Point mutations in the herpes simplex virus type 1 Vmw110 RING finger helix affect activation of gene expression, viral growth, and interaction with PML-containing nuclear structures.
about
ICP0 dismantles microtubule networks in herpes simplex virus-infected cellsHerpes simplex virus 2 ICP0 mutant viruses are avirulent and immunogenic: implications for a genital herpes vaccineThe bovine herpesvirus 1 immediate-early protein (bICP0) associates with histone deacetylase 1 to activate transcription.The infected cell protein 0 encoded by bovine herpesvirus 1 (bICP0) associates with interferon regulatory factor 7 and consequently inhibits beta interferon promoter activityViral 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 bodiesConjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus.Inactivating a cellular intrinsic immune defense mediated by Daxx is the mechanism through which the human cytomegalovirus pp71 protein stimulates viral immediate-early gene expressionThe herpes simplex virus ICP0 RING finger domain inhibits IRF3- and IRF7-mediated activation of interferon-stimulated genesFunctional inaccessibility of quiescent herpes simplex virus genomesInfected cell protein 0 functional domains and their coordination in herpes simplex virus replicationBovine Herpes Virus 1 (BHV-1) and Herpes Simplex Virus Type 1 (HSV-1) Promote Survival of Latently Infected Sensory Neurons, in Part by Inhibiting ApoptosisThe APC11 RING-H2 finger mediates E2-dependent ubiquitination.HSV-1 ICP0: paving the way for viral replicationA viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defenceSpatial and Temporal Resolution of Global Protein Synthesis during HSV Infection Using Bioorthogonal Precursors and Click ChemistryDrosophila male-specific lethal-2 protein: structure/function analysis and dependence on MSL-1 for chromosome association.ICP0 induces the accumulation of colocalizing conjugated ubiquitin.Herpes simplex virus tegument ICP0 is capsid associated, and its E3 ubiquitin ligase domain is important for incorporation into virions.Towards an understanding of the herpes simplex virus type 1 latency-reactivation cycleCharacterization of the trans-activation properties of equine herpesvirus 1 EICP0 proteinPerturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0.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 ICP0Efficient activation of viral genomes by levels of herpes simplex virus ICP0 insufficient to affect cellular gene expression or cell survival.Novel roles of cytoplasmic ICP0: proteasome-independent functions of the RING finger are required to block interferon-stimulated gene production but not to promote viral replication.Disruption of PML nuclear bodies is mediated by ORF61 SUMO-interacting motifs and required for varicella-zoster virus pathogenesis in skin.Herpes simplex virus immediate-early ICP0 protein inhibits Toll-like receptor 2-dependent inflammatory responses and NF-kappaB signalingA pre-immediate-early role for tegument ICP0 in the proteasome-dependent entry of herpes simplex virusBarrier to auto integration factor becomes dephosphorylated during HSV-1 Infection and Can Act as a host defense by impairing viral DNA replication and gene expressionRole of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1Attenuation of DNA-dependent protein kinase activity and its catalytic subunit by the herpes simplex virus type 1 transactivator ICP0.Interaction of herpes simplex virus 1 alpha regulatory protein ICP0 with elongation factor 1delta: ICP0 affects translational machinery.A single 13-kilobase divergent locus in the Kaposi sarcoma-associated herpesvirus (human herpesvirus 8) genome contains nine open reading frames that are homologous to or related to cellular proteins.The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PML-associated nuclear bodies at very early times in infected permissive cells.The herpes simplex virus type 1 immediate-early protein ICP0 is necessary for the efficient establishment of latent infection.Mutational 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.Cytoplasmic localized infected cell protein 0 (bICP0) encoded by bovine herpesvirus 1 inhibits β interferon promoter activity and reduces IRF3 (interferon response factor 3) protein levels.Herpes simplex virus type 1 ICP0 phosphorylation mutants impair the E3 ubiquitin ligase activity of ICP0 in a cell type-dependent manner.The zinc RING finger of bovine herpesvirus 1-encoded bICP0 protein is crucial for viral replication and virulence.Two overlapping regions within the N-terminal half of the herpes simplex virus 1 E3 ubiquitin ligase ICP0 facilitate the degradation and dissociation of PML and dissociation of Sp100 from ND10.
P2860
Q21136348-8310187E-BE5E-4820-B20E-BE708D8C4795Q21562177-81922C48-2CBC-4189-BD49-68AEA0415D41Q24291697-F762FBB6-B42C-415A-B2B6-EC2E20B07B48Q24322885-04CFE224-6CA9-4D6D-9FDF-ED36C5145366Q24527246-BCF5E340-A6C0-4614-AED6-F9E2CF0575A2Q24529499-87584BA9-6756-434A-A96E-F99C7F504E07Q24532901-C0F2988D-6E65-4D0D-8E89-FC609CD89E46Q24543400-83242DD5-756A-426B-9E36-38DCD5FF241FQ24607496-FF4A5DB1-63EB-4A2E-BA13-1ABA8417E351Q24815909-11C4F6BF-7C08-454E-AE54-71E98F0EDF62Q26766356-81ECE2C7-6666-4227-9047-E54B63A27008Q26864175-3671396F-7A0C-4702-A2D3-8A812CF2BAECQ27934826-82D21F29-DB97-41EF-8906-D46F29D53531Q28243426-2D9C08E5-5C9C-4A7F-A275-1B8B9D903BD7Q28477120-709CDEA7-F467-4371-9D3D-005D1EFC6DA8Q28554486-43042E84-3BDF-4BF0-A9D0-CA61FD750629Q30429073-BAFA01AB-8D65-4412-8284-EC08B32B01ECQ33603489-0584D6C0-1505-4F70-807E-720712E1EDC1Q33614341-E7949F3E-542A-4494-99F4-8BAE311D6007Q33654414-4770E8E7-E4C4-4758-9453-F5DDF83B244DQ33793131-9EF0089F-756B-4D9F-A0BE-23B27DE1299BQ33819612-6983758B-C2E3-40CE-9418-AB89E614006AQ33824256-A24DF706-2C57-4E98-B6EC-C61DB0AB464AQ33838501-84FB74C0-842B-4F32-A955-FB44C336F285Q33900347-3ED024A9-C056-45D3-BA5E-72E5F49949CEQ34013598-52B07A8C-780C-47AB-971C-9884B1B1529CQ34178155-0B2A15DB-85E6-428F-9DFA-E4E6AD024C58Q35077043-27EBFC87-1CD1-4C85-BFED-7498C9E6E513Q35191248-7D913865-DCCF-4144-B3BF-6BB8271DF93AQ35667107-B89212A3-673B-407A-9968-544D978A3961Q35871672-44542041-6C6F-49D0-9661-883FE8527231Q35876353-4E2755D8-64D2-4537-AABC-3D36111CA519Q35878042-27FA7FCD-4A9A-4F5E-BFA1-C8DF9D0F8CBBQ35886859-094D0F65-5CFA-418E-B60C-80B90C87EE3AQ35891871-26966E01-0B11-4960-B527-1ED91D5953FFQ35898699-D5F88FDF-C6DB-4E78-8BFD-06F29A7E9ACDQ36142258-542C2F29-694A-48A1-950B-873991C8F3AAQ36949684-DDBEE15F-7610-421B-BDA2-3A89B76E1B4FQ36994602-FF883D1C-39F1-4922-8CB6-9DAFB6F8C590Q37336832-AEECBC41-FE64-492C-AE69-D8416DA27C97
P2860
Point mutations in the herpes simplex virus type 1 Vmw110 RING finger helix affect activation of gene expression, viral growth, and interaction with PML-containing nuclear structures.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Point mutations in the herpes ...... containing nuclear structures.
@en
Point mutations in the herpes ...... containing nuclear structures.
@nl
type
label
Point mutations in the herpes ...... containing nuclear structures.
@en
Point mutations in the herpes ...... containing nuclear structures.
@nl
prefLabel
Point mutations in the herpes ...... containing nuclear structures.
@en
Point mutations in the herpes ...... containing nuclear structures.
@nl
P2093
P2860
P1433
P1476
Point mutations in the herpes ...... -containing nuclear structures
@en
P2093
P2860
P304
P407
P577
1995-11-01T00:00:00Z