ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase.
about
Virion assembly factories in the nucleus of polyomavirus-infected cellsViral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruptionEpstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodiesFormation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexesPondering the puzzle of PML (promyelocytic leukemia) nuclear bodies: can we fit the pieces together using an RNA regulon?Visualization by live-cell microscopy of disruption of ND10 during herpes simplex virus type 1 infection.The Rep protein of adeno-associated virus type 2 interacts with single-stranded DNA-binding proteins that enhance viral replication.Recruitment of cellular recombination and repair proteins to sites of herpes simplex virus type 1 DNA replication is dependent on the composition of viral proteins within prereplicative sites and correlates with the induction of the DNA damage respoInhibition of the herpes simplex virus type 1 DNA polymerase induces hyperphosphorylation of replication protein A and its accumulation at S-phase-specific sites of DNA damage during infection.A role for cytoplasmic PML in cellular resistance to viral infectionDefinition of herpes simplex virus type 1 helper activities for adeno-associated virus early replication eventsA dominant-negative herpesvirus protein inhibits intranuclear targeting of viral proteins: effects on DNA replication and late gene expression.Herpes simplex virus tegument ICP0 is capsid associated, and its E3 ubiquitin ligase domain is important for incorporation into virions.ICP27 phosphorylation site mutants are defective in herpes simplex virus 1 replication and gene expression.ATR and ATRIP are recruited to herpes simplex virus type 1 replication compartments even though ATR signaling is disabled.Herpes simplex virus reorganizes the cellular DNA repair and protein quality control machinery.Herpes simplex virus ICP0 mutants are hypersensitive to interferonModified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection.Truncation of the C-terminal acidic transcriptional activation domain of herpes simplex virus VP16 renders expression of the immediate-early genes almost entirely dependent on ICP0Origin-independent assembly of Kaposi's sarcoma-associated herpesvirus DNA replication compartments in transient cotransfection assays and association with the ORF-K8 protein and cellular PML.Interactions of herpes simplex virus type 1 with ND10 and recruitment of PML to replication compartments.Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitroInteraction of Kaposi's sarcoma-associated herpesvirus ORF6 protein with single-stranded DNA.Association between the herpes simplex virus-1 DNA polymerase and uracil DNA glycosylaseThe Kaposi's sarcoma-associated herpesvirus ORF6 DNA binding protein forms long DNA-free helical protein filamentsRecruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins.Determination of minimum herpes simplex virus type 1 components necessary to localize transcriptionally active DNA to ND10.Herpes simplex virus type 1 single strand DNA binding protein and helicase/primase complex disable cellular ATR signaling.Varicella zoster virus latency.Replication of the herpes simplex virus genome: does it really go around in circles?DNA mismatch repair proteins are required for efficient herpes simplex virus 1 replicationPoint mutations in exon I of the herpes simplex virus putative terminase subunit, UL15, indicate that the most conserved residues are essential for cleavage and packaging.Live covisualization of competing adeno-associated virus and herpes simplex virus type 1 DNA replication: molecular mechanisms of interaction.A mutation in the human herpes simplex virus type 1 UL52 zinc finger motif results in defective primase activity but can recruit viral polymerase and support viral replication efficiently.Latency Entry of Herpes Simplex Virus 1 Is Determined by the Interaction of Its Genome with the Nuclear EnvironmentInterleukin 6 signaling regulates promyelocytic leukemia protein gene expression in human normal and cancer cells.Herpes simplex virus infections are arrested in Oct-1-deficient cellsAdeno-Associated Virus Type 2 Rep68 Can Bind to Consensus Rep-Binding Sites on the Herpes Simplex Virus 1 Genome.Contribution of the C-terminal regions of promyelocytic leukemia protein (PML) isoforms II and V to PML nuclear body formationNuclear domain 10-associated proteins recognize and segregate intranuclear DNA/protein complexes to negate gene expression
P2860
Q21558475-507E479A-4115-4F37-84E8-23190B337DABQ24527246-FD07413B-A277-4785-8E07-227CEC79887AQ24529499-EF53D5B3-A68C-4198-BF86-BBCB1111D41CQ24607261-2BB20884-3C00-4F11-B2A6-2C58E6B04A04Q28755220-EC5FF578-E52B-45C3-BF87-6918A177F942Q30834143-4540248C-B6B3-45A9-8E71-B967FA8DE136Q31032266-F3B9E33B-F0D6-4A5C-B07A-2C3B29A12DDCQ33201426-956F4A1C-24A0-4B44-AAD5-EEBD9531E9A6Q33214993-ED225206-4D37-4536-92DE-812099D0563FQ33338503-5F1C77A8-0459-4122-A354-3F8B87959E45Q33417647-2C23EB87-4383-4A48-97AE-75566443EBCBQ33603607-B879BB49-CBEB-49B5-8187-502ABF73FDACQ33614341-3E1AB18B-3967-4B91-816A-DD1D7FC6EFA5Q33648884-7B01CDC9-B22E-4B51-B40F-2AA9913CE6F8Q33699630-CFD79DD9-F512-4C50-ADBA-7FFB7C7F0F44Q33760836-A26C7EB2-7260-432A-9FCD-FD52FC26C88DQ33798242-73A9435A-8FB7-4EED-A0CC-DA34419811B2Q33817623-A896635B-9551-40CD-8CB4-E1FACDA4AAB2Q33824256-EEFDB74C-8BC4-4B22-AFFC-221B54831A76Q33836726-7DBC85CD-4D9F-413E-B1E0-8950D9A5BF7EQ33850767-38476FC3-886A-4BAE-9396-6A4FDDB04E23Q33964524-5C915EE5-32BB-43FF-861D-652CCA72CD14Q34057808-868ABC30-2F4F-4772-9A58-5166B0B0D924Q34107227-A145B6A2-BF02-442C-B9D2-861926D5F0CDQ34669430-945921B9-78DD-456A-9D04-E61485A3C735Q34781727-AF40222B-14A2-4C1A-B4C0-6F424FE07616Q34976574-4CEB72AE-8800-4B82-B617-37E605C848DAQ35008795-D50946AA-5FEE-484D-9D55-64EA14CC9735Q35054349-923026BB-5857-4052-A0AB-116AC0B3FD92Q35145669-3E3C5312-D86E-41A7-A33F-D0FE76F920BAQ35531558-86F984B4-6E9C-4A35-A785-380B7D270553Q35802925-55C4851E-7DA3-4692-AB4D-4419933FB556Q35857328-A0B7E397-8AEF-4DDC-81BB-B575D4ED5692Q35947833-E2BAFE61-5C5B-4F92-930A-AACC11D5C9EEQ36130131-2CC27905-6A49-48A0-B56A-55CA927F97D0Q36137373-021F2C22-F927-41AB-AE9A-B6B3C05DC2E5Q36159009-AC861B03-5230-4D3F-BB62-64D595463EF6Q36208198-7FAFAE24-C125-4026-9D1C-9EBE342D2982Q36216480-B60468CC-25A5-4EC9-8C18-C21813287E53Q36412174-95AA152C-1189-4DA7-B94A-9AF5BC0838AC
P2860
ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
ND10 protein PML is recruited ...... sence of viral DNA polymerase.
@en
ND10 protein PML is recruited ...... sence of viral DNA polymerase.
@nl
type
label
ND10 protein PML is recruited ...... sence of viral DNA polymerase.
@en
ND10 protein PML is recruited ...... sence of viral DNA polymerase.
@nl
prefLabel
ND10 protein PML is recruited ...... sence of viral DNA polymerase.
@en
ND10 protein PML is recruited ...... sence of viral DNA polymerase.
@nl
P2093
P2860
P1433
P1476
ND10 protein PML is recruited ...... sence of viral DNA polymerase.
@en
P2093
P2860
P304
10100-10107
P407
P577
1998-12-01T00:00:00Z