Interaction of herpes simplex virus 1 alpha regulatory protein ICP0 with elongation factor 1delta: ICP0 affects translational machinery.
about
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.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 infectionThe bovine herpesvirus 1 immediate-early protein (bICP0) associates with histone deacetylase 1 to activate transcription.Herpes simplex virus 1 alpha regulatory protein ICP0 interacts with and stabilizes the cell cycle regulator cyclin D3The herpes simplex virus ICP0 RING finger domain inhibits IRF3- and IRF7-mediated activation of interferon-stimulated genesHerpes simplex virus type 1 immediate-early protein ICP27 is required for efficient incorporation of ICP0 and ICP4 into virionsInfected cell protein 0 functional domains and their coordination in herpes simplex virus replicationThe role of the CoREST/REST repressor complex in herpes simplex virus 1 productive infection and in latencyBovine 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 potential link between PML NBs and ICP0 in regulating lytic and latent infection of HSV-1Interaction of the equine herpesvirus 1 EICP0 protein with the immediate-early (IE) protein, TFIIB, and TBP may mediate the antagonism between the IE and EICP0 proteinsPosttranslational processing of infected cell proteins 0 and 4 of herpes simplex virus 1 is sequential and reflects the subcellular compartment in which the proteins localizeInteraction of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP) with HS1-associated protein X-1: implication of cytoplasmic function of EBNA-LP.Transactivator protein BICP0 of bovine herpesvirus 1 (BHV-1) is blocked by prostaglandin D2 (PGD2), which points to a mechanism for PGD2-mediated inhibition of BHV-1 replication.Cellular localization of the herpes simplex virus ICP0 protein dictates its ability to block IRF3-mediated innate immune responsesICP0 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.Cellular elongation factor 1delta is modified in cells infected with representative alpha-, beta-, or gammaherpesvirusesTowards an understanding of the herpes simplex virus type 1 latency-reactivation cycleRole of herpes simplex virus 1 immediate early protein ICP22 in viral nuclear egress.Eukaryotic elongation factor 1delta is hyperphosphorylated by the protein kinase encoded by the U(L)13 gene of herpes simplex virus 1Persistence and expression of the herpes simplex virus genome in the absence of immediate-early proteins.Herpes simplex virus type 1 UL51 protein is involved in maturation and egress of virus particles.Characterization of the trans-activation properties of equine herpesvirus 1 EICP0 proteinColocalization of the herpes simplex virus 1 UL4 protein with infected cell protein 22 in small, dense nuclear structures formed prior to onset of DNA synthesisTranslation elongation factor 1-alpha interacts specifically with the human immunodeficiency virus type 1 Gag polyproteinTruncation 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.Requirements for the nuclear-cytoplasmic translocation of infected-cell protein 0 of herpes simplex virus 1Identification of major phosphorylation sites of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP): ability of EBNA-LP to induce latent membrane protein 1 cooperatively with EBNA-2 is regulated by phosphorylationRole of cyclin D3 in the biology of herpes simplex virus 1 ICPO.The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors.Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymesNovel 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.Deletion of the herpes simplex virus VP22-encoding gene (UL49) alters the expression, localization, and virion incorporation of ICP0.Translational control of viral gene expression in eukaryotesHSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0.Herpes simplex virus 1 alpha regulatory protein ICP0 functionally interacts with cellular transcription factor BMAL1.Herpes simplex virus immediate-early ICP0 protein inhibits Toll-like receptor 2-dependent inflammatory responses and NF-kappaB signaling
P2860
Q22003919-21EAB42B-D5E7-4179-A417-07F6D4F6C1D6Q22009164-C0CCC076-30A9-4634-AE10-9B0050D06081Q24291697-230BD23F-4BCC-4A1A-B6CE-604310E1F2B9Q24314541-A1DC1E5C-330B-4E46-B4CC-3E9FE5B64A19Q24607496-2C1E2420-E764-43AB-BD70-90D3691811D1Q24657245-E3A6940B-8CAD-454E-9E0B-D9926F5012FFQ26766356-837D4D10-4251-476C-88AD-F208DEBEC5D3Q26823532-4A3655A5-CC99-4228-A915-CDB238D567E5Q26864175-C7BE7E6A-8C8B-4D40-BB4F-0E8D1C92A440Q27027918-17337FAA-967C-4215-82E0-510616D04585Q28115197-1FB5705F-B9C2-4668-A1F7-D07092DEB5A8Q28345181-1D09F643-0F14-40EA-A595-574FE658B6BCQ30939262-7D1B3290-9954-48B7-85C1-FBBE925D94C3Q33200367-1557361D-24B6-4E57-82B4-BABF9DC9AF88Q33573566-42623AF7-4314-4FCF-AEFA-C241FFE801A3Q33603489-A04AF7A1-D648-4670-AD83-A973DA83C7F0Q33614341-FE7B6058-39A4-4E8F-AC6E-F5813A2914A8Q33648613-7F748E94-1F18-4B54-B3D5-2BC3BDF5FE3FQ33654414-78E78FA7-7830-4BF2-AEDA-0F33035F5E78Q33744046-41DFC406-C196-40DD-9C45-3FE7409EE9EAQ33782229-ADAFE0F9-A0ED-4A96-B41A-938B19D4E07DQ33783411-34656A77-70A0-4B80-B002-3FE8756D6193Q33788695-68C968A3-A34B-4CE6-8C8E-119919216C94Q33793131-E20CC20F-9EB4-402F-9BA8-1C73F6A81C97Q33814451-028CD21F-B98A-4DCB-9199-105DFFBDEE12Q33814996-CE13835F-1924-4DFC-BEF0-50CE3643A2FEQ33824256-212513C3-D207-4258-86D4-A17242427129Q33838501-F8672AAF-80F3-4A9F-A2AB-B2D2D71FBAAAQ33851331-08ADEFFD-C102-4E8F-85AA-9C85E459965EQ33851767-FC6EA122-9930-4649-800D-13F908F1D80AQ33854952-856B3087-93EC-493F-86FB-E28DDEEB2E42Q33879094-BD5DE744-9668-4D26-845A-BB92CA95B747Q33894274-C0D89298-B05E-47AE-9149-33E835696F9AQ33900347-D33055A3-41E2-4BB1-A2AE-CB75BDE238ACQ33908744-074C21D9-1833-4E7C-9F43-F7CB8BC93B1DQ33935121-CBAA51FB-B134-43EA-B41D-AEA8B8BB5519Q33995747-9E4AC6C0-8977-4D5D-96B6-0AACF192E0E8Q34030278-4DECFDBE-ABE1-48D2-A0EE-59A4C6525DBFQ34108700-246BFE7F-C0A9-4E31-8F6F-2D8792F33CB8Q34178155-3693EA21-DF40-4BA3-B0F5-B27EB18320AF
P2860
Interaction of herpes simplex virus 1 alpha regulatory protein ICP0 with elongation factor 1delta: ICP0 affects translational machinery.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Interaction of herpes simplex ...... fects translational machinery.
@ast
Interaction of herpes simplex ...... fects translational machinery.
@en
type
label
Interaction of herpes simplex ...... fects translational machinery.
@ast
Interaction of herpes simplex ...... fects translational machinery.
@en
prefLabel
Interaction of herpes simplex ...... fects translational machinery.
@ast
Interaction of herpes simplex ...... fects translational machinery.
@en
P2860
P1433
P1476
Interaction of herpes simplex ...... fects translational machinery.
@en
P2093
P2860
P304
P407
P577
1997-02-01T00:00:00Z