Functional order of assembly of herpes simplex virus DNA replication proteins into prereplicative site structures.
about
US11 of herpes simplex virus type 1 interacts with HIPK2 and antagonizes HIPK2-induced cell growth arrestThe Epstein-Barr virus replication protein BBLF2/3 provides an origin-tethering function through interaction with the zinc finger DNA binding protein ZBRK1 and the KAP-1 corepressorAlpha-herpesvirus infection induces the formation of nuclear actin filamentsHerpes simplex virus type 1 immediate-early protein ICP22 is required for VICE domain formation during productive viral infection.The herpes simplex virus type 1 cleavage/packaging protein, UL32, is involved in efficient localization of capsids to replication compartmentsThe 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 respoProteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8.Inhibition 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 dominant-negative herpesvirus protein inhibits intranuclear targeting of viral proteins: effects on DNA replication and late 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.The Epstein-Barr virus lytic transactivator Zta interacts with the helicase-primase replication proteins.Analysis of HCF, the cellular cofactor of VP16, in herpes simplex virus-infected cells.Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection.The human cytomegalovirus IE2 and UL112-113 proteins accumulate in viral DNA replication compartments that initiate from the periphery of promyelocytic leukemia protein-associated nuclear bodies (PODs or ND10)Autographa californica multiple nucleopolyhedrovirus LEF-2 is a capsid protein required for amplification but not initiation of viral DNA replication.Origin-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.Processing of lagging-strand intermediates in vitro by herpes simplex virus type 1 DNA polymeraseAssociation between the herpes simplex virus-1 DNA polymerase and uracil DNA glycosylaseRole of the herpes simplex virus helicase-primase complex during adeno-associated virus DNA replicationRecruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins.Herpes simplex virus type 1 single strand DNA binding protein and helicase/primase complex disable cellular ATR signaling.Conformational changes in the herpes simplex virus ICP8 DNA-binding protein coincident with assembly in viral replication structures.DNA mismatch repair proteins are required for efficient herpes simplex virus 1 replicationHost cell nucleolin is required to maintain the architecture of human cytomegalovirus replication compartments.The latency-related gene of bovine herpesvirus 1 encodes a product which inhibits cell cycle progression.Evidence that the UL84 gene product of human cytomegalovirus is essential for promoting oriLyt-dependent DNA replication and formation of replication compartments in cotransfection assaysAssembly of complete, functionally active herpes simplex virus DNA replication compartments and recruitment of associated viral and cellular proteins in transient cotransfection assays.The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex.Herpes simplex virus infections are arrested in Oct-1-deficient cellsThe full-length protein encoded by human cytomegalovirus gene UL117 is required for the proper maturation of viral replication compartments.Antiviral Activity of Hatay Propolis Against Replication of Herpes Simplex Virus Type 1 and Type 2.Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation.Glycoprotein targeted therapeutics: a new era of anti-herpes simplex virus-1 therapeuticsDynamic and nucleolin-dependent localization of human cytomegalovirus UL84 to the periphery of viral replication compartments and nucleoli.The 60-residue C-terminal region of the single-stranded DNA binding protein of herpes simplex virus type 1 is required for cooperative DNA binding.Visualization of DNA G-quadruplexes in herpes simplex virus 1-infected cells.The absence of p53 during Human Cytomegalovirus infection leads to decreased UL53 expression, disrupting UL50 localization to the inner nuclear membrane, and thereby inhibiting capsid nuclear egress.
P2860
Q24313084-60C1AFE5-8A15-418C-B703-E3AB595C2BB6Q24558692-BA65B0E0-CE05-423D-8C05-18FFB16F7232Q27320136-E4B119A5-ECF8-4AB7-9589-08C9DA59B33AQ30434945-37988F1E-0D8A-4CB0-A74E-DBF0964E3618Q30453534-6730BA66-810B-49F6-9AEF-46B0E326E259Q31032266-C6A8CDE8-622A-49B6-A03F-85DD720F690AQ33201426-E3B33A1E-4360-459E-8619-402964FC06B2Q33202888-85DB3451-821B-417B-8B64-FB467225EB7FQ33214993-9A6996B7-6D79-4FB0-9DCB-31FF56506677Q33603607-0E14A7E3-B7DF-48EC-A993-A8B298F81672Q33699630-F1ADE8C4-91EC-4CF6-A92B-69F291D6DAF8Q33760836-EA37EF60-3E28-4AD3-9818-65C0FD40DD9AQ33785198-5D14E2B6-5DB6-49D1-B1B7-59D9113E697CQ33794386-7DF05F62-6094-45C2-A8D4-3A51FF46C612Q33817623-DA53B5FB-18B2-4DDF-86E6-E89F2BEC888DQ33825616-EA487673-7326-4BC3-8B3E-14A3D180C053Q33826825-A59E760E-A70C-4F70-B14B-3E7CC0E5782AQ33836726-E258187F-5293-40A7-A926-5FC32BBAE054Q33850767-CC6FB2CF-3448-4A70-BC66-612B627D0854Q33964152-1E226EC5-C85F-4F00-9B0F-38023CF83399Q34107227-14CA9D53-2C14-45D7-97AD-6705F2D7060AQ34648352-ED03DF7F-9ABC-4D82-B465-805E53FF1875Q34781727-7A4A93D0-6A36-45FF-9FFF-38165D3EF427Q35008795-C9EF2E62-A970-4B92-9223-1A31E9341054Q35149367-0DFC4E8B-4FC2-4783-A8F8-6333A45BE31BQ35531558-1783AE18-9740-485D-8B7A-EAE6BF798F01Q35759789-ACD41CB6-5779-4720-BA21-F103E25EFDA6Q35861605-75C23CC7-70CF-4CCA-B317-0296070BA85EQ35871538-C5BE16A4-6398-47E3-A3E3-FCBA54E8A3D6Q35881315-A09B2FA6-4CF0-43F6-804A-9C9DE50EC652Q35891002-618A07FF-D4F6-4C36-A363-0DFBBE332C7CQ36159009-B418F842-8FA3-49BE-86DE-39E12BDD426AQ36498138-6A6A6928-292F-4033-828B-3B9E2957E1FEQ36572251-6C7EF7BA-12B4-44E3-8EF5-684152B0F2A0Q36747965-3D4B94A5-AF9F-449A-8A9D-1C8CE6D3C74DQ36866689-CAE5E7ED-D79F-409E-8043-7DCE9D20F7F8Q38305382-2741B6A4-ABB9-443D-8F34-08B57D0D1428Q38308467-47A32CF1-BA3D-4059-B2BB-144846AC717DQ38735386-C3D88B2A-F10A-4FBC-A3D5-7AC3DBDF5DA3Q38753361-01A61E52-BCCA-49FD-A9D8-DC63C0C33F95
P2860
Functional order of assembly of herpes simplex virus DNA replication proteins into prereplicative site structures.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Functional order of assembly o ...... rereplicative site structures.
@ast
Functional order of assembly o ...... rereplicative site structures.
@en
type
label
Functional order of assembly o ...... rereplicative site structures.
@ast
Functional order of assembly o ...... rereplicative site structures.
@en
prefLabel
Functional order of assembly o ...... rereplicative site structures.
@ast
Functional order of assembly o ...... rereplicative site structures.
@en
P2093
P2860
P1433
P1476
Functional order of assembly o ...... prereplicative site structures
@en
P2093
L M Liptak
S L Uprichard
P2860
P304
P407
P577
1996-03-01T00:00:00Z