The carboxyl-terminal domain of RNA polymerase II is phosphorylated by a complex containing cdk9 and infected-cell protein 22 of herpes simplex virus 1.
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Nuclear CDKs drive Smad transcriptional activation and turnover in BMP and TGF-beta pathwaysShutoff of Host Gene Expression in Influenza A Virus and Herpesviruses: Similar Mechanisms and Common ThemesA Smad action turnover switch operated by WW domain readers of a phosphoserine codeAn Epigenetic Compound Library Screen Identifies BET Inhibitors That Promote HSV-1 and -2 Replication by Bridging P-TEFb to Viral Gene Promoters through BRD4Definition of herpes simplex virus type 1 helper activities for adeno-associated virus early replication eventsRole of herpes simplex virus 1 immediate early protein ICP22 in viral nuclear egress.Herpes simplex virus 1 ICP22 regulates the accumulation of a shorter mRNA and of a truncated US3 protein kinase that exhibits altered functionsHuman cytomegalovirus infection induces specific hyperphosphorylation of the carboxyl-terminal domain of the large subunit of RNA polymerase II that is associated with changes in the abundance, activity, and localization of cdk9 and cdk7.Herpes simplex virus 1 ICP22 inhibits the transcription of viral gene promoters by binding to and blocking the recruitment of P-TEFbICP27 interacts with the C-terminal domain of RNA polymerase II and facilitates its recruitment to herpes simplex virus 1 transcription sites, where it undergoes proteasomal degradation during infection.U(S)3 and U(S)3.5 protein kinases of herpes simplex virus 1 differ with respect to their functions in blocking apoptosis and in virion maturation and egress.Inhibition of cdk9 during herpes simplex virus 1 infection impedes viral transcriptionORF18 is a transfactor that is essential for late gene transcription of a gammaherpesvirus.Sequence variation in the herpes simplex virus U(S)1 ocular virulence determinant.Herpes Simplex Virus 1 (HSV-1) ICP22 protein directly interacts with cyclin-dependent kinase (CDK)9 to inhibit RNA polymerase II transcription elongationHerpes simplex virus immediate-early protein ICP22 triggers loss of serine 2-phosphorylated RNA polymerase IIKaposi's sarcoma-associated herpesvirus K-cyclin interacts with Cdk9 and stimulates Cdk9-mediated phosphorylation of p53 tumor suppressorThe interaction of herpes simplex virus 1 regulatory protein ICP22 with the cdc25C phosphatase is enabled in vitro by viral protein kinases US3 and UL13.Human cytomegalovirus UL97 kinase activity is required for the hyperphosphorylation of retinoblastoma protein and inhibits the formation of nuclear aggresomes.Role of cdk9 in the optimization of expression of the genes regulated by ICP22 of herpes simplex virus 1Roles of p53 in herpes simplex virus 1 replication.Recruitment of cdk9 to the immediate-early viral transcriptosomes during human cytomegalovirus infection requires efficient binding to cyclin T1, a threshold level of IE2 86, and active transcription.Herpes simplex virus 1 ICP22 but not US 1.5 is required for efficient acute replication in mice and VICE domain formation.Function of human cytomegalovirus UL97 kinase in viral infection and its inhibition by maribavir.HSV-1 ICP22: hijacking host nuclear functions to enhance viral infection.Negative elongation factor-mediated suppression of RNA polymerase II elongation of Kaposi's sarcoma-associated herpesvirus lytic gene expression.Herpes simplex virus 1 ICP4 forms complexes with TFIID and mediator in virus-infected cellsIdentification of sequences in herpes simplex virus type 1 ICP22 that influence RNA polymerase II modification and viral late gene expression.A Herpesviral Immediate Early Protein Promotes Transcription Elongation of Viral Transcripts.Influenza virus infection causes specific degradation of the largest subunit of cellular RNA polymerase II.Varicella-zoster virus infection of human foreskin fibroblast cells results in atypical cyclin expression and cyclin-dependent kinase activity.Pin1 plays a critical role as a molecular switch in canonical BMP signaling.Transcriptional regulation of the Herpes Simplex Virus 1alpha-gene by the viral immediate-early protein ICP22 in association with VP16.A truncation mutation of the neurovirulence ICP22 protein produced by a recombinant HSV-1 generated by bacterial artificial chromosome technology targets infected cell nuclei.
P2860
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P2860
The carboxyl-terminal domain of RNA polymerase II is phosphorylated by a complex containing cdk9 and infected-cell protein 22 of herpes simplex virus 1.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
The carboxyl-terminal domain o ...... 22 of herpes simplex virus 1.
@ast
The carboxyl-terminal domain o ...... 22 of herpes simplex virus 1.
@en
type
label
The carboxyl-terminal domain o ...... 22 of herpes simplex virus 1.
@ast
The carboxyl-terminal domain o ...... 22 of herpes simplex virus 1.
@en
prefLabel
The carboxyl-terminal domain o ...... 22 of herpes simplex virus 1.
@ast
The carboxyl-terminal domain o ...... 22 of herpes simplex virus 1.
@en
P2093
P2860
P1433
P1476
The carboxyl-terminal domain o ...... 22 of herpes simplex virus 1.
@en
P2093
Alice P W Poon
Lizette O Durand
Sunil J Advani
P2860
P304
P356
10.1128/JVI.79.11.6757-6762.2005
P577
2005-06-01T00:00:00Z