Herpes simplex virus ICP27 increases translation of a subset of viral late mRNAs.
about
Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathwaysKaposi's sarcoma-associated herpesvirus ORF57 protein interacts with PYM to enhance translation of viral intronless mRNAsRecruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replicationModulation of the Translational Landscape During Herpesvirus InfectionICP27 phosphorylation site mutants are defective in herpes simplex virus 1 replication and gene expression.Human cytomegalovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4EBP1Regulation of viral gene expression by duck enteritis virus UL54.Viral and cellular mRNA-specific activators harness PABP and eIF4G to promote translation initiation downstream of cap bindingThe suppression of apoptosis by α-herpesvirus.Herpes simplex virus 1 regulatory protein ICP27 undergoes a head-to-tail intramolecular interaction.Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export.Role of herpes simplex virus ICP27 in the degradation of mRNA by virion host shutoff RNaseHerpesviral replication compartments move and coalesce at nuclear speckles to enhance export of viral late mRNA.Relay of herpes simplex virus between Langerhans cells and dermal dendritic cells in human skin.An Epstein-Barr Virus-Encoded Protein Complex Requires an Origin of Lytic Replication In Cis to Mediate Late Gene Transcription.The structure of the folded domain from the signature multifunctional protein ICP27 from herpes simplex virus-1 reveals an intertwined dimer.Duck enteritis virus UL54 is an IE protein primarily located in the nucleus.Distribution and dynamics of transcription-associated proteins during parvovirus infection.Extreme dependence of gH and gL expression on ORF57 and association with highly unusual codon usage in rhesus monkey rhadinovirusHerpes simplex virus type 1 ICP27 regulates expression of a variant, secreted form of glycoprotein C by an intron retention mechanism.Selective degradation of mRNAs by the HSV host shutoff RNase is regulated by the UL47 tegument protein.Translation of intronless RNAs is strongly stimulated by the Epstein-Barr virus mRNA export factor EB2.Anti HSV-1 activity of halistanol sulfate and halistanol sulfate C isolated from Brazilian marine sponge Petromica citrina (Demospongiae).The HSV-1 ICP27 RGG box specifically binds flexible, GC-rich sequences but not G-quartet structuresThe many roles of the highly interactive HSV protein ICP27, a key regulator of infection.The Kaposi's Sarcoma-Associated Herpesvirus ORF57 Protein and Its Multiple Roles in mRNA Biogenesis.Deciphering novel host-herpesvirus interactions by virion proteomics.Tinkering with translation: protein synthesis in virus-infected cells.Functional comparison of herpes simplex virus 1 (HSV-1) and HSV-2 ICP27 homologs reveals a role for ICP27 in virion release.The herpes simplex virus 2 virion-associated ribonuclease vhs interferes with stress granule formationAntiherpetic potential of 6-bromoindirubin-3'-acetoxime (BIO-acetoxime) in human oral epithelial cells.Rhesus monkey rhadinovirus ORF57 induces gH and gL glycoprotein expression through posttranscriptional accumulation of target mRNAs.Duck enteritis virus (DEV) UL54 protein, a novel partner, interacts with DEV UL24 protein.Antiherpes evaluation of soybean isoflavonoids.Poly(A)-binding protein 1 partially relocalizes to the nucleus during herpes simplex virus type 1 infection in an ICP27-independent manner and does not inhibit virus replicationHerpes simplex virus-1 infection causes the secretion of a type I interferon-antagonizing protein and inhibits signaling at or before Jak-1 activation.Herpes simplex virus proteins ICP27 and UL47 associate with polyadenylate-binding protein and control its subcellular distribution.Epstein-Barr virus protein EB2 stimulates translation initiation of mRNAs through direct interactions with both PABP and eIF4G.Effects of Ilex paraguariensis A. St. Hil. (yerba mate) on herpes simplex virus types 1 and 2 replication.
P2860
Q24305296-6F26445E-F32B-4A9F-AA15-51FD76825DA0Q24309306-FEBB4F59-76DA-46A4-8476-2919A2D67C54Q24310689-B8BF9637-6BDD-4CA5-919F-BC762E690270Q28078469-404A55C5-52ED-4584-A962-9276D7DE75EBQ33648884-AB1D17A9-0169-4EA1-9359-C3005C6F66FFQ33664623-9525540C-D4FF-479C-846D-9F331263A8B7Q33682363-ACCC0A9D-2884-420C-AADB-8E4F56F86D40Q33810337-B5C22515-2E76-4237-91CA-14EF8EEB1DDBQ33815866-4E8F2FB3-C7F6-4F9F-BBDA-89459C8C0E70Q33826787-2E14D850-BF5A-4AEC-8F76-3C0BFEBCBCF0Q33990699-727061D8-7B95-4425-8956-876C7BA4D2A1Q34120868-049ACC06-4EF6-493C-9159-D0BE5E65E1FEQ35008429-1B10AD4C-4D77-4DC6-AA89-2EE839DCDF7AQ35602225-21811037-EA23-4D79-AA7A-648CF499E9BFQ36062461-EB431111-7FB1-4081-BE3D-6CB3E1FD3AFDQ36293751-8FA9E4BE-6637-4042-98CF-FB2DDBC278CEQ36317167-BBAD0E09-5A42-46BA-AAD4-235AB4147089Q36414315-7CBB1A27-A11F-4012-8B78-51F24F63AD37Q36747717-D69257E5-0C4D-4088-8C3D-CEB62C306A30Q36804576-78D63C02-A2EC-48F3-84C8-8A8B39E5B44CQ36820009-E58A16DF-55BB-455D-9300-CC0C4FAD2E10Q37318448-95238EF4-DEB3-4541-9071-CA976163BE73Q37369778-CC55D16A-76E6-44B7-919F-100418D31BF7Q37467403-EB47B9B8-1B10-4B3C-9A17-DACD644BE639Q37955947-1BC4DF6E-5E09-4058-9361-059A47FBFD43Q37987926-8AB7244A-B0E6-45A7-BDFC-732D4955734DQ38025394-2C31EF67-F2ED-49F3-B55C-BDC7A42701B5Q38064834-71C54F73-47A8-49C6-A24E-3D57F3B58BECQ38925477-16C49ADC-076A-4CD4-9663-AC15CA5B6335Q38964212-5EF46AAA-2D9F-49C2-A1FC-0DDE02A4B37EQ39197793-13FDF428-8EB4-4E94-806F-1D084B65182FQ39536459-FFF5FCBB-D97E-4C29-824A-3903BF66129DQ40066270-D402FCB6-ACC1-4741-82E6-10F1874CD9CBQ41117606-D647B535-F3E4-47DA-AE20-E83520BAB53EQ42005599-FE2F7F5B-FFED-467A-9EEC-D7967C8AEFA5Q42695727-491205B7-77AF-42D4-AACA-0CA45EAC0054Q42947231-A4D80F2A-5827-47F2-99BF-4FE11F038E46Q45324801-6C8EC3E9-53C6-4254-B8C0-262705A74978Q45363346-54F52D28-5D53-4B37-A082-618E130D14D8
P2860
Herpes simplex virus ICP27 increases translation of a subset of viral late mRNAs.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Herpes simplex virus ICP27 increases translation of a subset of viral late mRNAs.
@ast
Herpes simplex virus ICP27 increases translation of a subset of viral late mRNAs.
@en
type
label
Herpes simplex virus ICP27 increases translation of a subset of viral late mRNAs.
@ast
Herpes simplex virus ICP27 increases translation of a subset of viral late mRNAs.
@en
prefLabel
Herpes simplex virus ICP27 increases translation of a subset of viral late mRNAs.
@ast
Herpes simplex virus ICP27 increases translation of a subset of viral late mRNAs.
@en
P2860
P356
P1433
P1476
Herpes simplex virus ICP27 increases translation of a subset of viral late mRNAs.
@en
P2093
David M Knipe
Errin C Fontaine-Rodriguez
P2860
P304
P356
10.1128/JVI.02395-07
P407
P577
2008-01-23T00:00:00Z