus Gene Product Required for Encapsidation of Virus DNAQ40143846
Cell lines that support replication of a novel herpes simplex virus 1 UL31 deletion mutant can properly target UL34 protein to the nuclear rim in the absence of UL31.Q40505457
Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopyQ40653928
Second-site mutations encoding residues 34 and 78 of the major capsid protein (VP5) of herpes simplex virus type 1 are important for overcoming a blocked maturation cleavage site of the capsid scaffold proteinsQ40838224
Second site mutations in the N-terminus of the major capsid protein (VP5) overcome a block at the maturation cleavage site of the capsid scaffold proteins of herpes simplex virus type 1.Q40927281
The herpes simplex virus 1 UL 17 gene is required for localization of capsids and major and minor capsid proteins to intranuclear sites where viral DNA is cleaved and packagedQ40984041
Isolation and characterization of herpes simplex virus type 1 mutants defective in the UL6 geneQ41226040
The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assemblyQ41633915
Mutations in the N-terminus of VP5 alter its interaction with the scaffold proteins of herpes simplex virus type 1.Q43624954
Identification of the herpes simplex virus-1 protease cleavage sites by direct sequence analysis of autoproteolytic cleavage productsQ45775821
Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22aQ45778626
Characterization of herpes simplex virus strains differing in their effects on social behaviour of infected cellsQ45823697
Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coliQ45856655
Identification of genes encoding two capsid proteins (VP24 and VP26) of herpes simplex virus type 1.Q45877178
Processing of the herpes simplex virus assembly protein ICP35 near its carboxy terminal end requires the product of the whole of the UL26 reading frameQ45881006
P433issue1
P407language of work or nameEnglishQ1860
P1104number of pages11
P304page(s)63-73
P577publication date2012-04-28
P1433published inVirologyQ7934867
P1476titleRelease of the herpes simplex virus 1 protease by self cleavage is required for proper conformation of the portal vertex
P478volume429