Herpes simplex virus phosphoproteins. I. Phosphate cycles on and off some viral polypeptides and can alter their affinity for DNA.
about
Association of a protein phosphatase 1 activity with the human factor C1 (HCF) complexA single serine residue at position 375 of VP16 is critical for complex assembly with Oct-1 and HCF and is a target of phosphorylation by casein kinase IIHerpes simplex virus 1 mutant deleted in the alpha 22 gene: growth and gene expression in permissive and restrictive cells and establishment of latency in miceHerpes simplex virus type 1 immediate-early protein ICP27 is required for efficient incorporation of ICP0 and ICP4 into virionsHerpes simplex virus 1 protein kinase is encoded by open reading frame US3 which is not essential for virus growth in cell cultureInfected cell protein 0 functional domains and their coordination in herpes simplex virus replicationHSV-1 ICP0: paving the way for viral replicationPosttranslational processing of infected cell proteins 0 and 4 of herpes simplex virus 1 is sequential and reflects the subcellular compartment in which the proteins localizeAnalysis 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.Phosphorylation of the human cytomegalovirus 86-kilodalton immediate-early protein IE2.The PK domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) is required for immediate-early gene expression and virus growthNuclear accumulation of IE62, the varicella-zoster virus (VZV) major transcriptional regulatory protein, is inhibited by phosphorylation mediated by the VZV open reading frame 66 protein kinaseAccumulation of herpes simplex virus type 1 early and leaky-late proteins correlates with apoptosis prevention in infected human HEp-2 cells.Construction and properties of a cell line constitutively expressing the herpes simplex virus glycoprotein B dependent on functional alpha 4 protein synthesisDirect stimulation of translation by the multifunctional herpesvirus ICP27 protein.The cyclin-dependent kinase inhibitor roscovitine inhibits the transactivating activity and alters the posttranslational modification of herpes simplex virus type 1 ICP0.Molecular genetics of herpes simplex virus. VII. Characterization of a temperature-sensitive mutant produced by in vitro mutagenesis and defective in DNA synthesis and accumulation of gamma polypeptidesHerpes simplex virus 1 ICP0 phosphorylation site mutants are attenuated for viral replication and impaired for explant-induced reactivation.Alpha 4, the major regulatory protein of herpes simplex virus type 1, is stably and specifically associated with promoter-regulatory domains of alpha genes and of selected other viral genes.Herpes simplex virus immediate early infected-cell polypeptide 4 binds to DNA and promotes transcriptionDNA-binding site of major regulatory protein alpha 4 specifically associated with promoter-regulatory domains of alpha genes of herpes simplex virus type 1Intracellular localization of the herpes simplex virus type 1 major transcriptional regulatory protein, ICP4, is affected by ICP27Repression of the herpes simplex virus 1 alpha 4 gene by its gene product (ICP4) within the context of the viral genome is conditioned by the distance and stereoaxial alignment of the ICP4 DNA binding site relative to the TATA boxArginine-rich regions succeeding the nuclear localization region of the herpes simplex virus type 1 regulatory protein ICP27 are required for efficient nuclear localization and late gene expressionFunctional interactions between herpes simplex virus immediate-early proteins during infection: gene expression as a consequence of ICP27 and different domains of ICP4.An activity specified by the osteosarcoma line U2OS can substitute functionally for ICP0, a major regulatory protein of herpes simplex virus type 1Initial characterization of the membrane-associated form of ICP4 of herpes simplex virus type 1The herpes simplex virus type 1 regulatory protein ICP27 coimmunoprecipitates with anti-Sm antiserum, and the C terminus appears to be required for this interactionRole of protein kinase A and the serine-rich region of herpes simplex virus type 1 ICP4 in viral replication.Repression of the alpha0 gene by ICP4 during a productive herpes simplex virus infection.Overexpression of the herpes simplex virus type 1 immediate-early regulatory protein, ICP27, is responsible for the aberrant localization of ICP0 and mutant forms of ICP4 in ICP4 mutant virus-infected cells.Prolonged gene expression and cell survival after infection by a herpes simplex virus mutant defective in the immediate-early genes encoding ICP4, ICP27, and ICP22.The RGG box motif of the herpes simplex virus ICP27 protein mediates an RNA-binding activity and determines in vivo methylation.The herpes simplex virus immediate-early protein ICP0 affects transcription from the viral genome and infected-cell survival in the absence of ICP4 and ICP27Mutational analysis of the herpes simplex virus type 1 ICP0 C3HC4 zinc ring finger reveals a requirement for ICP0 in the expression of the essential alpha27 gene.Codons 262 to 490 from the herpes simplex virus ICP4 gene are sufficient to encode a sequence-specific DNA binding protein.Structure of the C-Terminal Domain of the Multifunctional ICP27 Protein from Herpes Simplex Virus 1The interaction of ICP4 with cell/infected-cell factors and its state of phosphorylation modulate differential recognition of leader sequences in herpes simplex virus DNA.Activities of herpes simplex virus type 1 (HSV-1) ICP4 genes specifying nonsense peptides
P2860
Q24515330-F772200E-392B-4EC4-99F5-A6CB46E05C7EQ24532192-9662FAB8-33E9-4A13-9465-93448BD09293Q24645922-51E2BBC9-3FCE-4764-B4B3-721EE84C4CC3Q24657245-33CEF48E-186E-46DC-A18D-71FE5E95527AQ24658270-A2A9B44B-239C-4111-9779-198AC2648FB6Q26766356-A758D583-8FFA-42B2-9D92-3B129AA79733Q28243426-70C68A16-5CC1-4134-9FBE-C1A637BFA89EQ28345181-B1BC81FC-CCCE-4C9C-8993-11F6C8534C65Q33644930-958D4278-DF1E-4744-A84B-7FE4F0A87B5BQ33648884-907F994C-DD01-421E-B37C-E0F25C8D5CE2Q33784945-E4C5E3B0-90C9-4662-A891-F0FE9AFC33A7Q33785400-70A34037-031E-46A7-ABDC-3F3C41D9B534Q33798767-7570F62B-025C-4C0D-A414-B4F19D564583Q33835841-6C46A2FE-8E39-46ED-9663-345B5B17AB02Q33928829-F58B973C-B51B-4C10-A4AA-2C33748E40F7Q34302063-E5F6D09C-C043-439F-B9F2-AF40D1BFF061Q34330457-614052BC-61E5-4BBC-BC16-D8B6BAA8AAE9Q35235288-1AA332F2-F137-40C5-BE45-10D0A0E64C3BQ35531602-9CC11ED6-A422-49EC-995E-8010BCC642A2Q35604596-F4B43CD2-7974-46C0-9107-78817C94BC9BQ35609408-3A606D6B-C164-4160-A522-058E02626255Q35614166-4B655FFA-1ABF-4F74-AC0E-9DB601244C96Q35828561-52A0515A-6C09-419C-ACE2-885FA953AD1DQ35839047-AFC6AA84-C838-48E0-A52E-CCF8828CD8D6Q35844013-8ED12EDF-EE19-436C-8CD2-5AE053E591E5Q35845959-63554759-0CD9-4A1E-89C3-CBAA44DE3125Q35848104-03853A89-F387-48FF-B587-CFDE96DB8774Q35849175-E6248EFF-729E-49F4-BA0D-DA219AF9E920Q35853293-9F70640E-73A5-4D72-81E5-B77DD3713C5AQ35854807-A5BA7DF8-D1FB-4B76-B38C-7C61425F9A0DQ35861084-6CA5E0CB-E3B3-408A-AB8F-397FC2AC13DEQ35866195-5B7843A7-82F0-4F3A-8E2B-43ED3A9E181EQ35868577-7A499DEC-8415-4A21-BD7F-F37C82CE8BEEQ35871646-AF342E0F-365A-4ECB-BDB6-01F25D6AD07BQ35886888-B71B51F2-FC84-455E-ADA7-4561A58DA7AEQ35898699-D4A519A1-DD3A-4FA6-8FD9-E749387CD65FQ35907591-A6E2339C-8612-43AF-9EED-371D21F6F469Q35913888-13A73DCF-FD36-4B18-99B4-637E2525AEEEQ35921488-BB90B8B7-96A9-4E42-9F2C-45976FA7BA26Q36129181-B34CF4E1-97B0-4C6F-863E-E12DCAB2977C
P2860
Herpes simplex virus phosphoproteins. I. Phosphate cycles on and off some viral polypeptides and can alter their affinity for DNA.
description
1980 nî lūn-bûn
@nan
1980 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1980 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1980年の論文
@ja
1980年論文
@yue
1980年論文
@zh-hant
1980年論文
@zh-hk
1980年論文
@zh-mo
1980年論文
@zh-tw
1980年论文
@wuu
name
Herpes simplex virus phosphopr ...... alter their affinity for DNA.
@ast
Herpes simplex virus phosphopr ...... alter their affinity for DNA.
@en
type
label
Herpes simplex virus phosphopr ...... alter their affinity for DNA.
@ast
Herpes simplex virus phosphopr ...... alter their affinity for DNA.
@en
prefLabel
Herpes simplex virus phosphopr ...... alter their affinity for DNA.
@ast
Herpes simplex virus phosphopr ...... alter their affinity for DNA.
@en
P2093
P2860
P1433
P1476
Herpes simplex virus phosphopr ...... alter their affinity for DNA.
@en
P2093
P2860
P304
P407
P577
1980-01-01T00:00:00Z