Human cytomegalovirus capsid assembly protein precursor (pUL80.5) interacts with itself and with the major capsid protein (pUL86) through two different domains.
about
The delta domain of the HK97 major capsid protein is essential for assemblyDimerization-Induced Allosteric Changes of the Oxyanion-Hole Loop Activate the Pseudorabies Virus Assemblin pUL26N, a Herpesvirus Serine ProteaseAssembly of the herpes simplex virus procapsid from purified components and identification of small complexes containing the major capsid and scaffolding proteins.Capsid structure of simian cytomegalovirus from cryoelectron microscopy: evidence for tegument attachment sites.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.Analysis and characterization of the complete genome of tupaia (tree shrew) herpesvirusYeast two hybrid analyses reveal novel binary interactions between human cytomegalovirus-encoded virion proteins.Cleavage of human cytomegalovirus protease pUL80a at internal and cryptic sites is not essential but enhances infectivity.Functional analysis of the triplex proteins (VP19C and VP23) of herpes simplex virus type 1Human cytomegalovirus UL47 tegument protein functions after entry and before immediate-early gene expressionMutant human cytomegalovirus lacking the immediate-early TRS1 coding region exhibits a late defectCytomegalovirus assemblin (pUL80a): cleavage at internal site not essential for virus growth; proteinase absent from virions.Identification of binary interactions between human cytomegalovirus virion proteins.Mutation 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 shellsDNA binding and condensation properties of the herpes simplex virus type 1 triplex protein VP19CA 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.Reevaluation of human cytomegalovirus coding potential.Modulation of the cellular distribution of human cytomegalovirus helicase by cellular factor Snapin.The rice tungro bacilliform virus gene II product interacts with the coat protein domain of the viral gene III polyprotein.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 extents.A mutation deleting sequences encoding the amino terminus of human cytomegalovirus UL84 impairs interaction with UL44 and capsid localizationCytomegalovirus assembly protein precursor and proteinase precursor contain two nuclear localization signals that mediate their own nuclear translocation and that of the major capsid protein.pH 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.The interaction between the major capsid protein and the smallest capsid protein of human cytomegalovirus is dependent on two linear sequences in the smallest capsid protein.Human cytomegalovirus tegument proteins ppUL82 (pp71) and ppUL35 interact and cooperatively activate the major immediate-early enhancer.Independently cloned halves of cytomegalovirus assemblin, An and Ac, can restore proteolytic activity to assemblin mutants by intermolecular complementation.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 productionExpression of the HSV-1 capsid protein VP19C in Escherichia coli: a single amino acid change overcomes an expression block of the full-length polypeptide.Cytomegalovirus capsid protease: biological substrates are cleaved more efficiently by full-length enzyme (pUL80a) than by the catalytic domain (assemblin)Human Cytomegalovirus Nuclear Capsids Associate with the Core Nuclear Egress Complex and the Viral Protein Kinase pUL97.
P2860
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P2860
Human cytomegalovirus capsid assembly protein precursor (pUL80.5) interacts with itself and with the major capsid protein (pUL86) through two different domains.
description
1997 nî lūn-bûn
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1997年の論文
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1997年論文
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1997年論文
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name
Human cytomegalovirus capsid a ...... through two different domains.
@ast
Human cytomegalovirus capsid a ...... through two different domains.
@en
type
label
Human cytomegalovirus capsid a ...... through two different domains.
@ast
Human cytomegalovirus capsid a ...... through two different domains.
@en
prefLabel
Human cytomegalovirus capsid a ...... through two different domains.
@ast
Human cytomegalovirus capsid a ...... through two different domains.
@en
P2093
P2860
P1433
P1476
Human cytomegalovirus capsid a ...... through two different domains
@en
P2093
P2860
P304
P407
P577
1997-01-01T00:00:00Z