The herpes simplex virus type 1 regulatory protein ICP27 coimmunoprecipitates with anti-Sm antiserum, and the C terminus appears to be required for this interaction
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Herpes simplex virus 1 regulatory protein ICP22 interacts with a new cell cycle-regulated factor and accumulates in a cell cycle-dependent fashion in infected cells.Association of herpes simplex virus type 1 ICP8 and ICP27 proteins with cellular RNA polymerase II holoenzymeICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway.Death, autoantigen modifications, and tolerance.Mta has properties of an RNA export protein and increases cytoplasmic accumulation of Epstein-Barr virus replication gene mRNA.Hsc70 focus formation at the periphery of HSV-1 transcription sites requires ICP27.Analysis of the phosphorylation sites of herpes simplex virus type 1 regulatory protein ICP27.ICP27 phosphorylation site mutants are defective in herpes simplex virus 1 replication and gene expression.ICP27 phosphorylation site mutants display altered functional interactions with cellular export factors Aly/REF and TAP/NXF1 but are able to bind herpes simplex virus 1 RNAICP27 recruits Aly/REF but not TAP/NXF1 to herpes simplex virus type 1 transcription sites although TAP/NXF1 is required for ICP27 export.Control of VP16 translation by the herpes simplex virus type 1 immediate-early protein ICP27.The Epstein-Barr virus (EBV) SM protein enhances pre-mRNA processing of the EBV DNA polymerase transcript.Herpesvirus mRNAs are sorted for export via Crm1-dependent and -independent pathwaysHerpes simplex virus ICP27 induces cytoplasmic accumulation of unspliced polyadenylated alpha-globin pre-mRNA in infected HeLa cells.Processing of alpha-globin and ICP0 mRNA in cells infected with herpes simplex virus type 1 ICP27 mutants.Identification of an export control sequence and a requirement for the KH domains in ICP27 from herpes simplex virus type 1HSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.Herpes simplex virus ICP27 protein provides viral mRNAs with access to the cellular mRNA export pathway.Mapping of functional regions in the amino-terminal portion of the herpes simplex virus ICP27 regulatory protein: importance of the leucine-rich nuclear export signal and RGG Box RNA-binding domain.Split genes and their expression in Kaposi's sarcoma-associated herpesvirus.ICP27 mediates HSV RNA export by shuttling through a leucine-rich nuclear export signal and binding viral intronless RNAs through an RGG motifThe RGG box motif of the herpes simplex virus ICP27 protein mediates an RNA-binding activity and determines in vivo methylation.Assembly of complete, functionally active herpes simplex virus DNA replication compartments and recruitment of associated viral and cellular proteins in transient cotransfection assays.Current approaches on viral infection: proteomics and functional validations.Herpes simplex virus ICP27 increases translation of a subset of viral late mRNAs.Herpes simplex virus 2 expresses a novel form of ICP34.5, a major viral neurovirulence factor, through regulated alternative splicing.Kaposi's sarcoma-associated herpesvirus ORF57 in viral RNA processing.Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication.The cellular RNA export receptor TAP/NXF1 is required for ICP27-mediated export of herpes simplex virus 1 RNA, but the TREX complex adaptor protein Aly/REF appears to be dispensable.Polyadenylylated nuclear RNA encoded by Kaposi sarcoma-associated herpesvirus.Herpes simplex virus ICP27 regulates alternative pre-mRNA polyadenylation and splicing in a sequence-dependent manner.Herpesvirus protein ICP27 switches PML isoform by altering mRNA splicing.Alternative splicing: the pledge, the turn, and the prestige : The key role of alternative splicing in human biological systems.The immediate-early gene product encoded by open reading frame 57 of herpesvirus saimiri modulates gene expression at a posttranscriptional level.Identification of a domain in human immunodeficiency virus type 1 rev that is required for functional activity and modulates association with subnuclear compartments containing splicing factor SC35Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32.ICP27 interacts with SRPK1 to mediate HSV splicing inhibition by altering SR protein phosphorylation.Herpes simplex virus type 1 protein IE63 affects the nuclear export of virus intron-containing transcripts.Shuttling of the herpes simplex virus type 1 regulatory protein ICP27 between the nucleus and cytoplasm mediates the expression of late proteins.Herpes simplex virus-1 infection causes the secretion of a type I interferon-antagonizing protein and inhibits signaling at or before Jak-1 activation.
P2860
Q22003919-176BDF89-030C-43E6-BD6B-6EE59277B712Q24537648-722E6133-22EA-4675-9FD3-7151897A26DCQ24538841-32ABFD47-FA07-44C6-806A-592892561E83Q24806787-4E8CF7EA-74EF-4DD7-AC11-17AF71EE1FECQ30453521-EB1C2ACB-BCF4-42C1-BDED-033E9161D471Q33317262-1E2D75F6-0071-47BF-AD88-C95C71B776BFQ33644930-024E21BA-4FF9-43F0-921D-156481EDC340Q33648884-A4D8F1BB-01A6-47A8-8391-FE805D5B6565Q33648948-9D8F232D-F1D3-497C-9A59-AF7D5BA497F5Q33707490-D6C51410-C91F-4B7A-B2EA-A4124DD145EDQ33707539-345B7EA0-E70B-424A-9A8B-98BF9869F863Q33785161-449ED4E6-B462-4951-ACA6-DE0A6FC2F6BDQ33800212-C56F8FDA-F03E-4A56-B855-113061D637B6Q33800574-16EE77D7-8491-440F-9816-C5F512E6357AQ33809422-E69B0FAA-6F62-4EDB-9779-09C043C7AA10Q33809951-52129562-236C-4BB4-BBE6-9A67077AD8DEQ33995747-ACF3FF91-6E99-43CE-A4A5-0C4A49446850Q34083087-EDBFE892-E06E-4548-B5DC-EA81A10D1B49Q34359278-0741A2E2-50D8-4BB2-B0A2-A09FCC041E24Q35125136-B9EA4879-EA61-44E9-9A94-AD3ECA55CFABQ35194372-38DA8D75-BEB4-4A78-919B-1D84FA77F52BQ35871646-51BA6E39-E855-4E8C-8ECF-BB8820B1D253Q35881315-C1A81206-B317-4B50-A5CF-5158A9BBA812Q36404090-21082754-4094-4287-A10D-6426432F6A43Q36498119-FD5E659F-D772-4A06-A091-B807704CC0ACQ36827252-97C4A014-9BD4-4837-969B-ACDEA55A233FQ37125662-DE169823-8B90-4339-B358-16BC25B103D9Q37191893-7B91217F-5C9E-4CC7-96F6-797141D086F5Q37232829-D05584C1-A8D0-4B16-88AD-E66F4490859DQ37273424-2650EF5D-49FF-43C6-B539-B8AFCF6101E2Q37379851-2C5A32EA-A201-415E-8E99-BE0B6F042ED0Q37406026-479ABDEE-AE95-4522-AA5C-332D666984E9Q38735423-B2A0121F-2FBA-46ED-98ED-944F32FF79B5Q39577543-FBD03085-ACAF-4038-B49A-3F9D34928DBEQ39593808-1264DDD4-4BBE-4C2D-91B5-80F991AD9BCDQ39597946-5562DC05-C657-44CF-A878-75FF3B3BAE0AQ39744901-28FAE78D-2825-49F7-BDBB-193554F8F81FQ39875527-5AC115B8-7CE5-4D69-913B-88D908CB2D00Q40015345-64BF4C14-A197-45C6-BBB9-3B636E6FDB94Q42695727-A1791478-BC1C-43E8-9D41-E00E86DD3DB8
P2860
The herpes simplex virus type 1 regulatory protein ICP27 coimmunoprecipitates with anti-Sm antiserum, and the C terminus appears to be required for this interaction
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
The herpes simplex virus type ...... required for this interaction
@ast
The herpes simplex virus type ...... required for this interaction
@en
type
label
The herpes simplex virus type ...... required for this interaction
@ast
The herpes simplex virus type ...... required for this interaction
@en
prefLabel
The herpes simplex virus type ...... required for this interaction
@ast
The herpes simplex virus type ...... required for this interaction
@en
P2860
P1433
P1476
The herpes simplex virus type ...... required for this interaction
@en
P2093
M K Hibbard
R M Sandri-Goldin
P2860
P304
P407
P577
1996-01-01T00:00:00Z