A herpesvirus regulatory protein appears to act post-transcriptionally by affecting mRNA processing.
about
A novel cellular protein, p60, interacting with both herpes simplex virus 1 regulatory proteins ICP22 and ICP0 is modified in a cell-type-specific manner and Is recruited to the nucleus after infectionFunctional interaction between pleiotropic transactivator pUL69 of human cytomegalovirus and the human homolog of yeast chromatin regulatory protein SPT6Temporal gene regulation of the channel catfish virus (Ictalurid herpesvirus 1).A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory proteinA novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory proteinVaricella-zoster virus open reading frame 61 protein is functionally homologous to herpes simplex virus type 1 ICP03' end mRNA processing: molecular mechanisms and implications for health and diseaseVaricella-zoster virus (VZV) open reading frame 61 protein transactivates VZV gene promoters and enhances the infectivity of VZV DNAHerpesvirus Late Gene Expression: A Viral-Specific Pre-initiation Complex Is KeyProcessing and transcriptome expansion at the mRNA 3' end in health and disease: finding the right endBovine Herpes Virus 1 (BHV-1) and Herpes Simplex Virus Type 1 (HSV-1) Promote Survival of Latently Infected Sensory Neurons, in Part by Inhibiting ApoptosisA novel transferable nuclear export signal mediates CRM1-independent nucleocytoplasmic shuttling of the human cytomegalovirus transactivator protein pUL69Mta has properties of an RNA export protein and increases cytoplasmic accumulation of Epstein-Barr virus replication gene mRNA.Identification of herpes simplex virus RNAs that interact specifically with regulatory protein ICP27 in vivo.The herpes simplex virus type 1 regulatory protein ICP27 is required for the prevention of apoptosis in infected human cells.Analysis of the phosphorylation sites of herpes simplex virus type 1 regulatory protein ICP27.The C-terminal region but not the Arg-X-Pro repeat of Epstein-Barr virus protein EB2 is required for its effect on RNA splicing and transportTowards an understanding of the herpes simplex virus type 1 latency-reactivation cycleICP27 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.Persistence and expression of the herpes simplex virus genome in the absence of immediate-early proteins.Purification and characterization of a cellular protein that binds to the downstream activation sequence of the strict late UL38 promoter of herpes simplex virus type 1The Epstein-Barr virus (EBV) SM protein enhances pre-mRNA processing of the EBV DNA polymerase transcript.The human herpesvirus 8 homolog of Epstein-Barr virus SM protein (KS-SM) is a posttranscriptional activator of gene expressionHerpesvirus 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.The conserved carboxyl-terminal half of herpes simplex virus type 1 regulatory protein ICP27 is dispensable for viral growth in the presence of compensatory mutationsIdentification of an export control sequence and a requirement for the KH domains in ICP27 from herpes simplex virus type 1Induction and prevention of apoptosis in human HEp-2 cells by herpes simplex virus type 1.Accumulation of herpes simplex virus type 1 early and leaky-late proteins correlates with apoptosis prevention in infected human HEp-2 cells.Epstein-Barr virus SM protein interacts with mRNA in vivo and mediates a gene-specific increase in cytoplasmic mRNA.Molecular mechanisms of eukaryotic pre-mRNA 3' end processing regulation.Herpes simplex virus type 1 infection leads to loss of serine-2 phosphorylation on the carboxyl-terminal domain of RNA polymerase II.Activation of HIV-1 pre-mRNA 3' processing in vitro requires both an upstream element and TAR.An early regulatory function required in a cell type-dependent manner is expressed by the genomic but not the cDNA copy of the herpes simplex virus 1 gene encoding infected cell protein 0.Epstein-Barr virus mRNA export factor EB2 is essential for production of infectious virus.Importance of codon usage for the temporal regulation of viral gene expressionAlternative poly(A) site selection in complex transcription units: means to an end?Herpes simplex virus type 1 and bovine herpesvirus 1 latency.
P2860
Q22009164-CE8FD6A4-AF52-4183-A844-915594E3603FQ22254757-4E25432F-59DD-4F29-8B8E-7467866674BCQ24523033-12F293CA-C7E8-4367-90B6-8306ABBD9A5FQ24532092-F4ECD82A-07E1-4B3A-A80A-16BA80404C04Q24532134-B1242466-EBC1-4DAD-B809-AC426EEF5050Q24647866-67CE58AA-E735-4B54-9462-1A08B9D28D45Q24648650-7D7680A3-1BE1-4E20-9818-86DBC2BF07F3Q24656106-DE0AAF5E-480A-4768-89C3-F452DF695F7FQ26745059-84E56204-E835-4A8C-A822-25F59FF5F37FQ26746120-182E2164-FDFC-4D95-BBA1-10DF022E02B7Q26864175-9F3BCF91-5B8F-487A-A13A-41CED4D34F45Q28366352-E317149B-031D-4310-A385-97C04BEB8CD5Q30453521-9DC385AF-91CF-41D9-AFC8-AD1AAD4C3A5DQ30941982-3408947D-0B1D-482C-9EF0-6A087F8A910AQ33643356-20BCA5BF-3FC0-4679-B8EC-8C02C307A704Q33644930-9783D632-11B0-4456-9FBF-D97F8FC8CEE2Q33647481-BF3BB3D5-9919-4AC2-B245-A665B073801BQ33654414-F1E5EAA7-70D4-467C-A73F-16B8680D1C53Q33707490-4525A71C-7F3B-4D34-B6B7-E25DBA959D98Q33707539-A7B2A4C0-6E30-42EA-BEAD-2E202CBB2212Q33783411-26EED9A0-15B8-45B4-B397-ABC302EFA613Q33784868-5D8E0ACA-05E1-40CC-B7B2-CB248D21BC10Q33785161-A4E0F17A-1698-440C-88F7-B4A16D563E06Q33796895-76B2D1BF-9190-4313-BC8C-9FA223242252Q33800212-A93E8905-62A0-48F2-AC3B-8D648FCFA47BQ33800574-64111AC3-99D6-47E1-8248-D19DEACE9BD9Q33809422-C65D3DE9-5678-4381-86E5-B4A61E2FDA8AQ33809511-130C092F-AA93-4D58-A041-3EB143E90CFAQ33809951-165F318F-8631-4618-86F2-EE331B8C50E2Q33825495-C1F533DA-6229-4F39-AB12-9EC7EA95D44AQ33835841-CDE70592-BE8F-4DE8-8DA5-0605B68551F8Q33842488-027C5F95-F026-4B48-A650-2B9B14A945A4Q33871092-F4D16760-0732-4B9D-A90C-224E19EACCB8Q33930346-F4C87401-D131-48CE-ABC4-F5E88663BD0EQ33938737-FAD7329E-1D0D-476F-9575-A8CCB8B4F5B2Q34346572-AC4F17FC-44FE-438B-B5E7-B3D9EAC4BE41Q34347652-9AD55D7C-667C-432E-A3B4-DC5C680655E7Q34499526-DDEB1719-B0C7-4C8F-9C36-0B799101E37AQ34630891-50CF6C29-4F92-44F3-A9E6-FA7CFDE98BB3Q35044114-DE847AD6-5688-43B8-8EB9-7A3688EE5D7F
P2860
A herpesvirus regulatory protein appears to act post-transcriptionally by affecting mRNA processing.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh-hant
name
A herpesvirus regulatory prote ...... by affecting mRNA processing.
@en
A herpesvirus regulatory prote ...... by affecting mRNA processing.
@nl
type
label
A herpesvirus regulatory prote ...... by affecting mRNA processing.
@en
A herpesvirus regulatory prote ...... by affecting mRNA processing.
@nl
prefLabel
A herpesvirus regulatory prote ...... by affecting mRNA processing.
@en
A herpesvirus regulatory prote ...... by affecting mRNA processing.
@nl
P356
P1433
P1476
A herpesvirus regulatory prote ...... by affecting mRNA processing.
@en
P2093
Mendoza GE
Sandri-Goldin RM
P304
P356
10.1101/GAD.6.5.848
P577
1992-05-01T00:00:00Z