The size and symmetry of B capsids of herpes simplex virus type 1 are determined by the gene products of the UL26 open reading frame
about
Determination and analysis of the complete nucleotide sequence of human herpesvirusStudy of herpes simplex virus maturation during a synchronous wave of assemblySeparate functional domains of the herpes simplex virus type 1 protease: evidence for cleavage inside capsids.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.Release of the catalytic domain N(o) from the herpes simplex virus type 1 protease is required for viral growthThe C-terminal 25 amino acids of the protease and its substrate ICP35 of herpes simplex virus type 1 are involved in the formation of sealed capsidsAssembly of the herpes simplex virus capsid: requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genesThe product of the herpes simplex virus type 1 UL25 gene is required for encapsidation but not for cleavage of replicated viral DNA.Evidence for controlled incorporation of herpes simplex virus type 1 UL26 protease into capsidsSilencing herpes simplex virus type 1 capsid protein encoding genes by siRNA: a promising antiviral therapeutic approach.Persistence and expression of the herpes simplex virus genome in the absence of immediate-early proteins.Phosphorylation of simian cytomegalovirus assembly protein precursor (pAPNG.5) and proteinase precursor (pAPNG1): multiple attachment sites identified, including two adjacent serines in a casein kinase II consensus sequence.Role of the UL25 gene product in packaging DNA into the herpes simplex virus capsid: location of UL25 product in the capsid and demonstration that it binds DNA.A null mutation in the gene encoding the herpes simplex virus type 1 UL37 polypeptide abrogates virus maturation.Identification of a novel linear B-cell epitope in the UL26 and UL26.5 proteins of Duck Enteritis VirusFunctional analysis of the triplex proteins (VP19C and VP23) of herpes simplex virus type 1phi X174 genome-capsid interactions influence the biophysical properties of the virion: evidence for a scaffolding-like function for the genome during the final stages of morphogenesisMutation of single hydrophobic residue I27, L35, F39, L58, L65, L67, or L71 in the N terminus of VP5 abolishes interaction with the scaffold protein and prevents closure of herpes simplex virus type 1 capsid shellsA domain in the herpes simplex virus 1 triplex protein VP23 is essential for closure of capsid shells into icosahedral structuresEnzymatic activities of human cytomegalovirus maturational protease assemblin and its precursor (pPR, pUL80a) are comparable: [corrected] maximal activity of pPR requires self-interaction through its scaffolding domain.The protease and the assembly protein of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8).Structural features of the scaffold interaction domain at the N terminus of the major capsid protein (VP5) of herpes simplex virus type 1.Identification of the sites of interaction between the scaffold and outer shell in herpes simplex virus-1 capsids by difference electron imaging.Characterization of mre11 loss following HSV-1 infection.Characterization of a soluble stable human cytomegalovirus protease and inhibition by M-site peptide mimics.Encapsidation of viral DNA requires the adenovirus L1 52/55-kilodalton protein.Roles of triplex and scaffolding proteins in herpes simplex virus type 1 capsid formation suggested by structures of recombinant particlespH reduction as a trigger for dissociation of herpes simplex virus type 1 scaffolds.Regions of the herpes simplex virus scaffolding protein that are important for intermolecular self-interaction.Residues of VP26 of herpes simplex virus type 1 that are required for its interaction with capsids.Cloning, expression and characterization of the proteinase from human herpesvirus 6Cytomegalovirus "missing" capsid protein identified as heat-aggregable product of human cytomegalovirus UL46.Virus-specific interaction between the human cytomegalovirus major capsid protein and the C terminus of the assembly protein precursorIndependently cloned halves of cytomegalovirus assemblin, An and Ac, can restore proteolytic activity to assemblin mutants by intermolecular complementation.Antibody cross-reactivity with CD46 and lack of cell surface expression suggest that moesin might not mediate measles virus binding.Na, an autoproteolytic product of the herpes simplex virus type 1 protease, can functionally substitute for the assembly protein ICP35.Self-association of herpes simplex virus type 1 ICP35 is via coiled-coil interactions and promotes stable interaction with the major capsid protein.Alterations in catalytic activity and virus maturation produced by mutation of the conserved histidine residues of herpes simplex virus type 1 protease.Assembly protein precursor (pUL80.5 homolog) of simian cytomegalovirus is phosphorylated at a glycogen synthase kinase 3 site and its downstream "priming" site: phosphorylation affects interactions of protein with itself and with major capsid proteiThe amino-conserved domain of human cytomegalovirus UL80a proteins is required for key interactions during early stages of capsid formation and virus production
P2860
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P2860
The size and symmetry of B capsids of herpes simplex virus type 1 are determined by the gene products of the UL26 open reading frame
description
1994 nî lūn-bûn
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1994年の論文
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1994年論文
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1994年論文
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1994年論文
@zh-hk
1994年論文
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1994年論文
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1994年论文
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1994年论文
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1994年论文
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name
The size and symmetry of B cap ...... of the UL26 open reading frame
@ast
The size and symmetry of B cap ...... of the UL26 open reading frame
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type
label
The size and symmetry of B cap ...... of the UL26 open reading frame
@ast
The size and symmetry of B cap ...... of the UL26 open reading frame
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prefLabel
The size and symmetry of B cap ...... of the UL26 open reading frame
@ast
The size and symmetry of B cap ...... of the UL26 open reading frame
@en
P2093
P2860
P1433
P1476
The size and symmetry of B cap ...... of the UL26 open reading frame
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P2093
P2860
P304
P407
P577
1994-09-01T00:00:00Z