Protein-protein interactions between human cytomegalovirus IE2-580aa and pUL84 in lytically infected cells.
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A nonconventional nuclear localization signal within the UL84 protein of human cytomegalovirus mediates nuclear import via the importin alpha/beta pathwayInhibition of human cytomegalovirus replication via peptide aptamers directed against the nonconventional nuclear localization signal of the essential viral replication factor pUL84.Identification of human cytomegalovirus UL84 virus- and cell-encoded binding partners by using proteomics analysisActivation of transcription of the human cytomegalovirus early UL4 promoter by the Ets transcription factor binding element.In vivo replication, latency, and immunogenicity of murine cytomegalovirus mutants with deletions in the M83 and M84 genes, the putative homologs of human cytomegalovirus pp65 (UL83).A cis repression sequence adjacent to the transcription start site of the human cytomegalovirus US3 gene is required to down regulate gene expression at early and late times after infectionThe human cytomegalovirus IE86 protein can block cell cycle progression after inducing transition into the S phase of permissive cells.Role of the specific interaction of UL112-113 p84 with UL44 DNA polymerase processivity factor in promoting DNA replication of human cytomegalovirus.Inhibition of cellular DNA synthesis by the human cytomegalovirus IE86 protein is necessary for efficient virus replication.Complete sequence and genomic analysis of rhesus cytomegalovirusInteraction network of proteins associated with human cytomegalovirus IE2-p86 protein during infection: a proteomic analysis.Host-viral effects of chromatin assembly factor 1 interaction with HCMV IE2The IE2 60-kilodalton and 40-kilodalton proteins are dispensable for human cytomegalovirus replication but are required for efficient delayed early and late gene expression and production of infectious virus.Multiple regulatory events influence human cytomegalovirus DNA polymerase (UL54) expression during viral infectionThe human cytomegalovirus UL94 open reading frame encodes a conserved herpesvirus capsid/tegument-associated virion protein that is expressed with true late kinetics.Evidence that the UL84 gene product of human cytomegalovirus is essential for promoting oriLyt-dependent DNA replication and formation of replication compartments in cotransfection assaysIdentification, analysis, and evolutionary relationships of the putative murine cytomegalovirus homologs of the human cytomegalovirus UL82 (pp71) and UL83 (pp65) matrix phosphoproteins.Human cytomegalovirus UL84 interacts with an RNA stem-loop sequence found within the RNA/DNA hybrid region of oriLyt.Human cytomegalovirus manipulation of latently infected cells.Functional interaction between the human cytomegalovirus 86-kilodalton IE2 protein and the cellular transcription factor CREB.Dynamic and nucleolin-dependent localization of human cytomegalovirus UL84 to the periphery of viral replication compartments and nucleoli.Human cytomegalovirus UL84 protein contains two nuclear export signals and shuttles between the nucleus and the cytoplasmA mutation deleting sequences encoding the amino terminus of human cytomegalovirus UL84 impairs interaction with UL44 and capsid localizationCharacterization of the transcriptional repressive element of the human cytomegalovirus immediate-early US3 gene.Viable human cytomegalovirus recombinant virus with an internal deletion of the IE2 86 gene affects late stages of viral replicationHuman cytomegalovirus UL84 localizes to the cell nucleus via a nuclear localization signal and is a component of viral replication compartments.Nucleocytoplasmic shuttling of human cytomegalovirus UL84 is essential for virus growth.Human cytomegalovirus IE2 86 and IE2 40 proteins differentially regulate UL84 protein expression posttranscriptionally in the absence of other viral gene products.Human cytomegalovirus UL84 oligomerization and heterodimerization domains act as transdominant inhibitors of oriLyt-dependent DNA replication: evidence that IE2-UL84 and UL84-UL84 interactions are required for lytic DNA replicationDevelopment of cell lines that provide tightly controlled temporal translation of the human cytomegalovirus IE2 proteins for complementation and functional analyses of growth-impaired and nonviable IE2 mutant viruses.Interaction of HCMV UL84 with C/EBPalpha transcription factor binding sites within oriLyt is essential for lytic DNA replication.Four of eleven loci required for transient complementation of human cytomegalovirus DNA replication cooperate to activate expression of replication genes.CREB and CREB-binding proteins play an important role in the IE2 86-kilodalton protein-mediated transactivation of the human cytomegalovirus 2.2-kilobase RNA promoter.Analysis of the complete DNA sequence of murine cytomegalovirus.The UL84 protein of human cytomegalovirus acts as a transdominant inhibitor of immediate-early-mediated transactivation that is able to prevent viral replication.Identification of domains within the human cytomegalovirus major immediate-early 86-kilodalton protein and the retinoblastoma protein required for physical and functional interaction with each other.Interaction of human cytomegalovirus pUL84 with casein kinase 2 is required for oriLyt-dependent DNA replication.Internal deletions of IE2 86 and loss of the late IE2 60 and IE2 40 proteins encoded by human cytomegalovirus affect the levels of UL84 protein but not the amount of UL84 mRNA or the loading and distribution of the mRNA on polysomesHuman cytomegalovirus UL84 insertion mutant defective for viral DNA synthesis and growth.Human cytomegalovirus DNA replication requires transcriptional activation via an IE2- and UL84-responsive bidirectional promoter element within oriLyt.
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P2860
Protein-protein interactions between human cytomegalovirus IE2-580aa and pUL84 in lytically infected cells.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Protein-protein interactions b ...... 4 in lytically infected cells.
@ast
Protein-protein interactions b ...... 4 in lytically infected cells.
@en
type
label
Protein-protein interactions b ...... 4 in lytically infected cells.
@ast
Protein-protein interactions b ...... 4 in lytically infected cells.
@en
prefLabel
Protein-protein interactions b ...... 4 in lytically infected cells.
@ast
Protein-protein interactions b ...... 4 in lytically infected cells.
@en
P2860
P1433
P1476
Protein-protein interactions b ...... 4 in lytically infected cells.
@en
P2093
D J Spector
M J Tevethia
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P304
P407
P577
1994-11-01T00:00:00Z