Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication. - Wikidata - wikimedia - TriplyDB

Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication.

Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication.

http://www.wikidata.org/entity/Q35101480

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Identification and characterization of a novel component of the human minichromosome maintenance complex Phosphoproteomic analyses reveal signaling pathways that facilitate lytic gammaherpesvirus replication Cyclin-dependent kinase-like function is shared by the beta- and gamma- subset of the conserved herpesvirus protein kinases Phosphoproteomic Profiling Reveals Epstein-Barr Virus Protein Kinase Integration of DNA Damage Response and Mitotic Signaling The papillomavirus E1 helicase activates a cellular DNA damage response in viral replication foci Homologous recombinational repair factors are recruited and loaded onto the viral DNA genome in Epstein-Barr virus replication compartments.Noise cancellation: viral fine tuning of the cellular environment for its own genome replication.A locus encompassing the Epstein-Barr virus bglf4 kinase regulates expression of genes encoding viral structural proteins Epstein-Barr virus BGLF4 kinase retards cellular S-phase progression and induces chromosomal abnormality.BGLF4 kinase modulates the structure and transport preference of the nuclear pore complex to facilitate nuclear import of Epstein-Barr virus lytic proteins Conserved herpesvirus kinases target the DNA damage response pathway and TIP60 histone acetyltransferase to promote virus replication.Partial MCM4 deficiency in patients with growth retardation, adrenal insufficiency, and natural killer cell deficiency.Epstein-Barr virus BGLF4 kinase induces premature chromosome condensation through activation of condensin and topoisomerase II.Epstein-Barr virus protein kinase BGLF4 targets the nucleus through interaction with nucleoporins.Epstein-Barr virus BGLF4 kinase downregulates NF-κB transactivation through phosphorylation of coactivator UXT.Key motifs in EBV (Epstein-Barr virus)-encoded protein kinase for phosphorylation activity and nuclear localization.Conserved herpesvirus protein kinases.Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production Epstein-Barr virus BGLF4 kinase suppresses the interferon regulatory factor 3 signaling pathway Protein array identification of substrates of the Epstein-Barr virus protein kinase BGLF4 Evidence for the progression through S-phase in the ectopic cell cycle re-entry of neurons in Alzheimer disease.The Mcm complex: unwinding the mechanism of a replicative helicase.DNA virus replication compartments.Simian virus 40 T/t antigens and lamin A/C small interfering RNA rescue the phenotype of an Epstein-Barr virus protein kinase (BGLF4) mutant.Maribavir inhibits epstein-barr virus transcription in addition to viral DNA replication Initiation of lytic DNA replication in Epstein-Barr virus: search for a common family mechanism.Herpes simplex virus-1 evasion of CD8+ T cell accumulation contributes to viral encephalitis.Potent DNA strand annealing activity associated with mouse Mcm2∼7 heterohexameric complex.Identification of an arginine-rich motif in human papillomavirus type 1 E1;E4 protein necessary for E4-mediated inhibition of cellular DNA synthesis in vitro and in cells.SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function.Phosphorylation of p27Kip1 by Epstein-Barr virus protein kinase induces its degradation through SCFSkp2 ubiquitin ligase actions during viral lytic replication.KSHV de-regulates host cellular replication during lytic reactivation by disrupting the MCM complex through ORF59

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Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication.

http://www.wikidata.org/entity/Q35101480

description

2006 nî lūn-bûn

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2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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Phosphorylation of MCM4 at sit ...... virus productive replication.

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Phosphorylation of MCM4 at sit ...... virus productive replication.

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type

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Phosphorylation of MCM4 at sit ...... virus productive replication.

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Phosphorylation of MCM4 at sit ...... virus productive replication.

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Phosphorylation of MCM4 at sit ...... virus productive replication.

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Phosphorylation of MCM4 at sit ...... virus productive replication.

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Phosphorylation of MCM4 at sit ...... virus productive replication.

@en

P2093

Ayumi Kudoh

http://www.w3.org/2001/XMLSchema#string

Hiroki Isomura

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Noriko Shirata

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Satoko Iwahori

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Tatsuya Tsurumi

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Tohru Daikoku

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Yasushi Kawaguchi

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Yukio Ishimi

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P2860

Inhibition of eukaryotic DNA replication by geminin binding to Cdt1

Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication

Geminin, an inhibitor of DNA replication, is degraded during mitosis

A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex

Human cytomegalovirus infection leads to accumulation of geminin and inhibition of the licensing of cellular DNA replication.

Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex requires forked DNA structures

Assembly of a complex containing Cdc45p, replication protein A, and Mcm2p at replication origins controlled by S-phase cyclin-dependent kinases and Cdc7p-Dbf4p kinase

Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase activity

DNA binding and helicase actions of mouse MCM4/6/7 helicase.

Uninterrupted MCM2-7 function required for DNA replication fork progression.

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10064-10072

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10.1128/JVI.00678-06

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P433

20

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80

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2006-10-01T00:00:00Z

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6788384

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17005684

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phosphorylation

Epstein–Barr virus

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1617282

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